Immobilization of formate dehydrogenase from Candida boidinii through cross-linked enzyme aggregates |
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| Institution: | 1. Department of Microbial Engineering, Konkuk University, Seoul 143-701, South Korea;2. Department of Chemical Engineering, Kwangwoon University, Seoul 139-701, South Korea;3. Department of Chemical and Biochemical Engineering, Dongguk University-Seoul, Seoul 100-715, South Korea;1. Department of Chemical Engineering, Kwangwoon University, 139-701 Seoul, Republic of Korea;2. The Institute of Molecular Biology and Genetics, Seoul National University, 151-742 Seoul, Republic of Korea;1. Faculty of Agriculture, Shinshu University, 8304 Minamiminowa, Nagano 399-4511, Japan;2. JST, PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan;3. Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan;1. Clean Energy Research Centre, Korea Institute of Science and Technology, P.O. Box 131, Cheongryyang, Seoul 136 791, Republic of Korea;2. Department of Microbial Engineering, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul 143-701, Republic of Korea;3. Department of Bio & Nano Chemistry, College of Natural Science, Kookmin University, 861-1, Jeongneung-dong, Sungbuk-gu, Seoul 137-702, Republic of Korea;1. Department of Chemical Engineering, Institute of Chemical Technology, Matunga (E), Mumbai 400019, India;2. Department of Food Technology, University Institute of Chemical Technology, North Maharashtra University, Jalgaon 425001, India;3. Department of Biotechnology Engineering, Kolhapur Institute of Technology''s College of Engineering, Gokul Shirgaon, Kolhapur 416 234, India;1. Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan, Iran;2. Department of Renewable Energy Engineering, Faculty of Advanced Sciences and Technologies, University of Isfahan, Iran |
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| Abstract: | We employed a cross-linked enzyme aggregate (CLEA) method to immobilize formate dehydrogenase (FDH) from Candida boidinii. The optimal conditions for the preparation of CLEAs were determined by examining effects of various parameters: the nature and amount of cross-linking reagent, additive concentration, cross-linking time, and pH during CLEA preparation. The recovered activities of CLEAs were significantly dependent on the concentration of glutaraldehyde; however, the recovered activity was not severely influenced by the content of dextran polyaldehyde as a mild cross-linker. Bovine serum albumin (BSA) was also used as a proteic feeder and enhanced the activity recovery by 130%. The highest recovered activity of CLEA was 18% for formate oxidation reaction and 25% for CO2 reduction reaction. The residual activity of CLEA prepared with dextran polyaldehyde (Dex-CLEA) was over 95% after 10 cycles of reuse. The thermal stability of Dex-CLEA was increased by a factor of 3.6 more than that of the free enzyme. CLEAs of FDH could be utilized efficiently for both NADH regeneration and CO2 reduction. |
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| Keywords: | Formate dehydrogenase Cross-linked enzyme aggregate Optimization |
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