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Substrate (chemistry)

About: Substrate (chemistry) is a research topic. Over the lifetime, 35902 publications have been published within this topic receiving 740722 citations. The topic is also known as: enzyme substrate.


Papers
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Journal ArticleDOI
TL;DR: A new function derived from kinetic data, the efficiency function, can be used to quantify the efficiency of a catalyst, and three types of evolutionary improvement are discussed: the uniform binding of the substrate to the enzyme, changes in the internal thermodynamics of the bound states, and more effective catalysis of elementary steps.
Abstract: A new function derived from kinetic data, the efficiency function, can be used to quantify the efficiency of a catalyst. For freely diffusing species the maximum efficiency is unity. The enzyme triose phosphate isomerase has an efficiency of 0.6 and is thus almost a perfect catalyst. The efficiency of the acetate ion as catalyst for the same reaction is 2.5 × 10−11. This increase in catalytic efficiency is discussed in terms of three types of evolutionary improvement: the uniform binding of the substrate to the enzyme, changes in the internal thermodynamics of the bound states, and more effective catalysis of elementary steps. These concepts are illustrated for triose phosphate isomerase.

138 citations

Journal ArticleDOI
TL;DR: The results are consistent with the hypothesis that the pancreatic enzyme binds to defect sites at the phase boundaries in substrate bilayers induced by the products and can be adequately described by a single equilibrium.

138 citations

Journal ArticleDOI
TL;DR: The main conclusion drawn from data is that the enzyme kinetics in presence of a substrate film, and probably also under bulk conditions, is controlled by an adsorption flux responsible for an initial lag period and an inactivation flux tending to decrease the reaction rate.

138 citations

Journal ArticleDOI
TL;DR: Epoxy groups containing porous membranes were prepared by UV-initiated photopolymerisation of hydroxyethylmethacrylate and glycidyl methamphetamine to provide multipoint covalent attachment of enzymes, therefore, to stabilize their three-dimensional structure.

138 citations

Journal ArticleDOI
TL;DR: In ethanol fermentation, instantaneous biomass yield of the yeast Saccharmoyces cerevisiae was found to decrease with increase in ethanol concentration, indicating a definite relationship between biomass yield and product inhibition.
Abstract: In ethanol fermentation, instantaneous biomass yield of the yeast Saccharmoyces cerevisiae was found to decrease (from 0.156 to 0.026) with increase in ethanol concentration (from 0 to 107 g/L), indicating a definite relationship between biomass yield and product inhibition. A suitable model was proposed to describe this decrease which incorporates the kinetic parameters of product inhibition rather than pure empirical constants. Substrate inhibition was found to occur when substrate concentration is above 150 g/L. A similar definite relationship was observed between substrate inhibition and instantaneous biomass yield. A simple empirical model is proposed to describe the declines in specIfic growth rate and biomass yield due to substrate inhibition. It is observed that product inhibition does not have any effect on product yield whereas substrate inhibition significantly affects the product yield, reflecting a drop in overall product yield from 0.45 to 0.30 as the initial substrate concentration increases from 150 to 280 g/L. These results are expected to have a significant influence in formulating optimum fermentor design variables and in developing an effective control strategy for optimizing ethanol producitivity.

138 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202214
2021807
20201,053
20191,064
20181,112
20171,024