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Hyperbranched polymer conjugated lipase with enhanced activity and stability

Paper ID Volume ID Publish Year Pages File Format Full-Text
4799 246 2007 7 PDF Available
Title
Hyperbranched polymer conjugated lipase with enhanced activity and stability
Abstract

Hyperbranched aromatic polyamides were synthesized from p-phenylenediamine and trimesic acid, and subjected to the conjugation of lipase using carbodiimide as a coupling reagent. The molecular weights of the conjugates were determined by size exclusion chromatography and gel electrophoresis, which showed that each polymer molecule could be covalently modified with a maximum of five to six lipase molecules. The Km of the conjugate to substrate, p-nitrophenylpalmitate, was equal to native lipase while Vmax was increased by 20%, suggesting an enhanced structural transition of lipase during catalysis conducted at the periphery of the polymer. Moreover, the conjugate exhibited a significantly enhanced stability at high temperature or in the presence of organic solvent, as compared to its native counterpart. This might due to the hydrophilic carboxylic groups of polymer that created a suitable microenvironment for lipase. These results indicate that hyperbranched polymer–enzyme conjugate, with the enhanced activity and stability, is promising for industrial biocatalysis.

Keywords
Bioconjugate; Enzyme modification; Hyperbranched polymer; Hyperbranched aromatic polyamide; Lipase; Enzyme stabilization
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 36, Issue 2, 15 September 2007, Pages 93–99
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
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Full-text PDF Download
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