Chitinase Chi1 from Myceliophthora Thermophila C1, a Thermostable Enzyme for Chitin and Chitosan Depolymerization

Overview

Journal J Agric Food Chem

Specialties Chemistry
Nutritional Sciences

Date 2018 Jan 24

PMID 29359934

Citations 14

Authors

Malgorzata Krolicka

Sandra W A Hinz

Martijn J Koetsier

Rob Joosten

Gerrit Eggink

Lambertus A M van den Broek

Carmen G Boeriu

Affiliations

Soon will be listed here.

Abstract

A thermostable Chitinase Chi1 from Myceliophthora thermophila C1 was homologously produced and characterized. Chitinase Chi1 shows high thermostability at 40 °C (>140 h 90% activity), 50 °C (>168 h 90% activity), and 55 °C (half-life 48 h). Chitinase Chi1 has broad substrate specificity and converts chitin, chitosan, modified chitosan, and chitin oligosaccharides. The activity of Chitinase Chi1 is strongly affected by the degree of deacetylation (DDA), molecular weight (Mw), and side chain modification of chitosan. Chitinase Chi1 releases mainly (GlcNAc) from insoluble chitin and chito-oligosaccharides with a polymerization degree (DP) ranging from 2 to 12 from chitosan, in a processive way. Chitinase Chi1 shows higher activity toward chitin oligosaccharides (GlcNAc) than toward (GlcNAc) and is inactive for (GlcNAc). During hydrolysis, oligosaccharides bind at subsites -2 to +2 in the enzyme's active site. Chitinase Chi1 can be used for chitin valorisation and for production of chitin- and chito-oligosaccharides at industrial scale.

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