Please use this identifier to cite or link to this item: http://hdl.handle.net/11452/22528
Title: Optimization of immobilization conditions of Thermomyces lanuginosus lipase on styrene-divinylbenzene copolymer using response surface methodology
Authors: Uludağ Üniversitesi/Fen Edebiyat Fakültesi/Kimya Bölümü.
0000-0002-0380-1992
0000-0002-9381-0410
Aybastier, Önder
Demir, Cevdet
X-4621-2018
ABA-2005-2020
35344478800
7003565902
Keywords: Thermomyces lanuginosus
Immobilization
Enzyme activity
Styrene-divinylbenzene
Response surface methodology
Biodiesel fuel production
Candida-rugosa lipase
Covalent immobilization
Microbial lipase
Oil
Biocatalys
Selectivity
Improvement
Activation
Parameters
Biochemistry & molecular biology
Chemistry
Thermomyces lanuginosus
Concentration (process)
Copolymerization
Enzyme immobilization
Enzymes
Methanol
Optimization
PH effects
Polynomials
Styrene
Surface properties
Buffer concentrations
Central composite designs
Covalent binding
Enzyme concentrations
Enzyme deactivation
Humicola lanuginosa
Immobilization conditions
Immobilized lipase
Loading capacities
Microbial lipase
Microporous
Operational stability
Optimal conditions
Optimum conditions
Quadratic polynomial
Response surface methodology
Significant factors
Specific activity
Styrene-divinylbenzene
Styrene-divinylbenzene copolymers
Tert butanol
Thermomyces lanuginosus
Thermomyces lanuginosus lipase
Enzyme activity
Biochemistry & molecular biology
Chemistry
Issue Date: May-2010
Publisher: Elsevier Science
Citation: Aybastier, Ö. ve Demir, C. (2010). "Optimization of immobilization conditions of Thermomyces lanuginosus lipase on styrene-divinylbenzene copolymer using response surface methodology". Journal of Molecular Catalysis B-enzymatic, 63(3-4), 170-178.
Abstract: Microbial lipase from Thermomyces lanuginosus (formerly Humicola lanuginosa) was immobilized by covalent binding on a novel microporous styrene-divinylbenzene polyglutaraldehyde copolymer (STY-DVB-PGA). The response surface methodology (RSM) was used to optimize the conditions for the maximum activity and to understand the significance and interaction of the factors affecting the specific activity of immobilized lipase. The central composite design was employed to evaluate the effects of enzyme concentration (4-16%, v/v), pH (6.0-8.0), buffer concentration (20-100 mM) and immobilization time (8-40h) on the specific activity. The results indicated that enzyme concentration, pH and buffer concentration were the significant factors on the specific activity of immobilized lipase and quadratic polynomial equation was obtained for specific activity. The predicted specific activity was 8.78 mu mol p-NP/mg enzyme min under the optimal conditions and the subsequent verification experiment with the specific activity of 8.41 mu mol p-NP/mg enzyme min confirmed the validity of the predicted model. The lipase loading capacity was obtained as 5.71 mg/g support at the optimum conditions. Operational stability was determined with immobilized lipase and it indicated that a small enzyme deactivation (12%) occurred after being used repeatedly for 10 consecutive batches with each of 24 h. The effect of methanol and tert-butanol on the specific activity of immobilized lipase was investigated. The immobilized lipase was almost stable in tert-butanol (92%) whereas it lost most of its activity in methanol (80%) after 15 min incubation.
URI: https://doi.org/10.1016/j.molcatb.2010.01.013
https://www.sciencedirect.com/science/article/pii/S1381117710000238
http://hdl.handle.net/11452/22528
ISSN: 1381-1177
1873-3158
Appears in Collections:Scopus
Web of Science

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