Organic solvents for bioorganic synthesis: 1. Optimization of parameters for a chymotrypsin catalyzed process

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Abstract

The influence of solvents on enzymatic activity and stability was investigated. As a model reaction the α-chymotrypsin-catalyzed esterification of N-acetyl-l-phenylalanine with ethanol was used. The enzyme was adsorbed on porous glass beads and used in various solvents. Small amounts of water were added to increase the enzymatic activity. These enzyme preparations obeyed. Michaelis-Menten kinetics. Km,app decreased slightly with the log P value of the solvent while Vapp increased markedly with the log P value. Log P values were also useful for generalizing the influence of solvents on enzyme stability. The enzyme preparations showed a markedly higher thermostability in dry solvents having log P values >0.7 than in less hydrophobic solvents. Also the operational stability was better in the more hydrophobic solvents. The amount of water added to the enzyme preparations greatly influenced the initial reaction rates. For some solvents optimal water contents were determined. The thermostability decreased with increasing water content. The observations are summarized in the conclusion that more hydrophobic solvents are preferable to less hydrophobic ones. The log P value gives a good guidance when selecting an organic solvent for enzymatic conversions.

Detaljer

Författare
Enheter & grupper
Externa organisationer
  • Lund University
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biokatalys och enzymteknik
Originalspråkengelska
Sidor (från-till)1-8
Antal sidor8
TidskriftApplied Microbiology and Biotechnology
Volym26
Utgåva nummer1
StatusPublished - 1987 apr 1
PublikationskategoriForskning
Peer review utfördJa