Open AccessGeneral and kinetic properties of endoglucanase from Aspergillus niger
Author(s) -
Singh Ajay,
Agrawal A.K.,
Abidi A.B.,
Darmwal N.S.
Publication year - 1990
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.1574-6968.1990.tb03826.x
Subject(s) - aspergillus niger , cellulase , enzyme , chemistry , sephadex , glycerol , sodium azide , reagent , metal ions in aqueous solution , ammonium , enzyme assay , sodium , metal , fractionation , biochemistry , active site , chromatography , organic chemistry
Endoglucanase of Aspergillus niger AS‐101 was partially purified by ammonium sulphate fractionation and molecular sieving on Sephadex G‐200. The enzyme was found to be unstable on storage, however, it received some protection on the addition of BSA, glycerol or sodium azide. Glycerol also protected the enzyme from inactivation due to freezing and thawing. Studies on the effect of thiol group reagents revealed the involvement of ‐SH group(s) at the active site of enzyme. The enzyme was a metallo‐protein or it required certain metal ions for activation. A variety of modulators such as macroionic compounds and metal ions showed varying effects on the purified endoglucanase.