Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate

被引：58
|
作者：
Zarafeta, Dimitra [1 ,2 ]
Kissas, Dimitrios [1 ,2 ]
Sayer, Christopher [3 ]
Gudbergsdottir, Soley R. [4 ]
Ladoukakis, Efthymios [2 ]
Isupov, Michail N. [3 ]
Chatziioannou, Aristotelis [1 ]
Peng, Xu [4 ]
Littlechild, Jennifer A. [3 ]
Skretas, Georgios [1 ]
Kolisis, Fragiskos N. [2 ]
机构：
[1] Natl Hellen Res Fdn, Inst Biol Med Chem & Biotechnol, Athens, Greece
[2] Natl Tech Univ Athens, Sch Chem Engn, Biotechnol Lab, Athens, Greece
[3] Univ Exeter, Coll Life & Environm Sci, Exeter, Devon, England
[4] Univ Copenhagen, Dept Biol, Danish Archaea Ctr, Copenhagen, Denmark
来源：
PLOS ONE | 2016年 / 11卷 / 01期
基金：
英国生物技术与生命科学研究理事会;
关键词：
DIRECTED EVOLUTION; ENZYMES; SEQUENCE; GENE; PURIFICATION; METAGENOME; PROTEINS; BACTERIA; XYLANASE; SITE;
D O I：
10.1371/journal.pone.0146454
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70 degrees C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.
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页数：18
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