Purification and characterization of chitinase A of Streptomyces cyaneus SP-27: An enzyme participates in protoplast formation from Schizophyllum commune mycelia

• Main Authors: Shigekazu Yano, Nopakarn Rattanakit, Arata Honda, Yuta Noda, Mamoru Wakayama, Abhinya Plikomol, Takashi Tachiki
• Format: Journal
• Published: 2018
• Subjects: Biochemistry, Genetics and Molecular Biology; Chemistry; Immunology and Microbiology
• Online Access: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=38549090992&origin=inward; http://cmuir.cmu.ac.th/jspui/handle/6653943832/60182
• Institution: Chiang Mai University

A culture filtrate of Bacillus circulans KA-304 grown on a cell-wall preparation of Schizophyllum commune has an activity to form protoplasts from S. commune mycelia. α-1,3-Glucanase and chitinase I, which were isolated from the filtrate, did not form the protoplast by itself while a mixture of them showed protoplast-forming activity. Streptomyces cyaneus SP-27 was isolated based on the productivity of chitinase. The culture filtrate of S. cyaneus SP-27 did not form S. commune protoplasts, but addition of it to α-1,3- glucanase of B. circulans KA-304 brought about protoplast-forming activity. Chitinase A isolated from the S. cyaneus SP-27 culture filtrate was more effective than chitinase I of B. circulans KA-304 for the protoplast formation in combination with α-1,3-glucanase. The N-terminal amino acid sequence of chitinase A (MW 29,000) has a sequential similarity to those of several Streptomycete family 19 chitinases. Chitinase A adsorbed to chitinous substrate and inhibited the growth of Trichoderma reesei mycelia. Anomer analysis of the reaction products also suggested that the enzyme is a family 19 chitinase.