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

Reslow, Mats ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1987) In Applied Microbiology and Biotechnology 26(1). p.1-8
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... (More)

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.

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type
Contribution to journal
publication status
published
subject
in
Applied Microbiology and Biotechnology
volume
26
issue
1
pages
8 pages
publisher
Springer
external identifiers
  • scopus:0023220250
ISSN
0175-7598
DOI
10.1007/BF00282141
language
English
LU publication?
yes
id
08db549d-d273-4b50-9f95-b31ceb25b1f8
date added to LUP
2019-06-22 19:01:47
date last changed
2021-01-03 04:45:28
@article{08db549d-d273-4b50-9f95-b31ceb25b1f8,
  abstract     = {{<p>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. K<sub>m,app</sub> decreased slightly with the log P value of the solvent while V<sub>app</sub> 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 &gt;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.</p>}},
  author       = {{Reslow, Mats and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0175-7598}},
  language     = {{eng}},
  month        = {{04}},
  number       = {{1}},
  pages        = {{1--8}},
  publisher    = {{Springer}},
  series       = {{Applied Microbiology and Biotechnology}},
  title        = {{Organic solvents for bioorganic synthesis : 1. Optimization of parameters for a chymotrypsin catalyzed process}},
  url          = {{http://dx.doi.org/10.1007/BF00282141}},
  doi          = {{10.1007/BF00282141}},
  volume       = {{26}},
  year         = {{1987}},
}