Characterization of a new endo-type alginate lyase from Vibrio sp W13

被引:67
|
作者
Zhu, Benwei [1 ,2 ]
Tan, Haidong [1 ]
Qin, Yuqi [3 ]
Xu, Qingsong [1 ]
Du, Yuguang [1 ,4 ]
Yin, Heng [1 ]
机构
[1] Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Shandong Univ, Natl Glycoengn Res Ctr, Jinan 250100, Peoples R China
[4] Chinese Acad Sci, Inst Proc Engn, Beijing 100190, Peoples R China
基金
中国国家自然科学基金;
关键词
Alginate lyase; Polysaccharide lyase family 7; Vibrio sp; OLIGOALGINATE LYASE; SEQUENCE-ANALYSIS; PURIFICATION; CLONING; OLIGOSACCHARIDE; POLYSACCHARIDE; DEPOLYMERIZATION; AGARIVORANS; INDUCTION; GROWTH;
D O I
10.1016/j.ijbiomac.2015.01.053
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A gene, encoding a new alginate lyase Algb, was identified and cloned from marine bacterium Vibrio sp. W13. The recombinant alginate lyase was characterized followed by being purified on Ni-NTA Sepharose. It exhibited the highest activity (457 U/mg) at pH 8.0 and 30 degrees C Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly beta-D-mannuronate) and polyG (poly alpha-L-guluronate). Furthermore, K-m values of Algb toward alginate (0.67 mg/ml) and polyMG (0.50 mg/ml) are lower than those toward polyG (1.04 mg/ml) and polyM (6.90 mg/ml). The TLC and ESI-MS analysis suggested that Algb mainly released oligosaccharides with DP of 2-5 from the four kinds of substrates in an endolytic manner. Therefore, it may be a potent tool to produce alginate oligosaccharides with low DP. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:330 / 337
页数:8
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