| Literature DB >> 25418481 |
Shangyong Li1, Xuemei Yang1, Lan Zhang1, Wengong Yu1, Feng Han1.
Abstract
The purpose of this study was to find a cold-adapted and surfactant-stable alginate lyase as a candidate for biotechnological and industrial applications. The gene for a new alginate lyase, AlyL1, from Agarivorans sp. L11 was cloned and expressed in Escherichia coli. The recombinant AlyL1 was most active at 40°C (1,370 U/mg). It was a cold-adapted alginate lyase, which showed 54.5% and 72.1% of maximum activity at 15°C and 20°C, respectively. AlyL1 was an alkaliphilic enzyme and most active at pH 8.6. In addition, it showed high stability in the presence of various surfactants at a high concentration (from 0.1% to 1% (w/v)). AlyL1 was an endo-type alginate lyase that degraded both polyM and polyG blocks, yielding disaccharides and trisaccharides as the main products. This is the first report of the cloning and functional expression of a cold-adapted and surfactant-stable alginate lyase. AlyL1 might be an interesting candidate for biotechnological and industrial applications.Entities:
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Year: 2015 PMID: 25418481 DOI: 10.4014/jmb.1409.09031
Source DB: PubMed Journal: J Microbiol Biotechnol ISSN: 1017-7825 Impact factor: 2.351