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Lyophilization of lipase with cyclodextrins for efficient catalysis in ionic liquids

Paper ID Volume ID Publish Year Pages File Format Full-Text
22281 43265 2007 5 PDF Available
Title
Lyophilization of lipase with cyclodextrins for efficient catalysis in ionic liquids
Abstract

Lipase was lyophilized with cyclodextrins to prepare lipase formulation suitable for the efficient resolution of allethrolone in ionic liquids. The effects of the type and amount of cyclodextrin used on lipase preparation were evaluated, and the properties of lyophilized lipase such as thermostability and pH sensitivity were investigated and compared with those of native lipase. The results showed that lipase lyophilized with cyclodextrins can achieve a higher conversion rate than the native one, and that lipase lyophilized with inorganic salts cannot improve the conversion rate of the resolution reaction. The catalytic behavior of the lyophilized lipase was strongly dependent on cyclodextrin type and reaction media. The activity of the lyophilized lipase increased as the amount of added cyclodextrins increased. The activity of the lipase lyophilized with cyclodextrins was optimum at pH 7 and 40°C, which was similar to that of the native one, but the half-life of the lyophilized lipase was low compared with that of the native one.

Keywords
lyophilization; lipase; cyclodextrins; ionic liquids; allethrolone
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Lyophilization of lipase with cyclodextrins for efficient catalysis in ionic liquids
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 103, Issue 4, April 2007, Pages 345–349
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us