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Continuous proteolysis with a stabilized protease. I. Chemical stabilization of an alkaline protease
Author(s) -
Boudrant J.,
Cuq J. L.,
Cheftel C.
Publication year - 1976
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260181207
Subject(s) - casein , chemistry , glutaraldehyde , protease , alkaline protease , proteolysis , hydrolysate , chromatography , enzyme , substrate (aquarium) , lysine , hydrolysis , biochemistry , organic chemistry , amino acid , biology , ecology
Abstract Due to the loss of enzymatic activity as a function of time, an alkaline protease, selected for the continuous preparation of protein hydrolysates (J. Boudrant and C. Cheftel, Biotechnol. Bioeng ., 18 , 1735, 1976), was chemically stabilized by a simple treatment with glutaraldehyde. Two fractions, soluble and insoluble, were obtained. The activities of these two fractions were measured with casein and N ‐benzoyl‐ L ‐arginine ethyl ester (BAEE) as a function of glutaraldehyde concentration used. It was noted that the insoluble fraction was practically inactive with the first substrate and that the heat stability of the soluble form was likewise enhanced. Molecular weights of these two forms were unchanged, but the uv‐spectrum of the soluble form was modified. From amino acid analysis, it appears that this treatment mainly provokes a decrease in lysine content.