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From protein engineering to immobilization: Promising strategies for the upgrade of industrial enzymes

By Raushan Kumar Singh, Manish Kumar Tiwari, Ranjitha Singh and Jung-kul Lee

Abstract

Abstract: Enzymes found in nature have been exploited in industry due to their inherent catalytic properties in complex chemical processes under mild experimental and environmental conditions. The desired industrial goal is often difficult to achieve using the native form of the enzyme. Recent developments in protein engineering have revolutionized the development of commercially available enzymes into better industrial catalysts. Protein engineering aims at modifying the sequence of a protein, and hence its structure, to create enzymes with improved functional properties such as stability, specific activity, inhibition by reaction products, and selectivity towards non-natural substrates. Soluble enzymes are often immobilized onto solid insoluble supports to be reused in continuous processes and to facilitate the economical recovery of the enzyme after the reaction without any significant loss to its biochemical properties. Immobilization confers considerable stability towards temperature variations and organic solvents. Multipoint and multisubunit covalent attachments of enzymes on appropriately functionalized supports via linkers provide rigidity to the immobilized enzyme structure, ultimately resulting in improved enzyme stability. Protein engineering and immobilization techniques ar

Topics: immobilization, inhibition, protein engineering, selectivity, stabilityInt. J. Mol. Sci. 2013, 14 1233
Year: 2014
OAI identifier: oai:CiteSeerX.psu:10.1.1.417.3471
Provided by: CiteSeerX
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