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. 1983 Dec 1;215(3):677-83.
doi: 10.1042/bj2150677.

Cellobiohydrolase from Trichoderma reesei

M Nummi, M L Niku-Paavola, A Lappalainen, T M Enari, V Raunio

Cellobiohydrolase from Trichoderma reesei

M Nummi et al. Biochem J. .

Abstract

A 1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91) was purified from the culture liquid of Trichoderma reesei by using biospecific sorption on amorphous cellulose and immunoaffinity chromatography. A single protein band in polyacrylamide-gel electrophoresis and one arc in immunoelectrophoresis corresponded to the enzyme activity. The Mr was 65 000. The pI was 4.2-3.6. The purified enzyme contained about 10% hexose. The enzyme differs from previously described cellobiohydrolases in being more effective in the hydrolysis of cellulose.

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