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Migration of reactive trace compounds from Novozym® 435 into organic solvents and ionic liquids

Paper ID Volume ID Publish Year Pages File Format Full-Text
4103 208 2010 6 PDF Available
Title
Migration of reactive trace compounds from Novozym® 435 into organic solvents and ionic liquids
Abstract

The commercial form of immobilized Candida antarctica lipase B (CALB), known as Novozym® 435, is a catalyst routinely used in enzymatic reactions. However, we observed a number of compounds migrated from this enzyme preparation into organic solvents and ionic liquids (ILs). These compounds were further identified by GC–MS analysis as a mixture of 17 substances, including 5 major components: glycerol, benzoic acid, 2-hydroxyethyl benzoate, 2-hydroxyethyl sorbate, and sorbic acid. The importance of this discovery is that all five major compounds are reactive in the presence of CALB, especially the last four compounds are potential acyl donors in enzymatic (trans)esterification reactions. We then quantified the migration of these acyl donors into various aqueous solutions, organic solvents and ILs, and observed that the migration into polar organic solvents and ILs was rapid (10–30 min). We also measured the reactivities of these acyl donors with 1-propanol in Novozym® 435-catalyzed (trans)esterifications. Our data suggest that the initial reaction rates of sorbic acid and sorbate ester were very fast; although the initial rates of benzoic acid and benzoate were much slower, their conversions into propyl benzoate were significant within 24 h period. The presence of these compounds in Novozym® 435 may not have considerable impact on fast reactions involving high substrate concentrations, however, it is important to realize that these trace compounds may affect the enzyme activity, and may cause confusion during the analysis of enzymatic reactions.

Keywords
Biocatalysis; Extraction; Novozym® 435; Ionic liquid; Enzyme; Immobilization
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Migration of reactive trace compounds from Novozym® 435 into organic solvents and ionic liquids
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 49, Issue 1, 15 March 2010, Pages 113–118
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