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Enhanced in vivo catalytic activity of PEG‐modified cellulase complex from Trichoderma reesei
Author(s) -
Mitra Gargi,
Bachhawat Bimal K.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700202471
Subject(s) - trichoderma reesei , cellulase , peg ratio , polyethylene glycol , chemistry , substrate (aquarium) , enzyme , biochemistry , dextranase , glucanase , conjugate , in vivo , biology , microbiology and biotechnology , ecology , finance , economics , mathematical analysis , mathematics
The cellulase complex from Trichoderma reesei was polyethylene glycol (PEG)‐modified with considerable retention of endo‐β‐1,4‐glucanase activity, as evaluated by the carboxymethylcellutase (CMCase) assay. While resistance towards heat denaturation was the same for either form, susceptibility towards proteolysis was slightly greater for the PEG‐conjugate, in contrast to most reports using other enzymes. The circulatory life of endoglucanase activity associated with the complex was enhanced upon PEG‐modification. This was confirmed by demonstrating degradation of chromogen‐tabelled substrate injected (i.v.) after 24hr of administration of the PEG‐ylated enzymes; in contrast the substrate remained undegraded in mice pretreated with the native complex. The PEG‐modified complex could be a good candidate for the treatment of pneumoconioses of textile workers exposed to cotton dust.