TY  - JOUR
AU  - Knežević, Zorica
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Jakovljević, Živana
AU  - Prodanović, Radivoje
PY  - 2006
UR  - https://machinery.mas.bg.ac.rs/handle/123456789/626
AB  - The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system.
PB  - Elsevier, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment
EP  - 278
IS  - 3
SP  - 269
VL  - 30
DO  - 10.1016/j.bej.2006.05.009
ER  - 

@article{
author = "Knežević, Zorica and Milosavić, Nenad and Bezbradica, Dejan and Jakovljević, Živana and Prodanović, Radivoje",
year = "2006",
abstract = "The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system.",
publisher = "Elsevier, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment",
pages = "278-269",
number = "3",
volume = "30",
doi = "10.1016/j.bej.2006.05.009"
}

Knežević, Z., Milosavić, N., Bezbradica, D., Jakovljević, Ž.,& Prodanović, R.. (2006). Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment. in Biochemical Engineering Journal
Elsevier, Amsterdam., 30(3), 269-278.
https://doi.org/10.1016/j.bej.2006.05.009

Knežević Z, Milosavić N, Bezbradica D, Jakovljević Ž, Prodanović R. Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment. in Biochemical Engineering Journal. 2006;30(3):269-278.
doi:10.1016/j.bej.2006.05.009 .

Knežević, Zorica, Milosavić, Nenad, Bezbradica, Dejan, Jakovljević, Živana, Prodanović, Radivoje, "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment" in Biochemical Engineering Journal, 30, no. 3 (2006):269-278,
https://doi.org/10.1016/j.bej.2006.05.009 . .