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Studies on the β‐glucosidase and endo‐1, 4‐glucanase activities from Clostridium papyrosolvens
Author(s) -
Lequerica Juan L.,
Valdés Teresa,
PérezMartínez Caspar
Publication year - 1992
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280540209
Subject(s) - cellobiose , chemistry , glucanase , biochemistry , enzyme , glucosidases , ammonium , fractionation , cellulase , chromatography , organic chemistry
Activities of endo‐β‐4‐glucanase and β‐glucosidase from Clostridium papyrosolvens (CECT 747) were studied under different conditions. No indications were found for the presence of more than one β‐glucosidase after ion exchange and ammonium sulphate fractionation. β‐Glucosidase showed activity against p ‐nitrophenyl‐β‐D‐glucopyranoside and cellobiose but was not inhibited by δ‐gluconolactone. Independent cellobiose phosphorylase activity could also be detected. The β‐glucosidase was essentially intracellular. By the use of stationary phase culture assays, enzyme induction at low concentrations of cellobiose was observed, whilst glucose had no effect. Regulation of endo‐β‐1,4‐glucanase and β‐glucosidase were compared.