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Preparation and properties of insolubilized proteinase of Trichoderma koningii.

Manonmani, H. K. and Joseph, R. (1993) Preparation and properties of insolubilized proteinase of Trichoderma koningii. Process Biochemistry, 28 (5). 325-329, 9 ref..

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Purified extracellular alkaline proteinase from Trichoderma koningii (local isolate) was insolubilized by crosslinking with glutaraldehyde. The temp. optimum of the insolubilized enzyme showed a dramatic upward shift to 60-70C from the native enzyme's 50C. The insolubilized enzyme was also relatively more stable over a wide temp. range of 35-80C and from pH 4.0 to 11.0. Activity of the native enzyme was reduced by the presence of Na+, K+, Ag+, Pb2+ and enhanced by Fe2+, Co2+, Ca2+, while a similar influence of these metal ions on the insolubilized enzyme was not evident. The detergents Triton-X and Tween-80 were more inhibitory to the native enzyme than to the insolubilized enzyme. Enhanced affinity to the substrates, casein, haemoglobin and bovine serum albumin, but with lowered Vmax values, was observed for the insolubilized enzyme in comparison to native enzyme. The insolubilized enzyme could be stored in distilled water at 4C for 60 days or recycled 8 times in enzymic reaction with practically no loss in activity.

Item Type: Article
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Food Microbiology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 04 Mar 2011 09:58
Last Modified: 22 Dec 2016 12:34
URI: http://ir.cftri.com/id/eprint/7934

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