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

Ayelet Fishman, Sobhi Basheer, Shimon Shatzmiller, Uri Cogan

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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 languageEnglish
Pages (from-to)535-538
Number of pages4
JournalBiotechnology Letters
Issue number6
StatePublished - 1998
Externally publishedYes


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