Immobilization of lipase on a hydrophobic zeolite type Y
Апстракт
Lipase from Candida cylindracea was immobilized by adsorption on a hydrophobic zeolite type Y. The maximal amount of bound protein of 8.2 mg g(-1) and an immobilization efficiency of 33% were achieved under optimum conditions. The kinetics of lipase binding to the zeolite were assessed using a general model of topochemical reactions. Based on the values of the parameters of the specific kinetic model, we propose that the adsorption process is controlled by surface kinetics. This was later experimentally confirmed. The activation energy for lipase adsorption on the zeolite is 43 kJ mol(-1).
Кључне речи:
Candida cylindracea lipase / zeolite / immobilization / kinetic modelИзвор:
Journal of the Serbian Chemical Society, 1998, 63, 4, 257-264Издавач:
- Serbian Chemical Society, Belgrade
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Knežević, Zorica AU - Mojović, Ljiljana AU - Adnađević, Borivoj PY - 1998 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/156 AB - Lipase from Candida cylindracea was immobilized by adsorption on a hydrophobic zeolite type Y. The maximal amount of bound protein of 8.2 mg g(-1) and an immobilization efficiency of 33% were achieved under optimum conditions. The kinetics of lipase binding to the zeolite were assessed using a general model of topochemical reactions. Based on the values of the parameters of the specific kinetic model, we propose that the adsorption process is controlled by surface kinetics. This was later experimentally confirmed. The activation energy for lipase adsorption on the zeolite is 43 kJ mol(-1). PB - Serbian Chemical Society, Belgrade T2 - Journal of the Serbian Chemical Society T1 - Immobilization of lipase on a hydrophobic zeolite type Y EP - 264 IS - 4 SP - 257 VL - 63 UR - https://hdl.handle.net/21.15107/rcub_technorep_156 ER -
@article{ author = "Knežević, Zorica and Mojović, Ljiljana and Adnađević, Borivoj", year = "1998", abstract = "Lipase from Candida cylindracea was immobilized by adsorption on a hydrophobic zeolite type Y. The maximal amount of bound protein of 8.2 mg g(-1) and an immobilization efficiency of 33% were achieved under optimum conditions. The kinetics of lipase binding to the zeolite were assessed using a general model of topochemical reactions. Based on the values of the parameters of the specific kinetic model, we propose that the adsorption process is controlled by surface kinetics. This was later experimentally confirmed. The activation energy for lipase adsorption on the zeolite is 43 kJ mol(-1).", publisher = "Serbian Chemical Society, Belgrade", journal = "Journal of the Serbian Chemical Society", title = "Immobilization of lipase on a hydrophobic zeolite type Y", pages = "264-257", number = "4", volume = "63", url = "https://hdl.handle.net/21.15107/rcub_technorep_156" }
Knežević, Z., Mojović, L.,& Adnađević, B.. (1998). Immobilization of lipase on a hydrophobic zeolite type Y. in Journal of the Serbian Chemical Society Serbian Chemical Society, Belgrade., 63(4), 257-264. https://hdl.handle.net/21.15107/rcub_technorep_156
Knežević Z, Mojović L, Adnađević B. Immobilization of lipase on a hydrophobic zeolite type Y. in Journal of the Serbian Chemical Society. 1998;63(4):257-264. https://hdl.handle.net/21.15107/rcub_technorep_156 .
Knežević, Zorica, Mojović, Ljiljana, Adnađević, Borivoj, "Immobilization of lipase on a hydrophobic zeolite type Y" in Journal of the Serbian Chemical Society, 63, no. 4 (1998):257-264, https://hdl.handle.net/21.15107/rcub_technorep_156 .