Production of L-serine from Glycine by Corynebacterium glycinophilum and Properties of Serine Hydroxymethyltransferase, a Key Enzyme in L-Serine Production
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概要
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Fermentative production of L-serine from glycine by Corynebacterium glycinophilum AJ-3413,an auxotrophic mutant of Leu and Met with increased productivity of L-serine using a one liter jar fermentor was carried out and the properties of serine hydroxymethyltransferase (SHMT), a key enzyme in L-serine synthesis, of the parental strain AJ-3170 were investigated. SHMT was effectively induced by the addition of glycine to the medium at an early stage of cultivation. Undre optimal conditions, AJ-3413 produced 16.0 g/l of L-serine from 30 g/l of glycine with a molar yield of 38%. The partially purified SHMT catalyzed the L-allo-threonine degradation in addition to L-serine degradation, but could not catalyze L-threonine degradation. This enzyme showed an absolute tetrahydrofolic acid requirement for L-serine degradation to glycine and formaldehyde, but not for L-allo-threonine degradation. Pyridoxal 5'-phosphate appeared to be required for enzyme activity. The K_m values for glycine and formaldehyde in L-serine synthesis, and for L-serine in L-serine degradation were 1.85,0.29 and 1.64 mM, respectively.
- 公益社団法人日本生物工学会の論文
- 1989-06-25
著者
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Yokozeki Kenzo
Central Research Laboratories Of Ajinomoto Co. Inc.
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KUBOTA Koji
Central Research Laboratories of Ajinomoto Co., Inc.
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Yokozeki Kenzo
Central Research Laboratories Of Ajinomoto Co.
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Kubota Koji
Central Research Laboratories Of Ajinomoto Co. Inc.
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Kubota Koji
Central Research Laboratories Ajinomoto Co. Inc.
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YOKOZEKI KENZO
Central Research Laboratories of Ajinomoto Co., Inc.,
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