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Competitive inhibition by substrates of the esterification reaction between L-phenylalanine and D-glucose catalysed by the lipases of Rhizomucor miehei and Candida rugosa.

Kenchaiah, Lohith and Balaraman, Manohar and Soundar, Divakar (2007) Competitive inhibition by substrates of the esterification reaction between L-phenylalanine and D-glucose catalysed by the lipases of Rhizomucor miehei and Candida rugosa. World Journal of Microbiology & Biotechnology, 23 (7). 955-964 ; 22 ref..

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Abstract

A detailed kinetic study on esterification between D-glucose and L-phenylalanine catalysed by lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) in organic media was performed. Results show that both lipases followed a Ping-Pong Bi-Bi mechanism with 2 distinct types of competitive inhibition. Double reciprocal plots and computer simulation studies showed that competitive double substrate inhibition took place at higher concn. leading to dead-end inhibition in the case of RML and in the case of CRL, inhibition only by D-glucose at higher concn. leading to dead-end lipase-D-glucose complexes. An attempt to obtain the best fit of these kinetic models through curve-fitting yielded in good approximation, the apparent values of important kinetic parameters were: for RML- kcat = 2.24 0.23mM/h/mg protein, Km L-phenylalanine = 95.6 9.7mM, Km D-glucose = 80.0 8.5mM, Ki L-phenylalanine = 90.0 9.2mM, Ki D-glucose = 13.6 1.42mM; and for CRL - kcat = 0.51 0.06mM/h/mg protein, Km L-phenylalanine = 10.0 0.98mM, Km D-glucose = 6.0 0.64mM, Ki D-glucose = 8.5 0.81mM.

Item Type: Article
Uncontrolled Keywords: AMINO-ACIDS; CANDIDA-; ENZYME-INHIBITORS; ESTERIFICATION-; GLUCOSE-; LIPASES-; RHIZOMUCOR-; CANDIDA-RUGOSA; KINETICS-; PHENYLALANINE-; RHIZOMUCOR-MIEHEI
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Fermentation Technology and Bioengineering
Food Engineering
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Aug 2008 11:03
Last Modified: 28 Dec 2011 10:02
URI: http://ir.cftri.com/id/eprint/8044

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