4.3 Article

High-level production and purification of a fully active recombinant dextransucrase from Leuconostoc mesenteroides NRRL B-512F

期刊

FEMS MICROBIOLOGY LETTERS
卷 261, 期 2, 页码 203-210

出版社

OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2006.00347.x

关键词

glucansucrase; dextransucrase; recombinant expression; protein design; dextran

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Recombinant expression of the dextransucrase dsrS gene by Escherichia coli was optimized to produce 5850 U L-culture(-1) of DSR-S, corresponding to a 30-fold increase compared with previous studies. Rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end caused no loss of activity. This new variant successfully purified was remarkably stable. With a k(cat) of 584 s(-1), it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme, and innovative gel properties were obtained.

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