TY  - JOUR
AU  - Knezevic, Zorica
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Jakovljević, Živana
AU  - Prodanović, Radivoje
PY  - 2006
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/787
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. (c) 2006 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Sa, Lausanne
T2  - Biochemical Engineering Journal
T1  - Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment
VL  - 30
IS  - 3
SP  - 269
EP  - 278
DO  - 10.1016/j.bej.2006.05.009
ER  - 

@article{
author = "Knezevic, 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. (c) 2006 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Biochemical Engineering Journal",
title = "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment",
volume = "30",
number = "3",
pages = "269-278",
doi = "10.1016/j.bej.2006.05.009"
}

Knezevic, 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 Science Sa, Lausanne., 30(3), 269-278.
https://doi.org/10.1016/j.bej.2006.05.009

Knezevic 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 .

Knezevic, 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 . .