Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as Cross-linked enzyme aggregates (CLEAs) |
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| Institution: | 1. Biochemistry Department, Science of Faculty, Ege University, 35100 Bornova/Izmir, Turkey;2. CLEA Technologies BV, Julianalaan 136, 2628 BL Delft, The Netherlands;3. Laboratory of Biocatalysis and Organic Chemistry, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands;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. BRD School of Biosciences, Satellite Campus, Vadtal Road, P.O. Box # 39, Sardar Patel University, Vallabh Vidhyanagar, Anand 388 120, Gujarat, India;2. Department of Materials Science, Sardar Patel University, Vallabh Vidhyanagar, Anand 388 120, Gujarat, India;1. Department of Microbial Engineering, Konkuk University, Seoul 143-701, South Korea;2. Department of Textile Engineering, Konkuk University, Seoul 143-701, South Korea;3. Department of Chemical Engineering, Kwangwoon University, Seoul 139-701, South Korea;4. Department of Advanced Materials & Chemical Engineering, Hannam University, Daejeon 305-811, South Korea |
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| Abstract: | Cross-linked enzyme aggregates (CLEA®s) were prepared from Candida rugosa lipase (CrL) using glutaraldehyde as the cross-linker. The optimum conditions of the immobilization process were determined (precipitant: ethanol, crosslinker concentration: 25 mM, enzyme concentration: 50 mg/ml, crosslinking time: 45 min.). CLEAs were shown to have several advantages compared to the free enzyme. They were more stable at 50 °C and 60 °C and had good reusability; retaining 40% of their initial activity after 15 recycles in aqueous media and remaining constant at that level thereafter, suggesting some initial leaching in water. The CLEAs catalyzed esterification reactions in cyclohexane, affording higher conversions than with the free enzyme, especially when longer fatty acids and alcohols were used as substrates. |
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