Isolation and characterization of lipoamide dehydrogenase from mackerel dark muscle |
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Affiliation: | 1. Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base, Ministry of Science and Technology, Nanjing 210014, PR China;2. Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China;3. School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Rd., 212013 Zhenjiang, Jiangsu, PR China;4. Key Laboratory of Cold Chain Logistics Technology for Agro-product, Ministry of Agriculture and Rural Affairs, PR China;1. Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, PR China;2. Pisa Marine Graduate School, Zhejiang Ocean University, PR China;3. International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Thailand;1. Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, China;2. Pisa Marine Graduate School, Zhejiang Ocean University, China;3. College of Electrical Engineering, North China University of Science and Technology, China;4. International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Thailand |
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Abstract: | - 1.1. Lipoamide dehydrogenase was purified 1500-fold from mackerel dark muscle.
- 2.2. The enzyme was homogeneous as judged by acrylamide gel electrophoresis in the presence and absence of SDS.
- 3.3. Molecular weights of 102,000 and 55,000 were estimated for the native and denatured enzyme, respectively.
- 4.4. Optimal activity for the enzyme was obtained at around pH 5.7 and enhanced with citri acid.
- 5.5. Loss of activity was less than 5% by incubating the enzyme at 70°C for 20 min.
- 6.6. An apparent Km of 3.1 × 10−3 M was obtained for dl-lipoic acid and 1.5 × 10−5 M for NADH.
- 7.7. The properties of lipoamide dehydrogenase from mackerel dark muscle observed in this investigation were very similar to those reported for the enzyme from other sources.
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