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Characterization of a new endo-type alginate lyase from Vibrio sp. NJU-03.

Abstract：

:A gene, encoding a new alginate lyase AlgNJU-03, was cloned from marine bacteria Vibrio sp. NJU-03. The recombinant alginate lyase was characterized followed by being purified by NTA-Ni Sepharose. It exhibited the highest activity (6468.99U/mg) at pH 7.0 and 30°C. Interestingly, AlgNJU-03 possessed broader substrate specificity and high activity toward both polyM (poly β-d-mannuronate) and polyG (poly α-l-guluronate), indicating that it is a bifunctional alginate lyase. Furthermore, Km of AlgNJU-03toward polyG (4.00mM) is lower than those toward alginate (8.50mM) and polyM (10.94mM), demonstrating that the enzyme has a higher affinity to polyG. Meanwhile, the catalytic efficiency (Kcat/Km) toward polyG (11.47s-1/mM) is much higher than those toward sodium alginate (3.60s-1/mM) and polyM (0.50s-1/mM). ESI-MS analysis suggested that AlgNJU-03 mainly released disaccharides, trisaccharides and tetrasaccharides from the three kinds of substrates in an endolytic manner. Therefore, it may be a potential tool to produce alginate oligosaccharides with low DP.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Zhu B,Sun Y,Ni F,Ning L,Yao Z

doi

10.1016/j.ijbiomac.2017.10.164

subject

Has Abstract

pub_date

2018-03-01 00:00:00

pages

1140-1147

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(17)34188-0

journal_volume

108

pub_type

杂志文章

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