Journal ArticleDOI
A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane
TLDR
Experimental observations clearly indicate that the substrates as well as the product (ethanol) act as dead-end inhibitors and a ping-pong bi-bi mechanism with competitive inhibition by substrates and products is proposed that predicts the experimental observation satisfactorily.About:
This article is published in Enzyme and Microbial Technology.The article was published on 1992-09-01. It has received 146 citations till now. The article focuses on the topics: Isoamyl acetate & Ethyl acetate.read more
Citations
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Journal ArticleDOI
Production, purification, characterization, and applications of lipases.
TL;DR: The production, recovery, and use of microbial lipases are discussed; issues of enzyme kinetics, thermostability, and bioactivity are addressed; and production of recombinant lipases is detailed.
Journal ArticleDOI
Bioreactors with immobilized lipases: state of the art.
TL;DR: This review attempts to provide an updated compilation of studies reported in the literature pertaining to reactors containing lipases in immobilized forms, in a way that helps the reader direct a bibliographic search and develop an integrated perspective of the subject.
Journal ArticleDOI
Kinetics and mechanisms of reactions catalyzed by immobilized lipases
TL;DR: A comprehensive overview of the state of the art pertaining to structural features of lipases is provided as an aid to understand immobilization, interfacial activation, and catalytic performance.
Journal ArticleDOI
Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds
TL;DR: A review of the recent developments in the rapidly growing field of lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds can be found in this article.
Journal ArticleDOI
Enzymatic synthesis of isoamyl acetate using immobilized lipase from Rhizomucor miehei
TL;DR: The effects of important reaction parameters for enhancing isoamyl acetate formation through lipase-catalyzed esterification ofisoamyl alcohol were investigated and the operational stability of lipase was also observed to be reasonably high enabling ten reuses of the biocatalyst.
References
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Journal ArticleDOI
A simplex method for function minimization
John A. Nelder,R. Mead +1 more
TL;DR: A method is described for the minimization of a function of n variables, which depends on the comparison of function values at the (n 41) vertices of a general simplex, followed by the replacement of the vertex with the highest value by another point.
Journal ArticleDOI
The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
TL;DR: A nomenclature to facilitate discussion of possible mechanisms for enzyme-catalyzed reactions with more than one substrate or product is proposed and examples are given to illustrate the types of information about reaction mechanisms that can be obtained.
Journal ArticleDOI
Enzymatic catalysis in organic media at 100 degrees C
TL;DR: Porcine pancreatic lipase catalyzes the transesterification reaction between tributyrin and various primary and secondary alcohols in a 99 percent organic medium and exhibits a high catalytic activity at that temperature.
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A Schematic Method of Deriving the Rate Laws for Enzyme-Catalyzed Reactions
Edward L. King,Carl Altman +1 more
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The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory.
TL;DR: A nomenclature is proposed to describe different types of inhibitions of enzyme-catalyzed reactions, particularly for reactions with more than one substrate and product, and the rate equations for such inhibitions are discussed.