期刊
MARINE DRUGS
卷 14, 期 6, 页码 -出版社
MDPI AG
DOI: 10.3390/md14060108
关键词
alginate lyase; Cellulophaga; enzymatic hydrolysis; oligosaccharides
资金
- Natural Science Foundation of the Jiangsu Higher Education Institutions of China [15KJB360007]
- National Natural Science Foundation of China [81503463]
Enzymatic hydrolysis of sodium alginate to produce alginate oligosaccharides has drawn increasing attention due to its advantages of containing a wild reaction condition, excellent gel properties and specific products easy for purification. However, the efficient commercial enzyme tools are rarely available. A new alginate lyase with high activity (24,038 U/mg) has been purified from a newly isolated marine strain, Cellulophaga sp. NJ-1. The enzyme was most active at 50 degrees C and pH 8.0 and maintained stability at a broad pH range (6.0-10.0) and temperature below 40 degrees C. It had broad substrate specificity toward sodium alginate, heteropolymeric MG blocks (polyMG), homopolymeric M blocks (polyM) and homopolymeric G blocks (polyG), and possessed higher affinity toward polyG (15.63 mM) as well as polyMG (23.90 mM) than polyM (53.61 mM) and sodium alginate (27.21 mM). The TLC and MS spectroscopy analysis of degradation products suggested that it completely hydrolyzed sodium alginate into oligosaccharides of low degrees of polymerization (DPs). The excellent properties would make it a promising tool for full use of sodium alginate to produce oligosaccharides.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据