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Updated: Feb 2, 2026

Preparation of Expanded Chitin Foams and their Use in the Removal of Aqueous Copper
Published on: February 27, 2021
ChiE1 from Coprinopsis cinerea is Characterized as a Processive Exochitinase and Revealed to Have a Significant
Jiangsheng Zhou1, Lingling Chen1, Liqin Kang1
1Jiangsu Key Laboratory for Microbes and Microbial Functional Genomics, Jiangsu Engineering and Technology Research Center for Industrialization of Microbial Resources, College of Life Science , Nanjing Normal University , 1 Wenyuan Road , Nanjing 210023 , PR China.
Abstract:
Fruiting bodies that exhibit strong autolysis of Coprinopsis cinerea are a good resource for the chitinolytic system. In this study, a new Chitinase ChiE1 from C. cinerea was cloned, heterologously expressed, and characterized. Biochemical analysis demonstrated that ChiE1 is an exochitinase with a processive mode of action. Although ChiE1 contains only a single catalytic domain without a binding domain, it can bind to and degrade insoluble chitin powder and colloidal chitin. The combination of ChiE1 and C. cinerea endochitinase ChiIII could increase the amount of reducing sugar released from chitin powder by approximately 120% compared to using ChiE1 and ChiIII alone. The synergistic action of ChiE1 and ChiIII on degradation of chitin powder is higher than all previously reported synergism of chitinases. The recombinant Chitinase ChiE1 expressed in Pichia pastoris may be used as a synergistic chitinase for a reconstituted chitinolytic system for agricultural, biological, and environmental applications.
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