Preparation and potential antitumor activity of alginate oligosaccharides degraded by alginate lyase from Cobetia marina

It is of great significance to develop marine resources and study its potential biological activity by using alginate lyase produced by marine psychrophilic bacteria. In the previous study, a new marine psychrophilic bacterium (Cobetia marina HQZ08) was screened from the growth area of Laminaria jap...

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Published inCarbohydrate research Vol. 534; p. 108962
Main Authors Qiu, Xiao-Ming, Lin, Qi, Zheng, Bing-De, Zhao, Wan-Lin, Ye, Jing, Xiao, Mei-Tian
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 01.12.2023
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Summary:It is of great significance to develop marine resources and study its potential biological activity by using alginate lyase produced by marine psychrophilic bacteria. In the previous study, a new marine psychrophilic bacterium (Cobetia marina HQZ08) was screened from the growth area of Laminaria japonica, and it was found that the strain could efficiently produce alginate-degrading enzyme (Aly30). In this paper, the ability of Aly30 to degrade alginate was optimized and the optimal degradation conditions were obtained. It was found that the main degradation product of alginate oligosaccharides was trisaccharide. In vitro cell experiments showed that the antitumor activity of low molecular weight alginate oligosaccharides was better than that of high molecular weight alginate oligosaccharides. In summary, Aly30 had the potential to produce alginate oligosaccharides with low degree of polymerization and antitumor activity, which provided a reference for the enzymatic preparation and application of alginate oligosaccharides. [Display omitted] •Alginate lyase screened from Cobetia marina HQZ08 could degrade alginate to produce oligosaccharides.•The main degradation products of alginate oligosaccharides were trisaccharides.•Low molecular weight alginate oligosaccharides had better antitumor activity.
Bibliography:ObjectType-Article-1
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content type line 23
ISSN:0008-6215
1873-426X
DOI:10.1016/j.carres.2023.108962