Open AccessIsolation and properties of a low molecular mass endoglucanase from Trichoderma reesei
Author(s) -
Sprey B.,
Uelker A.
Publication year - 1992
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.1574-6968.1992.tb05270.x
Subject(s) - trichoderma reesei , cellulase , molecular mass , isoelectric point , isoelectric focusing , chromatography , chemistry , enzyme , biochemistry , isolation (microbiology) , biology , microbiology and biotechnology
Optimal culture conditions for obtaining low molecular mass endoglucanase (EG) from culture fluids of Trichoderma reesei were determined. The purification of this unglycosylated EG in a two‐step procedure is described. In contrast to most cellulases, this EG did not bind to ConA‐affinity columns. The unglycosylated fraction of the culture fluid proteins was further purified by preparative isoelectric focusing. Conditions relevant to an enzyme assay for this EG were determined (pH optimum 5.8, temperature optimum 52°C).