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一种新型褐藻胶裂解酶及其截短体对酶学性质的影响

李辉梅 王文文 储建林 何冰芳 吴斌 钦松

生物加工过程2024,Vol.22Issue(2):156-165,10.
生物加工过程2024,Vol.22Issue(2):156-165,10.DOI:10.3969/j.issn.1672-3678.2024.02.005

一种新型褐藻胶裂解酶及其截短体对酶学性质的影响

A novel alginate lyase and the effect of its truncated form on enzymatic properties

李辉梅 1王文文 1储建林 2何冰芳 2吴斌 1钦松2

作者信息

  • 1. 南京工业大学 生物与制药工程学院,江苏 南京 211800
  • 2. 南京工业大学 药学院,江苏南京 211800
  • 折叠

摘要

Abstract

Alginate oligosaccharides,the degradation products of alginate,display unique physical and chemical properties,as well as excellent biological effects including anti-tumor,growth promotion,immune regulation,thus they have received extensive attention in recent years.Herein,we report our efforts in exploring more effective alginate lyases for the preparation of alginate oligosaccharides.First,microorganisms collected from seaside soil were screened to obtain strains which could degrade alginate.Alginate lyase was then cloned and expressed from the genome of the target strain,and the corresponding catalytic properties were investigated.As a result,a novel endo-type alginate lyase AlgC2m was identified from Paenibacillus lautus A2,which contained 439 amino acids with only 38%of the highest sequence identity.The N-terminal carbohydrate binding module(CBM32)and the C-terminal catalytic domain(CD)were connected by a linker.AlgC2m and its truncated form AlgC2m-CD showed different enzymatic activities(331.05 and 82.47 U/μmol,respectively)and optimum temperatures(45 and 30 ℃,respectively).Moreover,the truncated form AlgC2m-CD demonstrated preference for the degradation of polyG,affording tetrasaccharides with higher degree of polymerization in addition to usual disaccharides and trisaccharides.

关键词

褐藻胶裂解酶/碳水化合物结合模块/非催化结构域/Paenibacillus lautus/产物分布

Key words

alginate lyase/carbohydrate binding modules/non-catalytic domain/Paenibacillus lautus/product distribution

分类

生物工程

引用本文复制引用

李辉梅,王文文,储建林,何冰芳,吴斌,钦松..一种新型褐藻胶裂解酶及其截短体对酶学性质的影响[J].生物加工过程,2024,22(2):156-165,10.

基金项目

国家重点研发计划(2021YFC2101500) (2021YFC2101500)

生物加工过程

OACSTPCD

1672-3678

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