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Improvement of the enantioselectivity of lipase (fraction B) from Candida antarctica via adsorpiton on polyethylenimine-agarose under different experimental conditions

Paper ID Volume ID Publish Year Pages File Format Full-Text
18307 42718 2006 5 PDF Available
Title
Improvement of the enantioselectivity of lipase (fraction B) from Candida antarctica via adsorpiton on polyethylenimine-agarose under different experimental conditions
Abstract

Agarose gels coated with a dense layer of polyethylenimine (PEI-agarose containing 1000 μmol of ionised groups per wet gram of support) are able to adsorb proteins under a very wide range of experimental conditions (different temperatures and pH ranging from pH 5.0 to 9.0). Candida antarctica lipase (fraction B) (CAL-B) was adsorbed on PEI-agarose under very different experimental conditions. The different CAL-B preparations were evaluated as catalysts of the enantioselective hydrolysis of R,S-mandelic acid methyl ester under identical conditions. Interestingly, the best enantioselectivity was achieved with lipase adsorbed at pH 9.0 and 4 °C, conditions where the enzyme exhibited the best enantioslectivity when the reaction was carried out under those conditions. Even more interestingly, these properties were even improved if this preparation was used at pH 5 and 4 °C (E = 25). On the contrary, CAL-B adsorbed at pH 5.0 and 25 °C exhibits a much lower enantioselectivity (E = 3.5) under the same experimental conditions. That is, the same lipase (CAL-B) adsorbed on the same support (PEI-agarose) and used under the same conditions exhibits very different activity–selectivity properties just by using different adsorption conditions. It seems that different conformations of CAL-B can be fixed by intense multipoint anion-exchange involving very large regions of the enzyme surface interacting with these dense layers of polyethyleneimine.

Keywords
Lipase immobilization; CAL-B; Agarose-PEI; Kinetic resolution; Frozen of enzyme structures
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Improvement of the enantioselectivity of lipase (fraction B) from Candida antarctica via adsorpiton on polyethylenimine-agarose under different experimental conditions
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 2, 26 June 2006, Pages 167–171
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