The Improvement of a Droplet Gel-entrapping Method : The Co-immobilization of Leucine Dehydrogenase and Formate Dehydrogenase(Microbiology & Fermentation Industry)
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概要
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A droplet gel-entrapping method used for enzyme immobilization was improved to simplify the procedure and to increase the enzyme stability. This immobilization technique is suitable for coupled enzyme reactions requiring cofactors. Leucine dehydrogenase (LeuDH) and formate dehydrogenase (FDH) were freeze-dried with bovine serum albumin, dextrin and stabilizers. The freeze-dried enzyme powder was suspended in a methylcellosolve solution containing polyethyleneglycol(#4000)diacrylate, N,N'-methylenebisacrylamide and 2-hydroxyethylacrylate, and the suspension was gelled with initiators. The gel was cut up and the pieces were washed in a buffer to remove the methylcellosolve and the dextrin inside. The maximum conversion ratio for a LeuDH-FDH gel column was determined to be 99.8% by means of the recycling reaction. On long-term operation at 30℃ for leucine production, the initial conversion ratio (7.2%) gradually decreased to 6.6% over the first 10 days. However, the conversion ratio remained almost constant after the 10th day. The effects of flow rate, temperature, pH, and the concentrations of formate, α-ketoisocaproate, ammonium and NAD on the leucine productivity with the gel column were also investigated.
- 社団法人日本農芸化学会の論文
- 1987-11-23
著者
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Maeda Hidekatsu
Fermentation Research Institute Agency Of Industrial Science And Technology
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Kajiwara S
Fermentation Research Institute Agency Of Industrial Science And Technology Ministry Of Internationa
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Maeda Hidekatsu
Fermentation Research Institute Agency Of Industrial Science And Technology Ministry Of Internationa
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KAJIWARA Shigeru
Fermentation Research Institute, Agency of Industrial Science and Technology, Ministry of Internatio
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