ArticleJournal of industrial microbiology & biotechnology2015
Efficient aspartic acid production by a psychrophile-based simple biocatalyst.
Article in Journal of industrial microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 27 citations in OpenAlex.
- Performance comparison of downstream unit operations and process chains for the purification of amino acids for food, feed and pharma applications.Biotechnology reports (Amsterdam, Netherlands) · 2026Review
- Enhanced Stability ofPolymers · 2025Article
- A novel salt- and organic solvent-tolerant phosphite dehydrogenase fromFrontiers in bioengineering and biotechnology · 2023Article
- Our microbes not only produce antibiotics, they also overproduce amino acids.The Journal of antibiotics · 2017Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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