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Purification and characterization of an extracellular β-glucanase from Bacillus IMET B 376

✍ Scribed by Dr. sc. R. Borriss

Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
613 KB
Volume
21
Category
Article
ISSN
0233-111X

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✦ Synopsis

Abstract

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^++^.

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