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Purification and characterization of an extracellular β‐glucanase from Bacillus IMET B 376
Author(s) -
Borriss R.
Publication year - 1981
Publication title -
zeitschrift für allgemeine mikrobiologie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0044-2208
DOI - 10.1002/jobm.19810210103
Subject(s) - laminarin , glucanase , ammonium sulfate precipitation , cellulase , chromatography , cellulose , glucan , chemistry , enzyme , size exclusion chromatography , extracellular , adsorption , ammonium sulfate , biochemistry , organic chemistry
β‐1.3‐1.4‐glucanase (E.C.3.2.1.73) was obtained in highly purified form from the culture fluid of Bacillus IMET B 376 by precipitation with ammonium sulfate, adsorption on CM‐cellulose and then affinity chromatography on lichenan‐Sepharose 4B. The purified enzyme was active on lichenan and barley glucan but not on laminarin and on CM‐cellulose. The molecular weight of the enzyme was estimated to be 26,000 daltons. The K m values for lichenan and barley glucan were determined to be 1.43 and 1.15 mg/ml, respectively. The β‐glucanase has a broad pH optimum between 6 to 8, and was particularly thermostable in presence of Ca ++ .