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A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa

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This article is published in Journal of Organic Chemistry.The article was published on 1991-04-01. It has received 870 citations till now. The article focuses on the topics: Lipase & Candida rugosa.

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Synthetic scope and mechanistic studies of Ru(OH)x/Al2O3-catalyzed heterogeneous hydrogen-transfer reactions.

TL;DR: Results show that direct carbon-to-carbon hydrogen transfer occurs via a metal monohydride for the racemization of chiral secondary alcohols and reduction of carbonyl compounds to alcohols.
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Lipases: An overview of its current challenges and prospectives in the revolution of biocatalysis

TL;DR: The present review mainly summarizes a complete overview of lipases and its biocatalytic applications in pharmaceutical industries especially in the synthesis of (-)-Peroxetine hydrochloride, diltiazem hydrochlorides, chiral β-azidoalcohols, primary amines and amides, vitamin D3 derivatives.
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Selectivity-enhancement of hydrolase reactions

TL;DR: This review pinpoints the strategies which can be employed to improve the enantio- and diasteroselectivity of hydrolytic enzymes, i.e. esterases, proteases, and lipases.
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Understanding lipase stereoselectivity

TL;DR: Factors responsible for lipase stereoselectivity are reviewed, which involves a wide range of factors such as differentiation of enantiotopes, differentiation ofEnantiomers, type of substrate, biochemical interaction of the substrate with the enzyme, steric interaction with the substrate, competition between two different substrates, nature and availability of the active site for stereoselected action.
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