Purification and characterization of an extracellular beta-glucanase from Bacillus IMET B 376.
beta-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 Km values for lichenan and barley glucan were determined to be 1.43 and 1.15 mg/ml, respectively. The beta-glucanase has a broad pH optimum between 6 to 8, and was particularly thermostable in presence of Ca++.
D001407:Bacillus / Q000201:enzymology*; D002474:Cell-Free System; D002846:Chromatography, Affinity; D004789:Enzyme Activation; D004794:Enzyme Repression; D005936:Glucans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D012988:Soil Microbiology; D013379:Substrate Specificity; D013696:Temperature
D005936:Glucans; D006026:Glycoside Hydrolases; C028020:licheninase