Characterization of a New Bifunctional and Cold-Adapted Polysaccharide Lyase (PL) Family 7 Alginate Lyase from <i>Flavobacterium</i> sp.

Alginate oligosaccharides produced by enzymatic degradation show versatile physiological functions and biological activities. In this study, a new alginate lyase encoding gene <i>alyS02</i> from <i>Flavobacterium</i> sp. S02 was recombinantly expressed at a high level in <...

Full description

Bibliographic Details
Main Authors: Hai-Xiang Zhou, Shan-Shan Xu, Xue-Jing Yin, Feng-Long Wang, Yang Li
Format: Article
Language:English
Published: MDPI AG 2020-07-01
Series:Marine Drugs
Subjects:
Online Access:https://www.mdpi.com/1660-3397/18/8/388
Description
Summary:Alginate oligosaccharides produced by enzymatic degradation show versatile physiological functions and biological activities. In this study, a new alginate lyase encoding gene <i>alyS02</i> from <i>Flavobacterium</i> sp. S02 was recombinantly expressed at a high level in <i>Yarrowia lipolytica</i>, with the highest extracellular activity in the supernatant reaching 36.8 ± 2.1 U/mL. AlyS02 was classified in the polysaccharide lyase (PL) family 7. The optimal reaction temperature and pH of this enzyme were 30 °C and 7.6, respectively, indicating that AlyS02 is a cold-adapted enzyme. Interestingly, AlyS02 contained more than 90% enzyme activity at 25 °C, higher than other cold-adapted enzymes. Moreover, AlyS02 is a bifunctional alginate lyase that degrades both polyG and polyM, producing di- and trisaccharides from alginate. These findings suggest that AlyS02 would be a potent tool for the industrial applications.
ISSN:1660-3397