Journal ArticleDOI
Mechanism and yields in enzyme catalysed equilibrium and kinetically controlled synthesis of β-lactam antibiotics, peptides and other condensation products
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TLDR
Hydrolases can be used to catalyse the synthesis of condensation products such as β-lactam antibiotics, peptides, oligosaccharides and glycerides, and rational analysis of how yield controlling factors may be changed to obtain optimum yields is used to evaluate whether these biotechnological processes can compete with the chemical methods currently used for the synthesis.About:
This article is published in Enzyme and Microbial Technology.The article was published on 1986-01-01. It has received 329 citations till now. The article focuses on the topics: Condensation reaction & Yield (chemistry).read more
Citations
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Modifying enzyme activity and selectivity by immobilization.
Rafael C. Rodrigues,Claudia Ortiz,Ángel Berenguer-Murcia,Rodrigo Torres,Roberto Fernandez-Lafuente +4 more
TL;DR: In this tutorial review, some of the main reasons that may produce an improvement in enzyme activity, specificity or selectivity, either real or apparent, due to immobilization are listed.
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Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests, and recommendations for experimental design and analysis.
TL;DR: The application of thermodynamic and related analysis to reaction systems for enzymic or whole cell catalysis, in which there are high proportions of organic liquid, gas, or supercritical fluid, is discussed.
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Industrial applications of immobilized enzymes—A review
Alessandra Basso,Simona Serban +1 more
TL;DR: A series of large-scale applications of immobilized enzymes with benefits for the food, chemical, pharmaceutical, cosmetics and medical device industries, some of which have been scarcely reported on previously are presented.
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Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties.
Oveimar Barbosa,Rodrigo Torres,Claudia Ortiz,Ángel Berenguer-Murcia,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +5 more
TL;DR: This Review will discuss the suitable properties of the groups able to give the covalent attachment, and the groups unable to produce the first enzyme adsorption on the support, as well as the likely pathways for the evolution.
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Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530.
TL;DR: A serine protease from the keratin-degrading Streptomyces pactum DSM 40530 was purified by casein agarose affinity chromatography and showed high stereoselectivity and secondary specificity with different synthetic substrates.
References
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On the size of the active site in proteases. I. Papain.
Israel Schechter,Arieh Berger +1 more
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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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Redesigning trypsin: alteration of substrate specificity
Charles S. Craik,Corey Largman,Thomas S. Fletcher,Steven Roczniak,Philip J. Barr,Robert J. Fletterick,William J. Rutter +6 more
TL;DR: Although the mutant enzymes were reduced in catalytic rate, they showed enhanced substrate specificity relative to the native enzyme, achieved by the unexpected differential effects on the catalytic activity toward arginine and lysine substrates.
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An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides.
TL;DR: The results indicate that a Michaelis complex, which does not involve coordination of the scissile peptide to the zinc, is consistent with available experimental data and the most plausible of the two complexes.