Pectate lyases with increased thermostability and/or...

Details Pectate lyases with increased thermostability and/or... Pectate lyases with increased thermostability and/or...

2008-05-05

2011-11-22

Fronda, Christian (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Lyase

C435S183000, C435S252300, C435S320100, C536S023200

Reexamination Certificate

active

08062877

ABSTRACT:
Using site-directed mutagenesis to mutate theXanthomonas campestrispectate lyase gene, variants ofXanthomonas campestrispectate lyase with improved thermostability and/or enzymatic activity have been expressed inEscherichia coli, and then isolated and purified. The mutantXanthomonas campestrispectate lyases are more effective than the wild-type enzyme, also expressed inE. coli, in removing pectic compounds from natural hemp fiber.

REFERENCES:
Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84.
Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23.

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