Improving Activity of Salt-Lyophilized Enzymes in Organic Media View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2007-09-15

AUTHORS

Abhijeet P. Borole , Brian H. Davison

ABSTRACT

Lyophilization with salts has been identified as an important method of activating enzymes in organic media. Using salt-activated enzymes to transform molecules tethered to solid surfaces in organic phase requires solubilization of enzymes in the solvents. Methods of improving performance of salt-lyophilized enzymes, further, via chemical modification, and use of surfactants and surfactants to create fine emulsions prior to lyophilization are investigated. The reaction system used is transesterification of N-acetyl phenylalanine ethyl ester with methanol or propanol. Initial rate of formation of amino acid esters by subtilisin Carlsberg (SC) was studied and found to increase two to sevenfold by either chemical modification or addition of surfactants in certain solvents, relative to the salt (only)-lyophilized enzyme. The method to prepare highly dispersed enzymes in a salt-surfactant milieu also improved activity by two to threefold. To test the effect of chemical modification on derivatization of drug molecules, acylation of bergenin was investigated using chemically modified SC. More... »

PAGES

335-342

Book

TITLE

Biotechnology for Fuels and Chemicals

ISBN

978-1-60327-525-5
978-1-60327-526-2

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-60327-526-2_33

DOI

http://dx.doi.org/10.1007/978-1-60327-526-2_33

DIMENSIONS

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