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  - 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 . .

TY  - CONF
AU  - Pavlović, Marija
AU  - Dimitrijević, Aleksandra
AU  - Trbojević, Jovana
AU  - Milosavić, Nenad
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Veličković, Dušan
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5332
PB  - Belgrade : Society of Physical Chemists of Serbia
C3  - 11th International Conference of Fundamental and Applied Aspects of Physical Chemistry - Proceedings, September 24-28, 2012
T1  - Inhibition of transglucosylation synthesis of benzyl alcohol glucoside by glucosyl acceptor
VL  - 1
SP  - 185
EP  - 187
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5332
ER  - 

@conference{
author = "Pavlović, Marija and Dimitrijević, Aleksandra and Trbojević, Jovana and Milosavić, Nenad and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Veličković, Dušan",
year = "2012",
publisher = "Belgrade : Society of Physical Chemists of Serbia",
journal = "11th International Conference of Fundamental and Applied Aspects of Physical Chemistry - Proceedings, September 24-28, 2012",
title = "Inhibition of transglucosylation synthesis of benzyl alcohol glucoside by glucosyl acceptor",
volume = "1",
pages = "185-187",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5332"
}

Pavlović, M., Dimitrijević, A., Trbojević, J., Milosavić, N., Gavrović-Jankulović, M., Bezbradica, D.,& Veličković, D.. (2012). Inhibition of transglucosylation synthesis of benzyl alcohol glucoside by glucosyl acceptor. in 11th International Conference of Fundamental and Applied Aspects of Physical Chemistry - Proceedings, September 24-28, 2012
Belgrade : Society of Physical Chemists of Serbia., 1, 185-187.
https://hdl.handle.net/21.15107/rcub_cherry_5332

Pavlović M, Dimitrijević A, Trbojević J, Milosavić N, Gavrović-Jankulović M, Bezbradica D, Veličković D. Inhibition of transglucosylation synthesis of benzyl alcohol glucoside by glucosyl acceptor. in 11th International Conference of Fundamental and Applied Aspects of Physical Chemistry - Proceedings, September 24-28, 2012. 2012;1:185-187.
https://hdl.handle.net/21.15107/rcub_cherry_5332 .

Pavlović, Marija, Dimitrijević, Aleksandra, Trbojević, Jovana, Milosavić, Nenad, Gavrović-Jankulović, Marija, Bezbradica, Dejan, Veličković, Dušan, "Inhibition of transglucosylation synthesis of benzyl alcohol glucoside by glucosyl acceptor" in 11th International Conference of Fundamental and Applied Aspects of Physical Chemistry - Proceedings, September 24-28, 2012, 1 (2012):185-187,
https://hdl.handle.net/21.15107/rcub_cherry_5332 .