TY  - JOUR
AU  - Đurašinović, Tatjana
AU  - Lopandić, Zorana
AU  - Protić-Rosić, Isidora
AU  - Nešić, Andrijana
AU  - Trbojević-Ivić, Jovana
AU  - Jappe, Uta
AU  - Gavrović-Jankulović, Marija
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6338
AB  - Banana allergy is often associated with the pollen and latex allergies, which led us to the  hypothesis that some yet unidentified banana allergen could provide a basis of the latex-pollen-fruit syndrome. S-adenosyl-L-homocysteine hydrolase (SAHH) was recently identified in the literature as a novel plant allergen. This study aimed to assess the allergenic potential of the naturally occurring banana SAHH (nSAHH) and its recombinant homolog produced in E. coli (rSAHH). nSAHH showed IgE reactivity with a serum pool of twelve banana-allergic persons,
while rSAHH displayed IgE reactivity in ten out of the twelve tested patients. Five linear B-cell epitopes were identified on the rSAHH surface, exhibiting ≥ 90 % sequence homology with relevant plant SAHH allergens. Our findings have elucidated SAHH as a novel plant panallergen, underlying the cross-reactivity between plant derived food and respiratory allergens, confirming our initial hypothesis.
PB  - Elsevier
T2  - Food Chemistry
T1  - Identification of S-adenosyl-L-homocysteine hydrolase from banana fruit as a novel plant panallergen
VL  - 437
SP  - 137782
DO  - 10.1016/j.foodchem.2023.137782
ER  - 

@article{
author = "Đurašinović, Tatjana and Lopandić, Zorana and Protić-Rosić, Isidora and Nešić, Andrijana and Trbojević-Ivić, Jovana and Jappe, Uta and Gavrović-Jankulović, Marija",
year = "2024",
abstract = "Banana allergy is often associated with the pollen and latex allergies, which led us to the  hypothesis that some yet unidentified banana allergen could provide a basis of the latex-pollen-fruit syndrome. S-adenosyl-L-homocysteine hydrolase (SAHH) was recently identified in the literature as a novel plant allergen. This study aimed to assess the allergenic potential of the naturally occurring banana SAHH (nSAHH) and its recombinant homolog produced in E. coli (rSAHH). nSAHH showed IgE reactivity with a serum pool of twelve banana-allergic persons,
while rSAHH displayed IgE reactivity in ten out of the twelve tested patients. Five linear B-cell epitopes were identified on the rSAHH surface, exhibiting ≥ 90 % sequence homology with relevant plant SAHH allergens. Our findings have elucidated SAHH as a novel plant panallergen, underlying the cross-reactivity between plant derived food and respiratory allergens, confirming our initial hypothesis.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Identification of S-adenosyl-L-homocysteine hydrolase from banana fruit as a novel plant panallergen",
volume = "437",
pages = "137782",
doi = "10.1016/j.foodchem.2023.137782"
}

Đurašinović, T., Lopandić, Z., Protić-Rosić, I., Nešić, A., Trbojević-Ivić, J., Jappe, U.,& Gavrović-Jankulović, M.. (2024). Identification of S-adenosyl-L-homocysteine hydrolase from banana fruit as a novel plant panallergen. in Food Chemistry
Elsevier., 437, 137782.
https://doi.org/10.1016/j.foodchem.2023.137782

Đurašinović T, Lopandić Z, Protić-Rosić I, Nešić A, Trbojević-Ivić J, Jappe U, Gavrović-Jankulović M. Identification of S-adenosyl-L-homocysteine hydrolase from banana fruit as a novel plant panallergen. in Food Chemistry. 2024;437:137782.
doi:10.1016/j.foodchem.2023.137782 .

Đurašinović, Tatjana, Lopandić, Zorana, Protić-Rosić, Isidora, Nešić, Andrijana, Trbojević-Ivić, Jovana, Jappe, Uta, Gavrović-Jankulović, Marija, "Identification of S-adenosyl-L-homocysteine hydrolase from banana fruit as a novel plant panallergen" in Food Chemistry, 437 (2024):137782,
https://doi.org/10.1016/j.foodchem.2023.137782 . .

TY  - CHAP
AU  - Trbojević-Ivić, Jovana
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6339
AB  - Ovalbumin (OVA) is a multi-faceted protein with an immense significance in the human nutrition and food industry. As the most abundant protein of the egg white it contributes to the overall nutritional quality and functional properties of eggs. Proteolytic digestion of OVA yields bioactive peptides (OVA-BAPs) as highly regarded nutraceuticals with various health-promoting and disease-preventing benefits. The aim of this chapter is to present state-of-the-art in the research of OVA-BAPs. Based on the complexity of the chosen subject and the analysis of literature data, chapter is thematically divided into four sections. The first section will present trends and forecasts in the global BAP market, identifying key market segments and stakeholders and addressing the main challenges in production, application and distribution of BAPs. The second section will review current methodologies for production of food-derived BAPs, highlighting enzyme hydrolysis as the most comprehensive method. The third section represents a core unit of this chapter in which a detailed overview of OVA-BAP will be given. OVA-BAP bioactivity is the result of a complex interplay between their structural, biochemical, and pharmacokinetic properties, but it is also greatly affected by the method of OVA processing and OVA-BAP extraction. Effect of all these critical factors will be examined in detail. In the final section advances in production, functional characterization and applications of OVA-BAPs will be presented. Immobilization is the most comprehensive strategy for stabilization and activation of industrial enzymes. Efficiency of immobilized proteases in OVA-BAP production will be elucidated in this section, particularly referring to nanoimmobilized proteases. Artificial intelligence and machine learning are becoming prominent analytical methods in the screening of nutraceuticals and design of functional food. Their incorporation within the existing methodology for functional characterization of OVA-BAP will be elucidated. Bioavailability is the crucial factor affecting the intended health benefit of nutraceuticals. It is strongly affected by pharmacokinetics of the nutraceutical. Therefore, the final part of this chapter will highlight the importance of nanobiotechnology to improve bioavailability and thus bioactivity of OVA-BAPs.
PB  - Nova Science Publishers, Inc.
T2  - Advances in Health and Disease
T1  - Ovalbumin as a Source of Bioactive Peptides
VL  - 74
SP  - 1
EP  - 42
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6339
ER  - 

@inbook{
author = "Trbojević-Ivić, Jovana",
year = "2023",
abstract = "Ovalbumin (OVA) is a multi-faceted protein with an immense significance in the human nutrition and food industry. As the most abundant protein of the egg white it contributes to the overall nutritional quality and functional properties of eggs. Proteolytic digestion of OVA yields bioactive peptides (OVA-BAPs) as highly regarded nutraceuticals with various health-promoting and disease-preventing benefits. The aim of this chapter is to present state-of-the-art in the research of OVA-BAPs. Based on the complexity of the chosen subject and the analysis of literature data, chapter is thematically divided into four sections. The first section will present trends and forecasts in the global BAP market, identifying key market segments and stakeholders and addressing the main challenges in production, application and distribution of BAPs. The second section will review current methodologies for production of food-derived BAPs, highlighting enzyme hydrolysis as the most comprehensive method. The third section represents a core unit of this chapter in which a detailed overview of OVA-BAP will be given. OVA-BAP bioactivity is the result of a complex interplay between their structural, biochemical, and pharmacokinetic properties, but it is also greatly affected by the method of OVA processing and OVA-BAP extraction. Effect of all these critical factors will be examined in detail. In the final section advances in production, functional characterization and applications of OVA-BAPs will be presented. Immobilization is the most comprehensive strategy for stabilization and activation of industrial enzymes. Efficiency of immobilized proteases in OVA-BAP production will be elucidated in this section, particularly referring to nanoimmobilized proteases. Artificial intelligence and machine learning are becoming prominent analytical methods in the screening of nutraceuticals and design of functional food. Their incorporation within the existing methodology for functional characterization of OVA-BAP will be elucidated. Bioavailability is the crucial factor affecting the intended health benefit of nutraceuticals. It is strongly affected by pharmacokinetics of the nutraceutical. Therefore, the final part of this chapter will highlight the importance of nanobiotechnology to improve bioavailability and thus bioactivity of OVA-BAPs.",
publisher = "Nova Science Publishers, Inc.",
journal = "Advances in Health and Disease",
booktitle = "Ovalbumin as a Source of Bioactive Peptides",
volume = "74",
pages = "1-42",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6339"
}

Trbojević-Ivić, J.. (2023). Ovalbumin as a Source of Bioactive Peptides. in Advances in Health and Disease
Nova Science Publishers, Inc.., 74, 1-42.
https://hdl.handle.net/21.15107/rcub_cherry_6339

Trbojević-Ivić J. Ovalbumin as a Source of Bioactive Peptides. in Advances in Health and Disease. 2023;74:1-42.
https://hdl.handle.net/21.15107/rcub_cherry_6339 .

Trbojević-Ivić, Jovana, "Ovalbumin as a Source of Bioactive Peptides" in Advances in Health and Disease, 74 (2023):1-42,
https://hdl.handle.net/21.15107/rcub_cherry_6339 .

TY  - CHAP
AU  - Lopandić, Zorana
AU  - Protić-Rosić, Isidora
AU  - Trbojević-Ivić, Jovana
AU  - Zlatanova, Milena
AU  - Gavrović-Jankulović, Marija
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6340
AB  - Ovalbumin (OVA) is the most abundant egg white protein. It is a globular, acidic phosphorylated glycoprotein of the serpin family with a molecular weight of 45 kDa. OVA is rich in essential amino acids and upon proteolytic digestion yields bioactive peptides (BAPs), recognized nutraceuticals with hypotensive, antimicrobial, antioxidant, and anticancer properties that contribute to the overall nutritional and health benefits of eggs. OVA is a common choice in the food, biomedical, and pharmaceutical industries due to its useful properties during food processing, capacity to form biocompatible gels, and special properties as an effective transporter for a variety of nutraceuticals and pharmaceuticals. Cellular agriculture is an innovative interdisciplinary approach that bypasses conventional animal husbandry in the production of animal proteins. OVA expressed in Trichoderma reesei (T. reesei) most closely mimics the structural and functional properties of its natural homolog and is therefore considered a sustainable alternative to chicken egg white protein powder.
Egg allergy poses serious concerns for food safety and an important socioeconomic burden to the food sector and public health. OVA has been extensively studied as an important egg allergen in mice and in vitro experimental models, providing fundamental insights into the molecular mechanisms of allergy and identifying new therapeutic targets. This chapter focuses on providing a comprehensive overview of the state-of-the-art of OVA in human nutrition and the food industry. After presenting the structure underlying the functional properties of OVA, we provide a critical perspective on cellular agriculture as a non-poultry production of OVA. Additionally, the detailed nutritional and biotechnological significance of OVA is elaborated. The final part of this chapter provides a comprehensive insight into OVA as a model antigen and food allergen from a food safety perspective.
PB  - Nova Science Publishers, Inc.
T2  - Advances in Health and Disease
T1  - Ovalbumin - Two Sides of the Same Coin
VL  - 74
SP  - 43
EP  - 100
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6340
ER  - 

@inbook{
author = "Lopandić, Zorana and Protić-Rosić, Isidora and Trbojević-Ivić, Jovana and Zlatanova, Milena and Gavrović-Jankulović, Marija",
year = "2023",
abstract = "Ovalbumin (OVA) is the most abundant egg white protein. It is a globular, acidic phosphorylated glycoprotein of the serpin family with a molecular weight of 45 kDa. OVA is rich in essential amino acids and upon proteolytic digestion yields bioactive peptides (BAPs), recognized nutraceuticals with hypotensive, antimicrobial, antioxidant, and anticancer properties that contribute to the overall nutritional and health benefits of eggs. OVA is a common choice in the food, biomedical, and pharmaceutical industries due to its useful properties during food processing, capacity to form biocompatible gels, and special properties as an effective transporter for a variety of nutraceuticals and pharmaceuticals. Cellular agriculture is an innovative interdisciplinary approach that bypasses conventional animal husbandry in the production of animal proteins. OVA expressed in Trichoderma reesei (T. reesei) most closely mimics the structural and functional properties of its natural homolog and is therefore considered a sustainable alternative to chicken egg white protein powder.
Egg allergy poses serious concerns for food safety and an important socioeconomic burden to the food sector and public health. OVA has been extensively studied as an important egg allergen in mice and in vitro experimental models, providing fundamental insights into the molecular mechanisms of allergy and identifying new therapeutic targets. This chapter focuses on providing a comprehensive overview of the state-of-the-art of OVA in human nutrition and the food industry. After presenting the structure underlying the functional properties of OVA, we provide a critical perspective on cellular agriculture as a non-poultry production of OVA. Additionally, the detailed nutritional and biotechnological significance of OVA is elaborated. The final part of this chapter provides a comprehensive insight into OVA as a model antigen and food allergen from a food safety perspective.",
publisher = "Nova Science Publishers, Inc.",
journal = "Advances in Health and Disease",
booktitle = "Ovalbumin - Two Sides of the Same Coin",
volume = "74",
pages = "43-100",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6340"
}

Lopandić, Z., Protić-Rosić, I., Trbojević-Ivić, J., Zlatanova, M.,& Gavrović-Jankulović, M.. (2023). Ovalbumin - Two Sides of the Same Coin. in Advances in Health and Disease
Nova Science Publishers, Inc.., 74, 43-100.
https://hdl.handle.net/21.15107/rcub_cherry_6340

Lopandić Z, Protić-Rosić I, Trbojević-Ivić J, Zlatanova M, Gavrović-Jankulović M. Ovalbumin - Two Sides of the Same Coin. in Advances in Health and Disease. 2023;74:43-100.
https://hdl.handle.net/21.15107/rcub_cherry_6340 .

Lopandić, Zorana, Protić-Rosić, Isidora, Trbojević-Ivić, Jovana, Zlatanova, Milena, Gavrović-Jankulović, Marija, "Ovalbumin - Two Sides of the Same Coin" in Advances in Health and Disease, 74 (2023):43-100,
https://hdl.handle.net/21.15107/rcub_cherry_6340 .

TY  - CHAP
AU  - Trbojević-Ivić, Jovana
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6341
AB  - Bioethanol from inedible cellulose-rich biomass is the most promising candidate to replace fast depleting,
environmentally polluting fossil fuels. Hydrolysis of cellulose to glucose is the crucial step in its
biotransformation to bioethanol. Enzymatic hydrolysis is favored over acid hydrolysis, as enzymes are
eco-friendly biocatalysts with high substrate specificity and superior catalytic efficiency in mild reaction
conditions. Complete hydrolysis of cellulose is achieved by cellulase. Higher cellulase production
yield, stability, and catalytic efficiency are the main attentive points for the successful implementation
in industrial production of bioethanol. This chapter will highlight general characteristics of microbial
cellulases and their role in the bioconversion of cellulose to biofuels, economic sustainability of cellulosebased
biofuels, and the latest innovations in cellulase immobilization as the most comprehensive strategy
for improvement of enzyme stability, activity, and reusability for cost-effective large-scale application.
PB  - IGI Global
T2  - Biomass and Bioenergy Solutions for Climate Change Mitigation and Sustainability
T1  - Microbial Cellulase in the Production of Second Generation Biofuels: State-of-the-Art and Beyond
SP  - 233
EP  - 257
DO  - 10.4018/978-1-6684-5269-1
ER  - 

@inbook{
author = "Trbojević-Ivić, Jovana",
year = "2022",
abstract = "Bioethanol from inedible cellulose-rich biomass is the most promising candidate to replace fast depleting,
environmentally polluting fossil fuels. Hydrolysis of cellulose to glucose is the crucial step in its
biotransformation to bioethanol. Enzymatic hydrolysis is favored over acid hydrolysis, as enzymes are
eco-friendly biocatalysts with high substrate specificity and superior catalytic efficiency in mild reaction
conditions. Complete hydrolysis of cellulose is achieved by cellulase. Higher cellulase production
yield, stability, and catalytic efficiency are the main attentive points for the successful implementation
in industrial production of bioethanol. This chapter will highlight general characteristics of microbial
cellulases and their role in the bioconversion of cellulose to biofuels, economic sustainability of cellulosebased
biofuels, and the latest innovations in cellulase immobilization as the most comprehensive strategy
for improvement of enzyme stability, activity, and reusability for cost-effective large-scale application.",
publisher = "IGI Global",
journal = "Biomass and Bioenergy Solutions for Climate Change Mitigation and Sustainability",
booktitle = "Microbial Cellulase in the Production of Second Generation Biofuels: State-of-the-Art and Beyond",
pages = "233-257",
doi = "10.4018/978-1-6684-5269-1"
}

Trbojević-Ivić, J.. (2022). Microbial Cellulase in the Production of Second Generation Biofuels: State-of-the-Art and Beyond. in Biomass and Bioenergy Solutions for Climate Change Mitigation and Sustainability
IGI Global., 233-257.
https://doi.org/10.4018/978-1-6684-5269-1

Trbojević-Ivić J. Microbial Cellulase in the Production of Second Generation Biofuels: State-of-the-Art and Beyond. in Biomass and Bioenergy Solutions for Climate Change Mitigation and Sustainability. 2022;:233-257.
doi:10.4018/978-1-6684-5269-1 .

Trbojević-Ivić, Jovana, "Microbial Cellulase in the Production of Second Generation Biofuels: State-of-the-Art and Beyond" in Biomass and Bioenergy Solutions for Climate Change Mitigation and Sustainability (2022):233-257,
https://doi.org/10.4018/978-1-6684-5269-1 . .

TY  - CONF
AU  - Đurašinović, Tatjana
AU  - Bazović, Vedrana
AU  - Trbojević-Ivić, Jovana
AU  - Nešić, Andrijana N.
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5165
PB  - Belgrade : Faculty of Chemistry
C3  - Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia
T1  - Screening of potential inhibitors of recombinant S-adenosyl-L-homocysteine hydrolase from banana
SP  - 50
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5165
ER  - 

@conference{
author = "Đurašinović, Tatjana and Bazović, Vedrana and Trbojević-Ivić, Jovana and Nešić, Andrijana N. and Gavrović-Jankulović, Marija",
year = "2021",
publisher = "Belgrade : Faculty of Chemistry",
journal = "Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia",
title = "Screening of potential inhibitors of recombinant S-adenosyl-L-homocysteine hydrolase from banana",
pages = "50",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5165"
}

Đurašinović, T., Bazović, V., Trbojević-Ivić, J., Nešić, A. N.,& Gavrović-Jankulović, M.. (2021). Screening of potential inhibitors of recombinant S-adenosyl-L-homocysteine hydrolase from banana. in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia
Belgrade : Faculty of Chemistry., 50.
https://hdl.handle.net/21.15107/rcub_cherry_5165

Đurašinović T, Bazović V, Trbojević-Ivić J, Nešić AN, Gavrović-Jankulović M. Screening of potential inhibitors of recombinant S-adenosyl-L-homocysteine hydrolase from banana. in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia. 2021;:50.
https://hdl.handle.net/21.15107/rcub_cherry_5165 .

Đurašinović, Tatjana, Bazović, Vedrana, Trbojević-Ivić, Jovana, Nešić, Andrijana N., Gavrović-Jankulović, Marija, "Screening of potential inhibitors of recombinant S-adenosyl-L-homocysteine hydrolase from banana" in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia (2021):50,
https://hdl.handle.net/21.15107/rcub_cherry_5165 .

TY  - CONF
AU  - Pantović, Jelena
AU  - Trbojević-Ivić, Jovana
AU  - Nešić, Andrijana N.
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5166
PB  - Belgrade : Faculty of Chemistry
C3  - Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia
T1  - Expression, purification and characterization of recombinant L-phenylalanine dehydrogenase
SP  - 119
EP  - 120
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5166
ER  - 

@conference{
author = "Pantović, Jelena and Trbojević-Ivić, Jovana and Nešić, Andrijana N. and Gavrović-Jankulović, Marija",
year = "2021",
publisher = "Belgrade : Faculty of Chemistry",
journal = "Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia",
title = "Expression, purification and characterization of recombinant L-phenylalanine dehydrogenase",
pages = "119-120",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5166"
}

Pantović, J., Trbojević-Ivić, J., Nešić, A. N.,& Gavrović-Jankulović, M.. (2021). Expression, purification and characterization of recombinant L-phenylalanine dehydrogenase. in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia
Belgrade : Faculty of Chemistry., 119-120.
https://hdl.handle.net/21.15107/rcub_cherry_5166

Pantović J, Trbojević-Ivić J, Nešić AN, Gavrović-Jankulović M. Expression, purification and characterization of recombinant L-phenylalanine dehydrogenase. in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia. 2021;:119-120.
https://hdl.handle.net/21.15107/rcub_cherry_5166 .

Pantović, Jelena, Trbojević-Ivić, Jovana, Nešić, Andrijana N., Gavrović-Jankulović, Marija, "Expression, purification and characterization of recombinant L-phenylalanine dehydrogenase" in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia (2021):119-120,
https://hdl.handle.net/21.15107/rcub_cherry_5166 .

TY  - CONF
AU  - Zlatanova, Milena
AU  - Nešić, Andrijana N.
AU  - Trbojević-Ivić, Jovana
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5167
PB  - Belgrade : Faculty of Chemistry
C3  - Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia
T1  - Small molecules attenuate activation of the NF-kB signaling in epithelial cells by Act d 1 kiwifruit allergen
SP  - 186
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5167
ER  - 

@conference{
author = "Zlatanova, Milena and Nešić, Andrijana N. and Trbojević-Ivić, Jovana and Gavrović-Jankulović, Marija",
year = "2021",
publisher = "Belgrade : Faculty of Chemistry",
journal = "Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia",
title = "Small molecules attenuate activation of the NF-kB signaling in epithelial cells by Act d 1 kiwifruit allergen",
pages = "186",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5167"
}

Zlatanova, M., Nešić, A. N., Trbojević-Ivić, J.,& Gavrović-Jankulović, M.. (2021). Small molecules attenuate activation of the NF-kB signaling in epithelial cells by Act d 1 kiwifruit allergen. in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia
Belgrade : Faculty of Chemistry., 186.
https://hdl.handle.net/21.15107/rcub_cherry_5167

Zlatanova M, Nešić AN, Trbojević-Ivić J, Gavrović-Jankulović M. Small molecules attenuate activation of the NF-kB signaling in epithelial cells by Act d 1 kiwifruit allergen. in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia. 2021;:186.
https://hdl.handle.net/21.15107/rcub_cherry_5167 .

Zlatanova, Milena, Nešić, Andrijana N., Trbojević-Ivić, Jovana, Gavrović-Jankulović, Marija, "Small molecules attenuate activation of the NF-kB signaling in epithelial cells by Act d 1 kiwifruit allergen" in Proceedings of the Tenth Conference of the Serbian Biochemical Society, Biochemical Insight into Molecular Mechanicms, Serbia (2021):186,
https://hdl.handle.net/21.15107/rcub_cherry_5167 .

TY  - THES
AU  - Trbojević-Ivić, Jovana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7117
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:20779/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=51817999
UR  - http://nardus.mpn.gov.rs/123456789/11808
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3911
AB  - U ovoj doktorskoj disertaciji je ispitan potencijal HAP za imobilizaciju industrijski značajnih enzima na primeru 4 lipaze i 4 glikozidaze različitog porekla, strukture i supstratne specifičnosti. Od testiranih enzima za HAP se najefikasnije vezuju lipaza iz Candida rugosa (CRL) i β-galaktozidaza (laktaza) iz Aspergillus oryzae (AOL). Oba enzima se imobilizuju na HAP jednostavnom, brzom i efikasnom fizičkom adsorpcijom po mehanizmu metal-koordinatne veze. Kombinovanjem bioinformatičkog pristupa i molekulskog modelovanja za oba enzima su identifikovani i opisani površinski HAP-vezujući motivi.Imobilizacija na HAP je uzrokovala promenu supstratne specifičnosti CRL ka supstratima sa kraćim alkil-nizom i drastično povećanje stabilnosti i aktivnosti enzima u metanolu. Ove karakteristike imobilizata CRL na HAP (CRL-HAP) su prvi put u literaturi primenjene za sintezu metil-acetata, estra sa mirisom jabuke, koga slobodna CRL sintetiše u zanemarljivom prinosu. Pažljivim odabirom rastvarača i supstrata je, takođe po prvi put pokazano kako ovaj popularni i jeftin enzim, u slobodnom ili imobilizovanom obliku, može da se primeni i za efikasnu sintezu kapsinoida direktnom esterifikacijom vanilil-alkohola (VA) i masnih kiselina (MK) i transesterifikacijom kokosovog ulja.Efikasnost imobilizovanog preparata AOL (AOL-HAP) je ispitana u sintezi bioaktivnih supstanci, vanilil-galaktozida (VG) i galakto-oligosaharida (GOS). Po efikasnosti u sintezi ovih proizvoda preparat AOL-HAP se našao u rangu sa kovalentno imobilizovanim preparatima AOL. Jedna ista šarža AOL-HAP može se iskoristiti u 10 uzastopnih reakcionih ciklusa sinteze VG, odnosno GOS, sa poluživotom od 15 h.
AB  - Potential of hydroxyapatite (HAP) as immobilization carrier for industrially important enzymes was examined in a study, comprising of 4 lipases and 4 glycosidases of different origin, structure and substrate specificity. Lipase from Candida rugosa (CRL) and β-galactosidase (lactase) from Aspergillus oryzae (AOL) exhibited the most efficient binding to HAP. Both of the enzymes were immobilized on HAP by simple, fast and efficient physical adsorption through formation of metal-coordinative bond. Furthermore, by the combining of bioinformatic approach and molecular modeling, HAP-speciffic superficial motif on both selected enzymes was identified and described for the first time in the literature.Immobilization on HAP has shifted substrate specificity of CRL towards shorter alkyl-chains, coupled with significant increase in stability and activity of CRL in methanol. These characteristics of immobilized Candida rugosa lipase preparation (CRL-HAP) were sucessfully implemented in synthesis of methyl-acetate, an apple flavour for the first time in the literature. Free CRL synthesized methyl-acetate in very low yield, because of methanol-induced inactivation. By a meticulous selection of organic solvent and susbtrates, it was shown also for the first time that this popular and cost-effective microbial lipase, free or immobilized on HAP, can be used for efficient synthesis of capsinoids in two distinctive reactions: direct esterification of vanillyl-alcohol (VA) with free fatty acids and transesterification of coconut oil.Efficiency of AOL immobilized on HAP (AOL-HAP), was evaluated in synthesis of bioactive compounds: vanillyl-galactoside (VG) and galacto-oligosaccharide (GOS) probiotics. Efficiency of AOL-HAP in synthesis of these compounds was in a good correlation with the procedures in which covalently immobilized AOL was employed. Immobilized AOL preparation can be used in maximum 10 consecutive reaction cycles during VG and GOS synthesis, with the half-life of 15 hours.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj
UR  - https://hdl.handle.net/21.15107/rcub_nardus_11808
ER  - 

@phdthesis{
author = "Trbojević-Ivić, Jovana",
year = "2019",
abstract = "U ovoj doktorskoj disertaciji je ispitan potencijal HAP za imobilizaciju industrijski značajnih enzima na primeru 4 lipaze i 4 glikozidaze različitog porekla, strukture i supstratne specifičnosti. Od testiranih enzima za HAP se najefikasnije vezuju lipaza iz Candida rugosa (CRL) i β-galaktozidaza (laktaza) iz Aspergillus oryzae (AOL). Oba enzima se imobilizuju na HAP jednostavnom, brzom i efikasnom fizičkom adsorpcijom po mehanizmu metal-koordinatne veze. Kombinovanjem bioinformatičkog pristupa i molekulskog modelovanja za oba enzima su identifikovani i opisani površinski HAP-vezujući motivi.Imobilizacija na HAP je uzrokovala promenu supstratne specifičnosti CRL ka supstratima sa kraćim alkil-nizom i drastično povećanje stabilnosti i aktivnosti enzima u metanolu. Ove karakteristike imobilizata CRL na HAP (CRL-HAP) su prvi put u literaturi primenjene za sintezu metil-acetata, estra sa mirisom jabuke, koga slobodna CRL sintetiše u zanemarljivom prinosu. Pažljivim odabirom rastvarača i supstrata je, takođe po prvi put pokazano kako ovaj popularni i jeftin enzim, u slobodnom ili imobilizovanom obliku, može da se primeni i za efikasnu sintezu kapsinoida direktnom esterifikacijom vanilil-alkohola (VA) i masnih kiselina (MK) i transesterifikacijom kokosovog ulja.Efikasnost imobilizovanog preparata AOL (AOL-HAP) je ispitana u sintezi bioaktivnih supstanci, vanilil-galaktozida (VG) i galakto-oligosaharida (GOS). Po efikasnosti u sintezi ovih proizvoda preparat AOL-HAP se našao u rangu sa kovalentno imobilizovanim preparatima AOL. Jedna ista šarža AOL-HAP može se iskoristiti u 10 uzastopnih reakcionih ciklusa sinteze VG, odnosno GOS, sa poluživotom od 15 h., Potential of hydroxyapatite (HAP) as immobilization carrier for industrially important enzymes was examined in a study, comprising of 4 lipases and 4 glycosidases of different origin, structure and substrate specificity. Lipase from Candida rugosa (CRL) and β-galactosidase (lactase) from Aspergillus oryzae (AOL) exhibited the most efficient binding to HAP. Both of the enzymes were immobilized on HAP by simple, fast and efficient physical adsorption through formation of metal-coordinative bond. Furthermore, by the combining of bioinformatic approach and molecular modeling, HAP-speciffic superficial motif on both selected enzymes was identified and described for the first time in the literature.Immobilization on HAP has shifted substrate specificity of CRL towards shorter alkyl-chains, coupled with significant increase in stability and activity of CRL in methanol. These characteristics of immobilized Candida rugosa lipase preparation (CRL-HAP) were sucessfully implemented in synthesis of methyl-acetate, an apple flavour for the first time in the literature. Free CRL synthesized methyl-acetate in very low yield, because of methanol-induced inactivation. By a meticulous selection of organic solvent and susbtrates, it was shown also for the first time that this popular and cost-effective microbial lipase, free or immobilized on HAP, can be used for efficient synthesis of capsinoids in two distinctive reactions: direct esterification of vanillyl-alcohol (VA) with free fatty acids and transesterification of coconut oil.Efficiency of AOL immobilized on HAP (AOL-HAP), was evaluated in synthesis of bioactive compounds: vanillyl-galactoside (VG) and galacto-oligosaccharide (GOS) probiotics. Efficiency of AOL-HAP in synthesis of these compounds was in a good correlation with the procedures in which covalently immobilized AOL was employed. Immobilized AOL preparation can be used in maximum 10 consecutive reaction cycles during VG and GOS synthesis, with the half-life of 15 hours.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj",
url = "https://hdl.handle.net/21.15107/rcub_nardus_11808"
}

Trbojević-Ivić, J.. (2019). Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_11808

Trbojević-Ivić J. Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_11808 .

Trbojević-Ivić, Jovana, "Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_11808 .

TY  - CHAP
AU  - Trbojević-Ivić, Jovana
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5287
AB  - Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3) are ubiquitous enzymes that catalyze numerous reactions such as hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis. Broad substrate specificity and high stereo-, regio- and chemoselectivity make lipases attractive catalysts in a wide range of industrial applications. Lipases are used in the food, pharmaceutical, agrochemical, oleochemical, cosmetic and detergent industries. In spite of their tremendous potential, commercial application of lipases in industry is still limited due to their high cost and relatively low stability. This chapter describes the use of enzyme immobilization as an efficient strategy to overcome these drawbacks. Immobilization of lipases enhances properties such as thermostability and activity, facilitates separation of products and provides more flexibility with enzyme/substrate contact by using various reactor configurations.
Numerous methods for lipase immobilization are available. Baring in mind the scope of this book, the most common methods, including adsorption, cross-linking, adsorption followed by cross-linking, multipoint covalent attachment and physical entrapment will be discussed in detail. Advantages and disadvantages of commonly used immobilization methods and the design and selection of immobilization strategies are analyzed as well. Particular emphasis is placed on the most recent advances in the development of an efficient lipase immobilization system that would enable us to achieve the desired benefits. This chapter will also highlight benefits of immobilization in lipase stabilization, with respect to other employed methods such as chemical modification and recombinant DNA technology.
PB  - Nova Science Publishers, Inc.
T2  - Lipases: Structure, Functions and Role in Health and Disease
T1  - Immobilization and Stabilization of Microbial Lipases
SP  - 55
EP  - 105
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5287
ER  - 

@inbook{
author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Milosavić, Nenad",
year = "2018",
abstract = "Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3) are ubiquitous enzymes that catalyze numerous reactions such as hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis. Broad substrate specificity and high stereo-, regio- and chemoselectivity make lipases attractive catalysts in a wide range of industrial applications. Lipases are used in the food, pharmaceutical, agrochemical, oleochemical, cosmetic and detergent industries. In spite of their tremendous potential, commercial application of lipases in industry is still limited due to their high cost and relatively low stability. This chapter describes the use of enzyme immobilization as an efficient strategy to overcome these drawbacks. Immobilization of lipases enhances properties such as thermostability and activity, facilitates separation of products and provides more flexibility with enzyme/substrate contact by using various reactor configurations.
Numerous methods for lipase immobilization are available. Baring in mind the scope of this book, the most common methods, including adsorption, cross-linking, adsorption followed by cross-linking, multipoint covalent attachment and physical entrapment will be discussed in detail. Advantages and disadvantages of commonly used immobilization methods and the design and selection of immobilization strategies are analyzed as well. Particular emphasis is placed on the most recent advances in the development of an efficient lipase immobilization system that would enable us to achieve the desired benefits. This chapter will also highlight benefits of immobilization in lipase stabilization, with respect to other employed methods such as chemical modification and recombinant DNA technology.",
publisher = "Nova Science Publishers, Inc.",
journal = "Lipases: Structure, Functions and Role in Health and Disease",
booktitle = "Immobilization and Stabilization of Microbial Lipases",
pages = "55-105",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5287"
}

Trbojević-Ivić, J., Veličković, D., Dimitrijević, A.,& Milosavić, N.. (2018). Immobilization and Stabilization of Microbial Lipases. in Lipases: Structure, Functions and Role in Health and Disease
Nova Science Publishers, Inc.., 55-105.
https://hdl.handle.net/21.15107/rcub_cherry_5287

Trbojević-Ivić J, Veličković D, Dimitrijević A, Milosavić N. Immobilization and Stabilization of Microbial Lipases. in Lipases: Structure, Functions and Role in Health and Disease. 2018;:55-105.
https://hdl.handle.net/21.15107/rcub_cherry_5287 .

Trbojević-Ivić, Jovana, Veličković, Dušan, Dimitrijević, Aleksandra, Milosavić, Nenad, "Immobilization and Stabilization of Microbial Lipases" in Lipases: Structure, Functions and Role in Health and Disease (2018):55-105,
https://hdl.handle.net/21.15107/rcub_cherry_5287 .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Milosavić, Nenad
AU  - Dimitrijević, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Kolarski, Dušan
AU  - Veličković, Dušan
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2338
AB  - A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases
VL  - 218
SP  - 505
EP  - 508
DO  - 10.1016/j.foodchem.2016.09.049
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Milosavić, Nenad and Dimitrijević, Aleksandra and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Kolarski, Dušan and Veličković, Dušan",
year = "2017",
abstract = "A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases",
volume = "218",
pages = "505-508",
doi = "10.1016/j.foodchem.2016.09.049"
}

Trbojević-Ivić, J., Milosavić, N., Dimitrijević, A., Gavrović-Jankulović, M., Bezbradica, D., Kolarski, D.,& Veličković, D.. (2017). Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. in Food Chemistry
Elsevier Sci Ltd, Oxford., 218, 505-508.
https://doi.org/10.1016/j.foodchem.2016.09.049

Trbojević-Ivić J, Milosavić N, Dimitrijević A, Gavrović-Jankulović M, Bezbradica D, Kolarski D, Veličković D. Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. in Food Chemistry. 2017;218:505-508.
doi:10.1016/j.foodchem.2016.09.049 .

Trbojević-Ivić, Jovana, Milosavić, Nenad, Dimitrijević, Aleksandra, Gavrović-Jankulović, Marija, Bezbradica, Dejan, Kolarski, Dušan, Veličković, Dušan, "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases" in Food Chemistry, 218 (2017):505-508,
https://doi.org/10.1016/j.foodchem.2016.09.049 . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Milosavić, Nenad
AU  - Dimitrijević, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Kolarski, Dušan
AU  - Veličković, Dušan
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3102
AB  - A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases
VL  - 218
SP  - 505
EP  - 508
DO  - 10.1016/j.foodchem.2016.09.049
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Milosavić, Nenad and Dimitrijević, Aleksandra and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Kolarski, Dušan and Veličković, Dušan",
year = "2017",
abstract = "A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases",
volume = "218",
pages = "505-508",
doi = "10.1016/j.foodchem.2016.09.049"
}

Trbojević-Ivić, J., Milosavić, N., Dimitrijević, A., Gavrović-Jankulović, M., Bezbradica, D., Kolarski, D.,& Veličković, D.. (2017). Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. in Food Chemistry
Elsevier Sci Ltd, Oxford., 218, 505-508.
https://doi.org/10.1016/j.foodchem.2016.09.049

Trbojević-Ivić J, Milosavić N, Dimitrijević A, Gavrović-Jankulović M, Bezbradica D, Kolarski D, Veličković D. Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. in Food Chemistry. 2017;218:505-508.
doi:10.1016/j.foodchem.2016.09.049 .

Trbojević-Ivić, Jovana, Milosavić, Nenad, Dimitrijević, Aleksandra, Gavrović-Jankulović, Marija, Bezbradica, Dejan, Kolarski, Dušan, Veličković, Dušan, "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases" in Food Chemistry, 218 (2017):505-508,
https://doi.org/10.1016/j.foodchem.2016.09.049 . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
AU  - Pavlović, Marija
AU  - Rogniaux, Helene
AU  - Veličković, Dušan
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1914
AB  - Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's -COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling
VL  - 6
IS  - 41
SP  - 34818
EP  - 34824
DO  - 10.1039/c6ra07521e
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Milosavić, Nenad and Bezbradica, Dejan and Drakulić, Branko J. and Gavrović-Jankulović, Marija and Pavlović, Marija and Rogniaux, Helene and Veličković, Dušan",
year = "2016",
abstract = "Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's -COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling",
volume = "6",
number = "41",
pages = "34818-34824",
doi = "10.1039/c6ra07521e"
}

Trbojević-Ivić, J., Dimitrijević, A., Milosavić, N., Bezbradica, D., Drakulić, B. J., Gavrović-Jankulović, M., Pavlović, M., Rogniaux, H.,& Veličković, D.. (2016). Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(41), 34818-34824.
https://doi.org/10.1039/c6ra07521e

Trbojević-Ivić J, Dimitrijević A, Milosavić N, Bezbradica D, Drakulić BJ, Gavrović-Jankulović M, Pavlović M, Rogniaux H, Veličković D. Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling. in RSC Advances. 2016;6(41):34818-34824.
doi:10.1039/c6ra07521e .

Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, Milosavić, Nenad, Bezbradica, Dejan, Drakulić, Branko J., Gavrović-Jankulović, Marija, Pavlović, Marija, Rogniaux, Helene, Veličković, Dušan, "Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling" in RSC Advances, 6, no. 41 (2016):34818-34824,
https://doi.org/10.1039/c6ra07521e . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bezbradica, Dejan
AU  - Dragacevic, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1943
AB  - BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry
VL  - 96
IS  - 12
SP  - 4281
EP  - 4287
DO  - 10.1002/jsfa.7641
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Bezbradica, Dejan and Dragacevic, Vladimir and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2016",
abstract = "BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry",
volume = "96",
number = "12",
pages = "4281-4287",
doi = "10.1002/jsfa.7641"
}

Trbojević-Ivić, J., Veličković, D., Dimitrijević, A., Bezbradica, D., Dragacevic, V., Gavrović-Jankulović, M.,& Milosavić, N.. (2016). Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Hoboken., 96(12), 4281-4287.
https://doi.org/10.1002/jsfa.7641

Trbojević-Ivić J, Veličković D, Dimitrijević A, Bezbradica D, Dragacevic V, Gavrović-Jankulović M, Milosavić N. Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. in Journal of the Science of Food and Agriculture. 2016;96(12):4281-4287.
doi:10.1002/jsfa.7641 .

Trbojević-Ivić, Jovana, Veličković, Dušan, Dimitrijević, Aleksandra, Bezbradica, Dejan, Dragacevic, Vladimir, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry" in Journal of the Science of Food and Agriculture, 96, no. 12 (2016):4281-4287,
https://doi.org/10.1002/jsfa.7641 . .

TY  - JOUR
AU  - Mihailović, Mladen
AU  - Trbojević-Ivić, Jovana
AU  - Banjanac, Katarina
AU  - Milosavić, Nenad
AU  - Veličković, Dušan
AU  - Carević, Milica
AU  - Bezbradica, Dejan
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2391
AB  - In this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports
VL  - 81
IS  - 12
SP  - 1371
EP  - 1382
DO  - 10.2298/JSC160730099M
ER  - 

@article{
author = "Mihailović, Mladen and Trbojević-Ivić, Jovana and Banjanac, Katarina and Milosavić, Nenad and Veličković, Dušan and Carević, Milica and Bezbradica, Dejan",
year = "2016",
abstract = "In this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports",
volume = "81",
number = "12",
pages = "1371-1382",
doi = "10.2298/JSC160730099M"
}

Mihailović, M., Trbojević-Ivić, J., Banjanac, K., Milosavić, N., Veličković, D., Carević, M.,& Bezbradica, D.. (2016). Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 81(12), 1371-1382.
https://doi.org/10.2298/JSC160730099M

Mihailović M, Trbojević-Ivić J, Banjanac K, Milosavić N, Veličković D, Carević M, Bezbradica D. Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports. in Journal of the Serbian Chemical Society. 2016;81(12):1371-1382.
doi:10.2298/JSC160730099M .

Mihailović, Mladen, Trbojević-Ivić, Jovana, Banjanac, Katarina, Milosavić, Nenad, Veličković, Dušan, Carević, Milica, Bezbradica, Dejan, "Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports" in Journal of the Serbian Chemical Society, 81, no. 12 (2016):1371-1382,
https://doi.org/10.2298/JSC160730099M . .

TY  - CONF
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Kolarski, Dušan
AU  - Veličković, Dušan
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5279
PB  - Belgrade : Serbian Chemical Society
C3  - Fourth Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, November 5, 2016
T1  - Efikasnost Candida rugosa lipaza u sintezi kapsinoida tokom transesterifikacije kokosovog ulja
SP  - 75
EP  - 75
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5279
ER  - 

@conference{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Kolarski, Dušan and Veličković, Dušan",
year = "2016",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Fourth Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, November 5, 2016",
title = "Efikasnost Candida rugosa lipaza u sintezi kapsinoida tokom transesterifikacije kokosovog ulja",
pages = "75-75",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5279"
}

Trbojević-Ivić, J., Dimitrijević, A., Kolarski, D.,& Veličković, D.. (2016). Efikasnost Candida rugosa lipaza u sintezi kapsinoida tokom transesterifikacije kokosovog ulja. in Fourth Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, November 5, 2016
Belgrade : Serbian Chemical Society., 75-75.
https://hdl.handle.net/21.15107/rcub_cherry_5279

Trbojević-Ivić J, Dimitrijević A, Kolarski D, Veličković D. Efikasnost Candida rugosa lipaza u sintezi kapsinoida tokom transesterifikacije kokosovog ulja. in Fourth Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, November 5, 2016. 2016;:75-75.
https://hdl.handle.net/21.15107/rcub_cherry_5279 .

Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, Kolarski, Dušan, Veličković, Dušan, "Efikasnost Candida rugosa lipaza u sintezi kapsinoida tokom transesterifikacije kokosovog ulja" in Fourth Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, November 5, 2016 (2016):75-75,
https://hdl.handle.net/21.15107/rcub_cherry_5279 .

TY  - CONF
AU  - Dragačević, Vladimir
AU  - Trbojević-Ivić, Jovana
AU  - Mutić, Jelena
AU  - Bezbradica, Dejan
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5280
PB  - Belgrade : Serbian Chemical Society
C3  - Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015
T1  - Optimizacija proizvodnje i analitika biodizela dobijenog katalitičkom aktivnošću lipaze B Candidae antarcticae
SP  - 68
EP  - 68
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5280
ER  - 

@conference{
author = "Dragačević, Vladimir and Trbojević-Ivić, Jovana and Mutić, Jelena and Bezbradica, Dejan",
year = "2015",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015",
title = "Optimizacija proizvodnje i analitika biodizela dobijenog katalitičkom aktivnošću lipaze B Candidae antarcticae",
pages = "68-68",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5280"
}

Dragačević, V., Trbojević-Ivić, J., Mutić, J.,& Bezbradica, D.. (2015). Optimizacija proizvodnje i analitika biodizela dobijenog katalitičkom aktivnošću lipaze B Candidae antarcticae. in Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015
Belgrade : Serbian Chemical Society., 68-68.
https://hdl.handle.net/21.15107/rcub_cherry_5280

Dragačević V, Trbojević-Ivić J, Mutić J, Bezbradica D. Optimizacija proizvodnje i analitika biodizela dobijenog katalitičkom aktivnošću lipaze B Candidae antarcticae. in Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015. 2015;:68-68.
https://hdl.handle.net/21.15107/rcub_cherry_5280 .

Dragačević, Vladimir, Trbojević-Ivić, Jovana, Mutić, Jelena, Bezbradica, Dejan, "Optimizacija proizvodnje i analitika biodizela dobijenog katalitičkom aktivnošću lipaze B Candidae antarcticae" in Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015 (2015):68-68,
https://hdl.handle.net/21.15107/rcub_cherry_5280 .

TY  - CONF
AU  - Trbojević-Ivić, Jovana
AU  - Dragačević, Vladimir
AU  - Dimitrijević, Aleksandra
AU  - Gavrović-Jankulović, Marija
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5285
PB  - Beograd : Srpsko hemijsko društvo
C3  - Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015
T1  - Lipaze iz Candida rugosa imobilizovane na hidroksiapatitu: stabilan biokatalizator sa velikim industrijskim potencijalom
SP  - 69
EP  - 69
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5285
ER  - 

@conference{
author = "Trbojević-Ivić, Jovana and Dragačević, Vladimir and Dimitrijević, Aleksandra and Gavrović-Jankulović, Marija",
year = "2015",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015",
title = "Lipaze iz Candida rugosa imobilizovane na hidroksiapatitu: stabilan biokatalizator sa velikim industrijskim potencijalom",
pages = "69-69",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5285"
}

Trbojević-Ivić, J., Dragačević, V., Dimitrijević, A.,& Gavrović-Jankulović, M.. (2015). Lipaze iz Candida rugosa imobilizovane na hidroksiapatitu: stabilan biokatalizator sa velikim industrijskim potencijalom. in Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015
Beograd : Srpsko hemijsko društvo., 69-69.
https://hdl.handle.net/21.15107/rcub_cherry_5285

Trbojević-Ivić J, Dragačević V, Dimitrijević A, Gavrović-Jankulović M. Lipaze iz Candida rugosa imobilizovane na hidroksiapatitu: stabilan biokatalizator sa velikim industrijskim potencijalom. in Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015. 2015;:69-69.
https://hdl.handle.net/21.15107/rcub_cherry_5285 .

Trbojević-Ivić, Jovana, Dragačević, Vladimir, Dimitrijević, Aleksandra, Gavrović-Jankulović, Marija, "Lipaze iz Candida rugosa imobilizovane na hidroksiapatitu: stabilan biokatalizator sa velikim industrijskim potencijalom" in Third Conference of Young Chemists of Serbia - Book of Abstracts, Belgrade, Serbia, October 24, 2015 (2015):69-69,
https://hdl.handle.net/21.15107/rcub_cherry_5285 .

TY  - CONF
AU  - Trbojević-Ivić, Jovana
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bezbradica, Dejan
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5331
AB  - Razvili smo brz i efikasan metod imobilizacije industrijski veoma vrednih Candida rugosa
lipaza (CRL) na ekonomičan, biokompatibilan nosač - hidroksiapatit, sa visokim prinosom
imobilizacije (blizu 100 %) i prinosom aktivnosti od 50 %. Imobilizovane lipaze su pokazale
značajno višu stabilnost nego slobodni enzim, nakon termalnog tretmana na 60 oC i u
prisustvu različitih 95 % polarnih organskih rastvarača, pre svega kratkolančanih alifatičnih
alkohola, značajnih polaznih sirovina u sintezi brojnih estara i drugih značajnih proizvoda.
Predstavljeni rezultati ukazuju na veliki upotrebni potencijal dobijenog preparata u
različitim industrijskim procesima, koji iziskuju rad u nekonvencionalnim reakcionim
uslovima.
AB  - We have developed a simple and highly effective method for immobilising industrially very
appreciated and valuable Candida rugosa lipases from commercial preparation on
ecologically suitable, biodegradable and economical hydroxyapatite support. Our
immobilisation protocol resulted in excellent immobilisation yield of nearly 100 % and
activity yield of 50 %, which is significantly higher in comparison to other immobilisation
protocols for different enzymes on the same support. Immobilised lipase formulation has
proven to have superior stability, compared to free enzyme, at both high temperature (60 o
C) and in the presence of different polar organic solvents, especially short-chain alcohols:
methanol, ethanol and iso-propanol. Therefore, presented experimental data strongly
support the great future potential of the prepared Candida rugosa immobilisate
PB  - Belgrade : Serbian Chemical Society
C3  - 52. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Novi Sad, Srbija, 29. i 30. maj 2015.
T1  - Stabilizacija lipaza iz Candida rugosa jednostavnom i efikasnom imobilizacijom na hidroksiapatitu
SP  - 99
EP  - 99
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5331
ER  - 

@conference{
author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Bezbradica, Dejan and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2015",
abstract = "Razvili smo brz i efikasan metod imobilizacije industrijski veoma vrednih Candida rugosa
lipaza (CRL) na ekonomičan, biokompatibilan nosač - hidroksiapatit, sa visokim prinosom
imobilizacije (blizu 100 %) i prinosom aktivnosti od 50 %. Imobilizovane lipaze su pokazale
značajno višu stabilnost nego slobodni enzim, nakon termalnog tretmana na 60 oC i u
prisustvu različitih 95 % polarnih organskih rastvarača, pre svega kratkolančanih alifatičnih
alkohola, značajnih polaznih sirovina u sintezi brojnih estara i drugih značajnih proizvoda.
Predstavljeni rezultati ukazuju na veliki upotrebni potencijal dobijenog preparata u
različitim industrijskim procesima, koji iziskuju rad u nekonvencionalnim reakcionim
uslovima., We have developed a simple and highly effective method for immobilising industrially very
appreciated and valuable Candida rugosa lipases from commercial preparation on
ecologically suitable, biodegradable and economical hydroxyapatite support. Our
immobilisation protocol resulted in excellent immobilisation yield of nearly 100 % and
activity yield of 50 %, which is significantly higher in comparison to other immobilisation
protocols for different enzymes on the same support. Immobilised lipase formulation has
proven to have superior stability, compared to free enzyme, at both high temperature (60 o
C) and in the presence of different polar organic solvents, especially short-chain alcohols:
methanol, ethanol and iso-propanol. Therefore, presented experimental data strongly
support the great future potential of the prepared Candida rugosa immobilisate",
publisher = "Belgrade : Serbian Chemical Society",
journal = "52. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Novi Sad, Srbija, 29. i 30. maj 2015.",
title = "Stabilizacija lipaza iz Candida rugosa jednostavnom i efikasnom imobilizacijom na hidroksiapatitu",
pages = "99-99",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5331"
}

Trbojević-Ivić, J., Veličković, D., Dimitrijević, A., Bezbradica, D., Gavrović-Jankulović, M.,& Milosavić, N.. (2015). Stabilizacija lipaza iz Candida rugosa jednostavnom i efikasnom imobilizacijom na hidroksiapatitu. in 52. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Novi Sad, Srbija, 29. i 30. maj 2015.
Belgrade : Serbian Chemical Society., 99-99.
https://hdl.handle.net/21.15107/rcub_cherry_5331

Trbojević-Ivić J, Veličković D, Dimitrijević A, Bezbradica D, Gavrović-Jankulović M, Milosavić N. Stabilizacija lipaza iz Candida rugosa jednostavnom i efikasnom imobilizacijom na hidroksiapatitu. in 52. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Novi Sad, Srbija, 29. i 30. maj 2015.. 2015;:99-99.
https://hdl.handle.net/21.15107/rcub_cherry_5331 .

Trbojević-Ivić, Jovana, Veličković, Dušan, Dimitrijević, Aleksandra, Bezbradica, Dejan, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Stabilizacija lipaza iz Candida rugosa jednostavnom i efikasnom imobilizacijom na hidroksiapatitu" in 52. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Novi Sad, Srbija, 29. i 30. maj 2015. (2015):99-99,
https://hdl.handle.net/21.15107/rcub_cherry_5331 .

TY  - JOUR
AU  - Dusan, Velickovic
AU  - Nenad, Milosavic
AU  - Dejan, Bezbradica
AU  - Bihelović, Filip
AU  - Segal, Ann Marie
AU  - Šegan, Dejan M.
AU  - Trbojević-Ivić, Jovana
AU  - Aleksandra, Dimitrijevic
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1797
AB  - Our investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation
VL  - 98
IS  - 14
SP  - 6317
EP  - 6328
DO  - 10.1007/s00253-014-5587-9
ER  - 

@article{
author = "Dusan, Velickovic and Nenad, Milosavic and Dejan, Bezbradica and Bihelović, Filip and Segal, Ann Marie and Šegan, Dejan M. and Trbojević-Ivić, Jovana and Aleksandra, Dimitrijevic",
year = "2014",
abstract = "Our investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation",
volume = "98",
number = "14",
pages = "6317-6328",
doi = "10.1007/s00253-014-5587-9"
}

Dusan, V., Nenad, M., Dejan, B., Bihelović, F., Segal, A. M., Šegan, D. M., Trbojević-Ivić, J.,& Aleksandra, D.. (2014). The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation. in Applied Microbiology and Biotechnology
Springer, New York., 98(14), 6317-6328.
https://doi.org/10.1007/s00253-014-5587-9

Dusan V, Nenad M, Dejan B, Bihelović F, Segal AM, Šegan DM, Trbojević-Ivić J, Aleksandra D. The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation. in Applied Microbiology and Biotechnology. 2014;98(14):6317-6328.
doi:10.1007/s00253-014-5587-9 .

Dusan, Velickovic, Nenad, Milosavic, Dejan, Bezbradica, Bihelović, Filip, Segal, Ann Marie, Šegan, Dejan M., Trbojević-Ivić, Jovana, Aleksandra, Dimitrijevic, "The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation" in Applied Microbiology and Biotechnology, 98, no. 14 (2014):6317-6328,
https://doi.org/10.1007/s00253-014-5587-9 . .

TY  - JOUR
AU  - Pavlović, Marijana
AU  - Dimitrijevic, A.
AU  - Trbojević-Ivić, Jovana
AU  - Milosavic, N.
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Velickovic, D.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1432
AB  - alpha-1,4-Glucosidase from Saccharomyces cerevisiae is an enzyme which is widely used in synthesis of different drugs. Glucosidase inhibitors are studied as potential drugs for prevention of HIV and diabetes. For understanding of these processes it is very important to have insights in the transglucosylation activity of this enzyme. In this paper the kinetics of transglucosylation reaction catalyzed by this enzyme in the synthesis of benzyl alcohol glucoside was studied and all relevant kinetic constants for this system are found. It was shown one additional property of transglycosylation reactions catalyzed by glycosidases-inhibition by both, glucose acceptor and glucose donor, and mechanisms for these inhibitions were proposed.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Russian Journal of Physical Chemistry A
T1  - A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae
VL  - 87
IS  - 13
SP  - 2285
EP  - 2288
DO  - 10.1134/S0036024413130207
ER  - 

@article{
author = "Pavlović, Marijana and Dimitrijevic, A. and Trbojević-Ivić, Jovana and Milosavic, N. and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Velickovic, D.",
year = "2013",
abstract = "alpha-1,4-Glucosidase from Saccharomyces cerevisiae is an enzyme which is widely used in synthesis of different drugs. Glucosidase inhibitors are studied as potential drugs for prevention of HIV and diabetes. For understanding of these processes it is very important to have insights in the transglucosylation activity of this enzyme. In this paper the kinetics of transglucosylation reaction catalyzed by this enzyme in the synthesis of benzyl alcohol glucoside was studied and all relevant kinetic constants for this system are found. It was shown one additional property of transglycosylation reactions catalyzed by glycosidases-inhibition by both, glucose acceptor and glucose donor, and mechanisms for these inhibitions were proposed.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Russian Journal of Physical Chemistry A",
title = "A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae",
volume = "87",
number = "13",
pages = "2285-2288",
doi = "10.1134/S0036024413130207"
}

Pavlović, M., Dimitrijevic, A., Trbojević-Ivić, J., Milosavic, N., Gavrović-Jankulović, M., Bezbradica, D.,& Velickovic, D.. (2013). A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae. in Russian Journal of Physical Chemistry A
Maik Nauka/Interperiodica/Springer, New York., 87(13), 2285-2288.
https://doi.org/10.1134/S0036024413130207

Pavlović M, Dimitrijevic A, Trbojević-Ivić J, Milosavic N, Gavrović-Jankulović M, Bezbradica D, Velickovic D. A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae. in Russian Journal of Physical Chemistry A. 2013;87(13):2285-2288.
doi:10.1134/S0036024413130207 .

Pavlović, Marijana, Dimitrijevic, A., Trbojević-Ivić, Jovana, Milosavic, N., Gavrović-Jankulović, Marija, Bezbradica, Dejan, Velickovic, D., "A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae" in Russian Journal of Physical Chemistry A, 87, no. 13 (2013):2285-2288,
https://doi.org/10.1134/S0036024413130207 . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1456
AB  - The yeast Candida rugosa is a convenient source of lipases for science and industry. Crude preparation of Candida rugosa lipase (CRL) consists of several extracellular lipases. Isoenzyme profile depends on the culture or fermentation conditions. All isoforms are coded by the lip pseudogene family; they are monomers of 534 amino acids and molecular weight of about 60 kDa. They share the same catalytic mechanism and interfacial mode of activation. Isoenzymes differ in isoelectric points, post-translational modifications, substrate specificity and hydrophobicity. The presence of different lipase isoforms and other substances (i.e., inhibitors) in crude preparation leads to lack of their productivity in biocatalytic reactions. Purification of specific isoform improves its overall performance and stability. This paper provides an overview of different methods for purification of CRL isoenzymes up to date, their advantages and disadvantages.
AB  - Lipaze (hidrolaze estara glicerola, E.C.3.1.3.3) su važna grupa enzima, široko rasprostranjenih u prirodi. Mogu se izolovati iz materijala biljnog, životinjskog ili mikrobnog porekla. Zahvaljujući svojim karakteristikama, pobuđuju sve više pažnje kao efikasni biokatalizatori u različitim sintetičkim i hidrolitičkim procesima. Među lipazama, poreklom iz mikroorganizama, posebno su značajne one koje produkuje kvasac Candida rugosa. Komercijalni preparat lipaza iz C. rugosa može sadržati 5-7 izoformi ekstracelularnih lipaza. Sve te izoforme kodirane su od strane lip familije pseudogena, a na njihovu ekspresiju utiču uslovi u kojima se mikroorganizam gaji (sastav hranljive podloge je najvažniji). Ekstracelularne lipaze, koje proizvodi C. rugosa su monomerni glikoproteini, molekulske mase od oko 60 kDa, sa 534 aminokiseline. Za sve izoforme je karakterističan isti složeni mehanizam aktivacije na granici faza i mehanizam katalize, kakav se sreće i kod serin-proteaza. Izoenzimi se međusobno razlikuju po post-translacionim modifikacijama (udelu ugljohidratne komponente), supstratnoj specifičnosti, izoelektričnim tačkama i hidrofobnosti. Prisustvo više izoformi lipaza u komercijalnom preparatu utiče na njihovu produktivnost u reakcijama koje katalizuju. Takvi preparati često sadrže i druge supstance koje mogu uticati na aktivnost enzima (na primer inhibitore). Razdvajanjem pojedinačnih izoformi iz komercijalnog preparata poboljšavaju se njihova enantioselektivnost, specifična aktivnost i stabilnost enzima, što je od izuzetnog značaja za njihovu dalju primenu. U ovom radu su predstavljeni različiti pristupi u razdvajanju pojedinačnih izoformi vanćelijskih lipaza iz komercijalnog preparata C. rugosa, njihove prednosti i nedostaci.
PB  - Assoc Chemists & Chemical Engineers Of Serbia, Belgrade
T2  - Hemijska industrija
T1  - Isolation of Candida rugosa lipase isoforms
T1  - Izolovanje izoformi lipaze iz Candida rugosa
VL  - 67
IS  - 5
SP  - 703
EP  - 706
DO  - 10.2298/HEMIND120828113T
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Veličković, Dušan and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2013",
abstract = "The yeast Candida rugosa is a convenient source of lipases for science and industry. Crude preparation of Candida rugosa lipase (CRL) consists of several extracellular lipases. Isoenzyme profile depends on the culture or fermentation conditions. All isoforms are coded by the lip pseudogene family; they are monomers of 534 amino acids and molecular weight of about 60 kDa. They share the same catalytic mechanism and interfacial mode of activation. Isoenzymes differ in isoelectric points, post-translational modifications, substrate specificity and hydrophobicity. The presence of different lipase isoforms and other substances (i.e., inhibitors) in crude preparation leads to lack of their productivity in biocatalytic reactions. Purification of specific isoform improves its overall performance and stability. This paper provides an overview of different methods for purification of CRL isoenzymes up to date, their advantages and disadvantages., Lipaze (hidrolaze estara glicerola, E.C.3.1.3.3) su važna grupa enzima, široko rasprostranjenih u prirodi. Mogu se izolovati iz materijala biljnog, životinjskog ili mikrobnog porekla. Zahvaljujući svojim karakteristikama, pobuđuju sve više pažnje kao efikasni biokatalizatori u različitim sintetičkim i hidrolitičkim procesima. Među lipazama, poreklom iz mikroorganizama, posebno su značajne one koje produkuje kvasac Candida rugosa. Komercijalni preparat lipaza iz C. rugosa može sadržati 5-7 izoformi ekstracelularnih lipaza. Sve te izoforme kodirane su od strane lip familije pseudogena, a na njihovu ekspresiju utiču uslovi u kojima se mikroorganizam gaji (sastav hranljive podloge je najvažniji). Ekstracelularne lipaze, koje proizvodi C. rugosa su monomerni glikoproteini, molekulske mase od oko 60 kDa, sa 534 aminokiseline. Za sve izoforme je karakterističan isti složeni mehanizam aktivacije na granici faza i mehanizam katalize, kakav se sreće i kod serin-proteaza. Izoenzimi se međusobno razlikuju po post-translacionim modifikacijama (udelu ugljohidratne komponente), supstratnoj specifičnosti, izoelektričnim tačkama i hidrofobnosti. Prisustvo više izoformi lipaza u komercijalnom preparatu utiče na njihovu produktivnost u reakcijama koje katalizuju. Takvi preparati često sadrže i druge supstance koje mogu uticati na aktivnost enzima (na primer inhibitore). Razdvajanjem pojedinačnih izoformi iz komercijalnog preparata poboljšavaju se njihova enantioselektivnost, specifična aktivnost i stabilnost enzima, što je od izuzetnog značaja za njihovu dalju primenu. U ovom radu su predstavljeni različiti pristupi u razdvajanju pojedinačnih izoformi vanćelijskih lipaza iz komercijalnog preparata C. rugosa, njihove prednosti i nedostaci.",
publisher = "Assoc Chemists & Chemical Engineers Of Serbia, Belgrade",
journal = "Hemijska industrija",
title = "Isolation of Candida rugosa lipase isoforms, Izolovanje izoformi lipaze iz Candida rugosa",
volume = "67",
number = "5",
pages = "703-706",
doi = "10.2298/HEMIND120828113T"
}

Trbojević-Ivić, J., Dimitrijević, A., Veličković, D., Gavrović-Jankulović, M.,& Milosavić, N.. (2013). Isolation of Candida rugosa lipase isoforms. in Hemijska industrija
Assoc Chemists & Chemical Engineers Of Serbia, Belgrade., 67(5), 703-706.
https://doi.org/10.2298/HEMIND120828113T

Trbojević-Ivić J, Dimitrijević A, Veličković D, Gavrović-Jankulović M, Milosavić N. Isolation of Candida rugosa lipase isoforms. in Hemijska industrija. 2013;67(5):703-706.
doi:10.2298/HEMIND120828113T .

Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, Veličković, Dušan, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Isolation of Candida rugosa lipase isoforms" in Hemijska industrija, 67, no. 5 (2013):703-706,
https://doi.org/10.2298/HEMIND120828113T . .