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. 1984 Nov 1;223(3):707-14.
doi: 10.1042/bj2230707.

Purification and properties of a beta-1,6-glucanase from Penicillium brefeldianum

G P Schep, M G Shepherd, P A Sullivan

Purification and properties of a beta-1,6-glucanase from Penicillium brefeldianum

G P Schep et al. Biochem J. .

Abstract

An inducible endo-beta-1,6-glucanase was purified from Penicillium brefeldianum by DEAE-cellulose, Bio-Gel P-150 and high-pressure liquid chromatography. The final preparation was essentially free from beta-1,3-glucanase and beta-glucosidase activities. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed one protein band with an Mr of 44000. The Vmax. and Km values were calculated to be 624 units (mumol/min)/mg and 2.78 mg/ml respectively. The glucanase had lytic activity against mycelial cells of the yeast Candida albicans. The yield of purified beta-1,6-glucanase from 100 mg dry weight of freeze-dried culture filtrate varied from 60 to 180 units.

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