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Endo‐(1 → 3)β‐D‐glucanase activity secreted by Bacillus sp. no. 215
Author(s) -
Bertram P.A.,
Chen P.,
Buller C.S.,
Akagi J.M.
Publication year - 1994
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1994.tb00472.x
Subject(s) - curdlan , strain (injury) , alcaligenes , enzyme , alcaligenes faecalis , bacillaceae , divalent , bacillus (shape) , bacillales , extracellular , glucanase , substrate (aquarium) , microbiology and biotechnology , bacteria , glucan , biochemistry , chemistry , enzyme assay , biology , bacillus subtilis , polysaccharide , pseudomonas , genetics , ecology , organic chemistry , anatomy
The production of an extracellular endo‐(1 → 3)‐β‐D‐glucanase by Bacillus sp. no. 215 was induced during growth with (1 → 3)‐β‐D‐glucan (curdlan) from Cellulomonas flavigena strain KU as carbon and energy source. Maximum levels of activity (0.26 U ml ‐1 resp. 1.40 U mg ‐1 ) were detected in cell‐free culture supernatant fluid after 25 h of aerobic growth at 55°C. The cells secreted an endo‐(1 → 3)‐β‐D‐glucanase with low electrophoretic mobility that used curdlan from C. flavigena strain KU and from Agrobacterium sp. (formerly Alcaligenes faecalis var. myxogenes ) as substrates. The enzyme activity was highest at pH 7.0 and 55°C. It exhibited a remarkably low thermal stability with a half‐life of 14 min at 55°C in the presence of substrate. Divalent metal cations were required for enzyme activity.