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Enzyme-catalyzed processes in organic solvents.

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Zaks, A, Klibanov, A M·1985·Proceedings of the National Academy of Sciences

Abstract

Three different lipases (porcine pancreatic, yeast, and mold) can vigorously act as catalysts in a number of nearly anhydrous organic solvents. Various transesterification reactions catalyzed by porcine pancreatic lipase in hexane obey Michaelis-Menten kinetics. The dependence of the catalytic activity of the enzyme in organic media on the pH of the aqueous solution from which it was recovered is bell-shaped, with the maximum coinciding with the pH optimum of the enzymatic activity in water. The catalytic power exhibited by the lipases in organic solvents is comparable to that displayed in water. In addition to transesterification, lipases can catalyze several other processes in organic media including esterification, aminolysis, acyl exchange, thiotransesterification, and oximolysis; some of these reactions proceed to an appreciable extent only in nonaqueous solvents.

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Metadata

Authors
Zaks, A., & Klibanov, A. M.
Venue
Proceedings of the National Academy of Sciences
Published
1985-05
Volume
82
Issue
10
Pages
3192-3196
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2035176560
Cited by
1,235
References
0
FWCI
7.59
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Enzyme-catalyzed processes in organic solvents. https://app.cochat.ai/papers/10.1073/pnas.82.10.3192
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Zaks, A., & Klibanov, A. M. (1985). Enzyme-catalyzed processes in organic solvents. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.10.3192

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.