Abstract
Porcine pancreatic lipase catalyzes the transesterification reaction between tributyrin and various primary and secondary alcohols in a 99 percent organic medium. Upon further dehydration, the enzyme becomes extremely thermostable. Not only can the dry lipase withstand heating at 100°C for many hours, but it exhibits a high catalytic activity at that temperature. Reduction in water content also alters the substrate specificity of the lipase: in contrast to its wet counterpart, the dry enzyme does not react with bulky tertiary alcohols.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 3:41 p.m.) |
Deposited | 7 months, 2 weeks ago (Jan. 11, 2025, 2:27 a.m.) |
Indexed | 1 week ago (Aug. 24, 2025, 7:08 p.m.) |
Issued | 41 years, 2 months ago (June 15, 1984) |
Published | 41 years, 2 months ago (June 15, 1984) |
Published Print | 41 years, 2 months ago (June 15, 1984) |
@article{Zaks_1984, title={Enzymatic Catalysis in Organic Media at 100°C}, volume={224}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.6729453}, DOI={10.1126/science.6729453}, number={4654}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Zaks, Aleksey and Klibanov, Alexander M.}, year={1984}, month=jun, pages={1249–1251} }