NDLI: Effects of Alcohols and Compatible Solutes on the Activity of β-Galactosidase

Content Provider	Springer Nature Link
Author	Bell, Andrew N. W. Magill, Emma Hallsworth, John E. Timson, David J.
Copyright Year	2012
Abstract	During alcoholic fermentation, the products build up and can, ultimately, kill the organism due to their effects on the cell’s macromolecular systems. The effects of alcohols on the steady-state kinetic parameters of the model enzyme β-galactosidase were studied. At modest concentrations (0 to 2 M), there was little effect of methanol, ethanol, propanol and butanol on the kinetic constants. However, above these concentrations, each alcohol caused the maximal rate, V $_{max}$, to fall and the Michaelis constant, K $_{m}$, to rise. Except in the case of methanol, the chaotropicity of the solute, rather than its precise chemical structure, determined and can, therefore, be used to predict inhibitory activity. Compounds which act as compatible solutes (e.g. glycerol and other polyols) generally reduced enzyme activity in the absence of alcohols at the concentration tested (191 mM). In the case of the ethanol- or propanol-inhibited β-galactosidase, the addition of compatible solutes was unable to restore the enzyme’s kinetic parameters to their uninhibited levels; addition of chaotropic solutes such as urea tended to enhance the effects of these alcohols. It is possible that the compatible solutes caused excessive rigidification of the enzyme’s structure, whereas the alcohols disrupt the tertiary and quaternary structure of the protein. From the point of view of protecting enzyme activity, it may be unwise to add compatible solutes in the early stages of industrial fermentations; however, there may be benefits as the alcohol concentration increases.
Starting Page	786
Ending Page	794
Page Count	9
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	169
Issue Number	3
e-ISSN	15590291
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-12-30
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Protein denaturation Chaotropic solute Model enzyme Steady-state kinetics Polyol Enzyme flexibility Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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