Fatty-acid-modified enzymes as enantioselective catalysts in microaqueous organic media

Ayelet Fishman; Sobhi Basheer; Shimon Shatzmiller; Uri Cogan

doi:10.1023/A:1005385208618

Fatty-acid-modified enzymes as enantioselective catalysts in microaqueous organic media

Ayelet Fishman, Sobhi Basheer, Shimon Shatzmiller, Uri Cogan

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Highly active lipase and protease complexes were prepared by non-covalent modification with stearic acid. The protein content and yield of the modified enzyme complexes depended on the enzymes' source. The increase in the transesterification activity of the modified enzymes was 15 fold for Candida rugosa lipase and porcine pancreatic lipase, with preservation of the enantioselectivity. Pseudomonas sp. lipase which showed no activity in its crude form, exhibited an activity of 38 μmol/h·mg protein in the modified form.

Original language	English
Pages (from-to)	535-538
Number of pages	4
Journal	Biotechnology Letters
Volume	20
Issue number	6
DOIs	https://doi.org/10.1023/A:1005385208618
State	Published - 1998
Externally published	Yes

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abstract = "Highly active lipase and protease complexes were prepared by non-covalent modification with stearic acid. The protein content and yield of the modified enzyme complexes depended on the enzymes' source. The increase in the transesterification activity of the modified enzymes was 15 fold for Candida rugosa lipase and porcine pancreatic lipase, with preservation of the enantioselectivity. Pseudomonas sp. lipase which showed no activity in its crude form, exhibited an activity of 38 μmol/h·mg protein in the modified form.",

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AU - Cogan, Uri

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AB - Highly active lipase and protease complexes were prepared by non-covalent modification with stearic acid. The protein content and yield of the modified enzyme complexes depended on the enzymes' source. The increase in the transesterification activity of the modified enzymes was 15 fold for Candida rugosa lipase and porcine pancreatic lipase, with preservation of the enantioselectivity. Pseudomonas sp. lipase which showed no activity in its crude form, exhibited an activity of 38 μmol/h·mg protein in the modified form.

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Fatty-acid-modified enzymes as enantioselective catalysts in microaqueous organic media

Abstract

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