Affiliation:
1. grid.257022.0 0000000087113200 Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter Hiroshima University 1-3-1, Kagamiyama 739-8530 Higashi-Hiroshima Japan
2. grid.419082.6 0000000417549200 Core Research of Evolutional Science and Technology (CREST) Japan Science and Technology Agency (JST) Tokyo Japan
Abstract
Abstract
We previously constructed a Psychrophile-based Simple bioCatalyst (PSCat) reaction system, in which psychrophilic metabolic enzymes are inactivated by heat treatment, and used it here to study the conversion of aspartic acid from fumaric acid mediated by the activity of aspartate ammonia-lyase (aspartase). In Escherichia coli, the biosynthesis of aspartic acid competes with that of L-malic acid produced from fumaric acid by fumarase. In this study, E. coli aspartase was expressed in psychrophilic Shewanella livingstonensis Ac10 heat treated at 50 °C for 15 min. The resultant PSCat could convert fumaric acid to aspartic acid without the formation of L-malic acid because of heat inactivation of psychrophilic fumarase activity. Furthermore, alginate-immobilized PSCat produced high yields of aspartic acid and could be re-used nine times. The results of our study suggest that PSCat can be applied in biotechnological production as a new approach to increase the yield of target compounds.
Funder
Core Research of Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST)
Publisher
Oxford University Press (OUP)
Subject
Applied Microbiology and Biotechnology,Biotechnology,Bioengineering
Cited by
24 articles.
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