Elevated temperature and chemical modification selectively abolishes levan forming activity of levansucrase of Zymomonas mobilis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-02

AUTHORS

Gurunathan Sangiliyandi, Krishnan Chandra Raj, Paramasamy Gunasekaran

ABSTRACT

A levansucrase (SacB) of Zymomonas mobilis was purified to electrophoretic homogeneity from a recombinant Escherichia coli. The 55 kDa enzyme hydrolysed β-fructosides but not α-glucosides and catalysed levan formation from sucrose as well as raffinose. The optimum temperature for polymerase activity (30 °C ) was lower than that for hydrolase activity (50 °C ). In contrast to other levansucrases, polymerase activity of levansucrase was inhibited by para- chloromercuribenzoate (1 mM) but with little or no effect on hydrolase activity. Selective modulation of polymerase activity by this inhibitor will be useful in revealing the mechanism of levansucrase catalysis. More... »

PAGES

179-182

References to SciGraph publications

Journal

TITLE

Biotechnology Letters

ISSUE

2

VOLUME

21

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1005493024086

DOI

http://dx.doi.org/10.1023/a:1005493024086

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050603958


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