Efficient production of methionine from 2-amino-4-methylthiobutanenitrile by recombinant Escherichia coli harboring nitrilase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-08-02

AUTHORS

Li-Qun Jin, Zong-Tong Li, Zhi-Qiang Liu, Yu-Guo Zheng, Yin-Chu Shen

ABSTRACT

Methionine as an essential amino acid has been attracting more attention for its important applications in food and feed additives. In this study, for efficient production of methionine from 2-amino-4-methylthiobutanenitrile, a codon-optimized nitrilase gene was newly synthesized and expressed, and the catalytic conditions for methionine production were studied. The optimal temperature and pH for methionine synthesis were 40 °C and 7.5, respectively. The recombinant nitrilase was thermo-stable with half-life of 5.52 h at 40 °C. The substrate loading was optimized in given amount of catalyst and fixed substrate/catalyst ratio mode to achieve higher productivity. Methionine was produced in 100 % conversion within 120 min with a substrate loading of 300 mM. The production of methionine with the immobilized resting cells in packed-bed reactor was investigated. The immobilized nitrilase exhibited good operation stability and retained over 80 % of the initial activity after operating for 100 h. After separation, the purity and the total yield of methionine reached 99.1 and 97 %, respectively. This recombinant nitrilase could be a potential candidate for application in production of methionine. More... »

PAGES

1479-1486

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10295-014-1490-8

DOI

http://dx.doi.org/10.1007/s10295-014-1490-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045942958

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25085741


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