期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 72, 期 12, 页码 3091-3099出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.80141
关键词
chitinase; seaweed; red algae; substrate specificity; cleavage pattern
类别
资金
- Kyowa Technos Co., Ltd.
- National Institute of Agrobiological Sciences
- Kansas State University
Three seaweed chitinase isozymes (Chi-A, B, and C) were purified from a red algae, Chondrus verrucosus. The molecular weights and isoelectric points were 24.5 kDa and 3.5 for Chi-A, 25.5 kDa and 4.6 for Chi-B, and 24.5 kDa and < 3.5 for Chi-C. Optimum pH and temperature were observed at pH 2.0 at 80 degrees C for Chi-A and Chi-C, and at pH 1.0 and 70 degrees C for Chi-B. Toward N-acetylchitooligosaccharide (GlcNAc(n)) (n = 2 to 6), Chi-A, B, and C hydrolyzed GlcNAC(5) and GlcNAC(6) and produced GlcNAC(n) (n = 2 to 4). GlcNAc(n) (n = 3, 4) with the reducing end-side of P anomer was detected in the hydrolysis products. These results indicate that the reactions of Chi-A, B, and C for GlcNAc(n) were a retaining mechanism similar to that of family 18 chitinase. Toward crystalline chitins, Chi-A, B, and C degraded squid pen beta-chitin more than crab shell or shrimp shell alpha-chitin.
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