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  - 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  - 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  - Trbojević, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5305
PB  - Beograd : Srpsko hemijsko društvo
PB  - Belgrade : Serbian Chemical Society
C3  - Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.
T1  - Adsorpcija lipaze iz Candida rugosa na hidroksiapatitu
SP  - 87
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5305
ER  - 

@conference{
author = "Trbojević, Jovana and Dimitrijević, Aleksandra and Veličković, Dušan and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2012",
publisher = "Beograd : Srpsko hemijsko društvo, Belgrade : Serbian Chemical Society",
journal = "Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.",
title = "Adsorpcija lipaze iz Candida rugosa na hidroksiapatitu",
pages = "87",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5305"
}

Trbojević, J., Dimitrijević, A., Veličković, D., Gavrović-Jankulović, M.,& Milosavić, N.. (2012). Adsorpcija lipaze iz Candida rugosa na hidroksiapatitu. in Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.
Beograd : Srpsko hemijsko društvo., 87.
https://hdl.handle.net/21.15107/rcub_cherry_5305

Trbojević J, Dimitrijević A, Veličković D, Gavrović-Jankulović M, Milosavić N. Adsorpcija lipaze iz Candida rugosa na hidroksiapatitu. in Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012.. 2012;:87.
https://hdl.handle.net/21.15107/rcub_cherry_5305 .

Trbojević, Jovana, Dimitrijević, Aleksandra, Veličković, Dušan, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Adsorpcija lipaze iz Candida rugosa na hidroksiapatitu" in Prva konferencija mladih hemičara Srbije - Kratki izvodi radova, Beograd, 19. i 20. oktobar, 2012. (2012):87,
https://hdl.handle.net/21.15107/rcub_cherry_5305 .

TY  - JOUR
AU  - Milosavić, Nenad
AU  - Prodanović, Radivoje
AU  - Jankov, Ratko M.
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/878
AB  - 4-Hydroxyphenyl-beta-isomaltoside has been synthesized by alpha-glucosidase assisted transglycosylation between arbutin as acceptor and sucrose as donor molecules, respectively. Optimum conditions for the transglucosylation reaction were 40 degrees C for 20 h with 10 mM arbutin and 1.5 M sucrose in a 100 mM sodium citrate/phosphate buffer at pH 5.0. The new glucoside was obtained in a 50% molar yield with respect to arbutin. (C) 2007 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Tetrahedron Letters
T1  - A simple and efficient one-step, regioselective, enzymatic glucosylation of arbutin by alpha-glucosidase
VL  - 48
IS  - 40
SP  - 7222
EP  - 7224
DO  - 10.1016/j.tetlet.2007.07.152
ER  - 

@article{
author = "Milosavić, Nenad and Prodanović, Radivoje and Jankov, Ratko M.",
year = "2007",
abstract = "4-Hydroxyphenyl-beta-isomaltoside has been synthesized by alpha-glucosidase assisted transglycosylation between arbutin as acceptor and sucrose as donor molecules, respectively. Optimum conditions for the transglucosylation reaction were 40 degrees C for 20 h with 10 mM arbutin and 1.5 M sucrose in a 100 mM sodium citrate/phosphate buffer at pH 5.0. The new glucoside was obtained in a 50% molar yield with respect to arbutin. (C) 2007 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Tetrahedron Letters",
title = "A simple and efficient one-step, regioselective, enzymatic glucosylation of arbutin by alpha-glucosidase",
volume = "48",
number = "40",
pages = "7222-7224",
doi = "10.1016/j.tetlet.2007.07.152"
}

Milosavić, N., Prodanović, R.,& Jankov, R. M.. (2007). A simple and efficient one-step, regioselective, enzymatic glucosylation of arbutin by alpha-glucosidase. in Tetrahedron Letters
Pergamon-Elsevier Science Ltd, Oxford., 48(40), 7222-7224.
https://doi.org/10.1016/j.tetlet.2007.07.152

Milosavić N, Prodanović R, Jankov RM. A simple and efficient one-step, regioselective, enzymatic glucosylation of arbutin by alpha-glucosidase. in Tetrahedron Letters. 2007;48(40):7222-7224.
doi:10.1016/j.tetlet.2007.07.152 .

Milosavić, Nenad, Prodanović, Radivoje, Jankov, Ratko M., "A simple and efficient one-step, regioselective, enzymatic glucosylation of arbutin by alpha-glucosidase" in Tetrahedron Letters, 48, no. 40 (2007):7222-7224,
https://doi.org/10.1016/j.tetlet.2007.07.152 . .