Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan |
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| Affiliation: | 1. Department of Pure Chemistry, Faculty of Chemistry, Shahid Beheshti University, G.C., Tehran, Iran;2. Nanobiotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, Iran;3. Novozymes A/S, Krogshøjvej 36, 2880 Bagsværd, Copenhagen, Denmark;4. Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran;1. Laboratory of Molecular Biotechnology of Eukaryotes, Center of Biotechnology of Sfax, University of Sfax, Sidi Mansour Street Km 6, BP 1177, 3038 Sfax, Tunisia;2. Laboratory of Microbiology, Habib Bourguiba University-Hospital, Sfax, Tunisia;3. Faculty of Medicine, University of Sfax, Sfax, Tunisia;1. Department of Chemistry, University of Zanjan, Zanjan, Iran;2. Bioprocess Engineering Department, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), P.O. Box 14965/161, Tehran, Iran;3. Department of Environmental Health Engineering, Zanjan University of Medical Sciences, Zanjan, Iran;4. Department of Chemistry, Amirkabir University of Technology (Tehran Polytechnic), Tehran, Iran;5. Nanobiotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, Iran;1. Healthy-Lipids Group, Sección Departamental de Ciencias de la Alimentación, Faculty of Sciences, Universidad Autónoma de Madrid, 28049 Madrid, Spain;2. Pharmacy and Biotechnology Department, School of Biomedical Sciences, Universidad Europea de Madrid, Madrid, Spain;3. Department of Biocatalysis, Institute of Catalysis, CSIC, 28049 Madrid, Spain;1. Sakarya University, Science & Arts Faculty, Department of Chemistry, 54187, Sakarya, Turkey;2. Sakarya University, Biomedical, Magnetic and Semiconductor Materials Application and Research Center (BIMAS-RC), 54187, Sakarya, Turkey;3. Sakarya University, Engineering Faculty, Department of Food Engineering, 54187, Sakarya, Turkey |
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| Abstract: | The Talaromyces thermophilus lipase (TTL) was immobilized by different methods namely adsorption, ionic binding and covalent coupling, using various carriers. Chitosan, pre-treated with glutaraldehyde, was selected as the most suitable support material preserving the catalytic activity almost intact and offering maximum immobilization capacity (76% and 91%, respectively). The chitosan-immobilized lipase could be reputably used for ten cycles with more than 80% of its initial hydrolytic activity. Shift in the optimal temperature from 50 to 60 °C and in the pH from 9.5 to 10, were observed for the immobilized lipase when compared to the free enzyme.The catalytic esterification of oleic acid with 1-butanol has been carried out using hexane as organic solvent. A high performance synthesis of 1-butyl oleate was obtained (95% of conversion yield) at 60 °C with a molar ratio of 1:1 oleic acid to butanol and using 100 U (0.2 g) of immobilized lipase. The esterification product is analysed by GC/MS to confirm the conversion percentage calculated by titration. |
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