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Purification and properties of an extracellular proteinase of Trichoderma koningii.

Manonmani, H. K. and Joseph, R. (1993) Purification and properties of an extracellular proteinase of Trichoderma koningii. Enzyme and Microbial Technology, 15 (7). 624-628, 18 ref..

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Abstract

A proteinase secreted by Trichoderma koningii (local isolate) was purified to apparent homogeneity by ion exchange, gel permeation and affinity chromatography. The enzyme was optimally active at pH 10.5 and 50C and had a pI of 9.0. It contained 16% carbohydrate (2.57% rhamnose, 8.24% arabinose, 4.22% xylose and 1.42% galactose) and was rich in glycine, serine, alanine and aspartic acid residues. Glycine was found at the N-terminus and serine appeared to be present at the active site. Fe2+, Co2+ and Ca2+ at 1mM enhanced catalysis by 3.0-, 2.5- and 1.7-fold, respectively. K+, Na+, Ag+ and Pb2+ inhibited enzyme activity, while Cu2+ and Hg2+ at 1mM were not significantly inhibitory.

Item Type: Article
Uncontrolled Keywords: ENZYMES-; FUNGI-; PROTEINASES-; TRICHODERMA-
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology
Divisions: Food Microbiology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 Jun 2011 11:06
Last Modified: 28 Dec 2011 09:53
URI: http://ir.cftri.com/id/eprint/6379

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