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Effect of membrane perturbing treatments on the membrane-bound peptidases of Streptococcus cremoris HP

Published online by Cambridge University Press:  01 June 2009

Fred A. Exterkate
Fred A. Exterkate
Affiliation:
Netherlands Institute for Dairy Research (NIZO), Ede, The Netherlands
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Summary

The effects of solubilization, treatment with organic solvents and storage under alkaline conditions on membrane-associated peptidases of intact cells of Streptococcus cremoris HP were studied. Differences in the response of the peptidase activities towards these membrane perturbing treatments were observed. Pyrrolidonecarboxylylpeptidase (PCP) and an endopeptidase (P50) showed 50% irreversible inhibition at the same concentration of each solvent tested. An amino- and proline iminopeptidase activity and the endopeptidase P37 were in this respect much more sensitive to the action of the solvents. Within a homologous series of n-alkanols irreversible inhibition of PCP showed a dependence on the hydrophobicity of the solvent molecules. Only P37 activity was increased considerably upon solubilization of the enzyme. Similar levels of activation were found upon treatment of cells with 3% (v/v) n-butanol at 25 °C or storage at 30 °C at an alkaline pH. Optimal activity of P50 during n-butanol treatment was at 25 °C using a concentration of 5% (v/v), but no activation was observed upon solubilization. The results are discussed in terms of enzyme–lipid interaction and accessibility of the enzymes in situ. It is concluded that the enzymes apparently occupy different positions within the membrane although they may together constitute a functional peptide-hydrolysing unit.

Type
Original Articles
Information
Journal of Dairy Research , Volume 46 , Issue 3 , July 1979 , pp. 473 - 484
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

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