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/123456789/3102
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  - 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  - CONF
AU  - Stojanović, Marija
AU  - Carević, Milica
AU  - Jakovetić, Sonja
AU  - Dimitrijević, Aleksandra
AU  - Trbojević, Jovana
AU  - Mihailović, Mladen
AU  - Veličković, Dušan
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5306
C3  - Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.
T1  - Enzymatic synthesis of L-ascorbyl linoleate
SP  - 64
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5306
ER  - 

@conference{
author = "Stojanović, Marija and Carević, Milica and Jakovetić, Sonja and Dimitrijević, Aleksandra and Trbojević, Jovana and Mihailović, Mladen and Veličković, Dušan",
year = "2012",
journal = "Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.",
title = "Enzymatic synthesis of L-ascorbyl linoleate",
pages = "64",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5306"
}

Stojanović, M., Carević, M., Jakovetić, S., Dimitrijević, A., Trbojević, J., Mihailović, M.,& Veličković, D.. (2012). Enzymatic synthesis of L-ascorbyl linoleate. in Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012., 64.
https://hdl.handle.net/21.15107/rcub_cherry_5306

Stojanović M, Carević M, Jakovetić S, Dimitrijević A, Trbojević J, Mihailović M, Veličković D. Enzymatic synthesis of L-ascorbyl linoleate. in Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.. 2012;:64.
https://hdl.handle.net/21.15107/rcub_cherry_5306 .

Stojanović, Marija, Carević, Milica, Jakovetić, Sonja, Dimitrijević, Aleksandra, Trbojević, Jovana, Mihailović, Mladen, Veličković, Dušan, "Enzymatic synthesis of L-ascorbyl linoleate" in Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012. (2012):64,
https://hdl.handle.net/21.15107/rcub_cherry_5306 .