Discovery and characterization of a thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolate
Zarafeta, Dimitra; Kissas, Dimitrios; Sayer, Christopher; et al.Gudbergsdottir, Sóley R.; Ladoukakis, Efthymios; Isupov, MN; Chatziioannou, Aristotelis; Peng, Xu; Littlechild, JA; Skretas, Georgios; Kolisis, Fragiskos N.
Date: 7 January 2016
Journal
PLoS One
Publisher
Public Library of Science
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Abstract
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 ...
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°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.
Biosciences - old structure
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