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Mizuno K, Awazu N, Tachiki T. Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune. Biosci Biotechnol Biochem. 1998;62(1):39-43doi: 10.1271/bbb.62.39.
Mizuno, K., Awazu, N., & Tachiki, T. (1998). Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune. Bioscience, biotechnology, and biochemistry, 62(1), 39-43. https://doi.org/10.1271/bbb.62.39
Mizuno, K, et al. "Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune." Bioscience, biotechnology, and biochemistry vol. 62,1 (1998): 39-43. doi: https://doi.org/10.1271/bbb.62.39
Mizuno K, Awazu N, Tachiki T. Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune. Biosci Biotechnol Biochem. 1998;62(1):39-43. doi: 10.1271/bbb.62.39. PMID: 27393352.
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Biosci Biotechnol Biochem. 1998;62(1):39-43. doi: 10.1271/bbb.62.39.

Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune.

Bioscience, biotechnology, and biochemistry

K Mizuno, N Awazu, T Tachiki

Affiliations

  1. a Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan University.

PMID: 27393352 DOI: 10.1271/bbb.62.39

Abstract

Hydrolyzing activities toward p-nitrophenyl (p-NP)-β-D-glucoside and laminarin in a culture filtrate of Bacillus circulans KA-304, which has been observed to form protoplasts from Schizophyllum commune mycelia, increased when the bacterium was grown on a cell-wall preparation (CWP) of S. commune or laminarin as a carbon source. An analysis of the filtrate with the CWP suggested occurrence of two major p-NP-β-D-glucoside-hydrolyzing enzymes (β-D-glucosidases I and II) and a laminarin-hydrolyzing enzyme. After separation by DEAE-cellulose column chromatography, β-D-glucosidases I and II were isolated (β-D-glucosidase I: 13-fold purification with 34% yield; β-D-glucosidase II: 26-fold with 8%). The enzymes resembled each other in their properties except for their molecular weight, subunit structure (β-D-glucosidase I: 200,000, tetramer; II: 100,000, dimer), and susceptibility to such substances as p-chloromercuribenzoic acid and Ag(+) ion. β-D-Glucosidases I and II hydrolyzed gentiobiose (β-1,6 glucosidic linkage; Km=3.6 mM, β-D-glucosidase I; 4.6 mM, β-D-glucosidase II) and laminaribiose (β-1,3 glucosidic linkage; Km=6.1 mM, β-D-glucosidase I; 6.7 mD β-D-glucosidase II), and showed a certain reactivity toward laminarin as well.

Keywords: Bacillus circulans KA-304; Schizophyllum commune; laminarinase; β-D-glucosidase

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