Chitinase system of Aeromonas salmonicida, and characterization of enzymes involved in chitin degradation

Author:

Pentekhina Iuliia12,Hattori Tatsuyuki1,Tran Dinh Minh3,Shima Mizuki4,Watanabe Takeshi14,Sugimoto Hayuki14,Suzuki Kazushi145

Affiliation:

1. Graduate School of Science and Technology, Niigata University, Niigata, Japan

2. School of Economics and Management, Far Eastern Federal University, Vladivostok, Russia

3. Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot, Vietnam

4. Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Niigata, Japan

5. Sakeology Center, Niigata University, Niigata, Japan

Abstract

Abstract The genes encoding chitin-degrading enzymes in Aeromonas salmonicida SWSY-1.411 were identified and cloned in Escherichia coli. The strain contained two glycoside hydrolase (GH) families 18 chitinases: AsChiA and AsChiB, two GH19 chitinases: AsChiC and AsChiD, and an auxiliary activities family 10 protein, lytic polysaccharide monooxygenase: AsLPMO10A. These enzymes were successfully expressed in E. coli and purified. AsChiB had the highest hydrolytic activity against insoluble chitin. AsChiD had the highest activity against water-soluble chitin. The peroxygenase activity of AsLPMO10A was lower compared to SmLPMO10A from Serratia marcescens. Synergism on powdered chitin degradation was observed when AsChiA and AsLPMO10A were combined with other chitinases of this strain. More than twice the increase of the synergistic effect was observed when powdered chitin was treated by a combination of AsLPMO10A with all chitinases. GH19 chitinases suppressed the hyphal growth of Trichoderma reesei.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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