Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment
Samo za registrovane korisnike
2006
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 i...n aqueous and microaqueous reaction system.
Ključne reči:
immobilized enzymes / Candida rugosa lipase / Eupergit / enzyme deactivation / kinetic parameters / microemulsionsIzvor:
Biochemical Engineering Journal, 2006, 30, 3, 269-278Izdavač:
- Elsevier, Amsterdam
Finansiranje / projekti:
- Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (RS-MESTD-MPN2006-2010-142020)
DOI: 10.1016/j.bej.2006.05.009
ISSN: 1369-703X
WoS: 000239101800007
Scopus: 2-s2.0-33745267288
Institucija/grupa
Tehnološko-metalurški fakultetTY - JOUR AU - Knežević, Zorica AU - Milosavić, Nenad AU - Bezbradica, Dejan AU - Jakovljević, Živana AU - Prodanović, Radivoje PY - 2006 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/990 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 . .