Abstract
Alginate oligosaccharides produced by enzymatic degradation show versatile physiological functions and biological activities. In this study, a new alginate lyase encoding gene alyS02 from Flavobacterium sp. S02 was recombinantly expressed at a high level in Yarrowia lipolytica, 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.
Highlights
IntroductionDevelopment and application of algal biomass have been increasingly emphasized in various fields [1,2,3]
Over the past decades, development and application of algal biomass have been increasingly emphasized in various fields [1,2,3]
S02 was isolated from brown seaweed in the Yellow Sea, China, the genomic analysis of which implied there existed a putative alginate lyase-encoding gene alyS02
Summary
Development and application of algal biomass have been increasingly emphasized in various fields [1,2,3]. The depolymerization products of alginate by enzymatic catalysis, have attracted more attention due to their better solubility and remarkable biological activities compared with macromolecular alginates [11] They can be used as therapeutic agents such as anticoagulants, tumor inhibitors, anti-allergy medicine, and anti-viral drugs [12,13,14,15]. In the past several years, many alginate lyases with various properties have been isolated, cloned, purified and characterized from those sources especially from a diversity of marine bacteria [55]. Few of these reported enzymes have been commercially used owing to their poor properties [56]. These special features suggest that AlyS02 would be a useful enzyme for industrial applications
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