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A comparison of immobilised protease activities
Author(s) -
Jasim Munir A.,
Hall George M.,
Mann John,
Taylor Keith D. A.
Publication year - 1987
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280400404
Subject(s) - papain , trypsin , chemistry , glutaraldehyde , pepsin , cyanogen bromide , hydrolysis , enzyme , protease , chromatography , proteases , immobilized enzyme , substrate (aquarium) , biochemistry , biology , peptide sequence , ecology , gene
Five proteases, bromelain, ficin, papain, pepsin and trypsin were immobilised on cellulose supports by two different techniques using cyanogen bromide or glutaraldehyde. The degree of immobilisation was determined and the activity of the immobilised enzymes compared to that of the free enzymes using egg albumin as a substrate. The stability of each immobilised enzyme was determined by repeated hydrolysis of egg albumin and the most active enzymes used in sequence—the technique of multiple hydrolysis—in order to maximise hydrolysis. In terms of the degree of immobilisation, activity and stability of the enzymes cyanogen bromide was more effective than glutaraldehyde. For the individual enzymes pepsin, trypsin, ficin, bromelain and papain were most active, stable and immobilised to the greatest extent.