Open AccessPurification and properties of a 1,3‐β‐glucanase from Penicillium oxalicum autolysates
Author(s) -
CopaPatiño JoséLuis,
Reyes Fuensanta,
PérezLeblic María Isabel
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03675.x
Subject(s) - laminarin , enzyme , chemistry , chromatography , concanavalin a , glucanase , penicillium , enzyme assay , biochemistry , autolysis (biology) , food science , in vitro
High 1,3‐β‐glucanase activity was detected during autolysis in a culture medium containing Penicillium oxalicum . It was due to the combined action of four enzymes. The purification process for the major enzyme produced a homogeneous band in the SDS polyacrylamide gel that corresponded to a molecular weight of 79 400 daltons. The enzyme p I was 6.3 and it was only active against 1,3‐β‐glucans, with a S 0.5 of 0.23 mg ml −1 against laminarin. The enzymatic optima were found at pH 4 and 55°C, and instability was evident when pH and temperature were altered. The enzyme was not active against oxidated lamanarin and was barely inhibited by glucono‐D‐lactone. Hg 2+ , Ag + and Fe 2+ were effective inhibitors. The enzyme was adsorbed by concanavalin‐A‐sepharose.