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ENZYMIC DEGRADATION OF CEREAL HEMICELLULOSES V. β‐GLUCAN DEGRADATION BY A MOULD ENZYME
Author(s) -
Preece I. A.,
Bhuiyan M. A. M.
Publication year - 1964
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1964.tb01998.x
Subject(s) - degradation (telecommunications) , glucan , enzyme , food science , chemistry , biochemistry , computer science , telecommunications
An enzyme preparation from the culture fluid of a strain of Penicillium chrysogenum has limited action on barley β‐glucan, liberating as the principal products of hydrolysis laminaribiose, β‐glucosyl‐4‐laminaribiose, and β‐cellobiosyl‐4‐laminaribiose. The endo‐activity of this preparation is unaccompanied by exo‐activity or by β‐gluco‐oligosaccharases, but the fungus mycelium contains the same enzyme along with oligosaccharases. It is considered that the enzyme is an endo‐β‐1,3‐glucanase. Comparison of the products given by this enzyme with those produced from β‐glucan by barley enzyme preparations further supports the suggestion that, in barley, an enzyme of this type is accompanied by an endo‐β‐1,4‐glucanase.