• DOI:10.1007/978-94-011-0611-5_3
• Corpus ID: 102139832

Fundamentals of non-aqueous enzymology

@inproceedings{Yang1996FundamentalsON,
  title={Fundamentals of non-aqueous enzymology},
  author={Z. Yang and Alan J. Russell},
  year={1996}
}

• Z. Yang, A. Russell
• Published 1996
• Chemistry

Non-aqueous enzymology is such a rapidly developing research area that it has attracted interest from chemists, biochemists and chemical engineers. This has been reflected by an explosive growth of the literature (for reviews see Dordick, 1989; Klibanov, 1989; Blinkovsky et al., 1992; Russell et al., 1992; Halling, 1994). It is generally accepted that when enzymes are placed in organic media, they exhibit altered properties such as enhanced thermostability (Ayala et al., 1986; Wheeler and Croteau, 1986), altered specificity (see review by Wescott and Klibanov, 1994), molecular memory (Stahl et al., 1991; Dabulis and Klibanov, 1993), and the ability to catalyze reactions that are kinetically or thermodynamically impossible in aqueous solution (Kuhl et al., 1990; West et al., 1990). In addition, the industrial utility of biocatalysts is enhanced because of the increased solubility of hydrophobic substrates, ease of product and enzyme recovery, and reduced risk of microbial contamination of reactors. In order to take full advantage of these perceived benefits of non-aqueous enzymology, we must first understand the fundamental interaction between a solvent and an enzyme. The structural and mechanistic integrity of the protein, the role of water and solvents on activity, and the specific solvent effects on the kinetics and thermodynamics of enzyme-catalyzed processes, are all central to the development of our understanding of non-aqueous enzymology and its applications.