Thermodynamic analysis of solvent effect on substrate specificity of lyophilized enzymes suspended in organic media

Journal Article · Tue Nov 04 23:00:00 EST 1997 · Biotechnology and Bioengineering

DOI:https://doi.org/10.1002/(SICI)1097-0290(19971105)56:3<340::AID-BIT12>3.0.CO;2-K· OSTI ID:566368

Wescott, C R; Klibanov, A M ^[1]

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1. Massachusetts Inst. of Tech., Cambridge, MA (United States). Dept. of Chemistry

A simple methodology has been successfully employed to explain the solvent dependence of the substrate specificity of enzymes in organic media. This methodology, which does not require the knowledge of the enzyme structure and is thus applicable to lyophilized and other noncrystalline enzyme preparations, predicts that the k{sub cat}/K{sub M} ratio for two substrates should be proportional to their Raoult`s law activity coefficients. This approach has been validated for two enzymes, subtilisin Carlsberg and {alpha}-chymotrypsin, catalyzing the propanolysis of unnatural (in addition to natural) ester substrates in a variety of anhydrous solvents.

• Sponsoring Organization: USDOE, Washington, DC (United States)
• OSTI ID: 566368
• Journal Information: Biotechnology and Bioengineering, Journal Name: Biotechnology and Bioengineering Journal Issue: 3 Vol. 56; ISSN BIBIAU; ISSN 0006-3592
• Country of Publication: United States
• Language: English

Related Subjects

54 ENVIRONMENTAL SCIENCES
BIODEGRADATION
BIOTECHNOLOGY
IMMOBILIZED ENZYMES
ORGANIC SOLVENTS
REMEDIAL ACTION
SERINE PROTEINASES
SPECIFICITY
SUBSTRATES