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Partial purification and some properties of øC2(W) lysin, a lytic enzyme produced by phage-infected cells of Streptococcus lactis C2

Published online by Cambridge University Press:  01 June 2009

W. Michael A. Mullan  and
Robert J. M. Crawford
W. Michael A. Mullan
Affiliation:
Department of Dairy Technology, West of Scotland Agricultural College, AyrScotland
Robert J. M. Crawford
Affiliation:
Department of Dairy Technology, West of Scotland Agricultural College, AyrScotland
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Summary

The lytic enzyme present in øC2(W) lysates was isolated by means of ion-exchange chromatography and further purified by gel filtration and ultrafiltration. The phage enzyme had an apparent pH optimum of 6·5–6·9 and was rapidly inactivated at temperatures > 47°C. The apparent temperature optimum was 37°C and Q10 and Ea values over the range 22–32°C were 2·5 and 69·2 kJ/mol respectively. Monovalent and divalent cations activated the enzyme. Reduced -SH groups on the enzyme were required for lytic activity. Gel filtration revealed a mol. wt of ˜ 46000. Strain-dependent differences in sensitivity of group N lactic streptococci to lysin were found. Group D streptococci were also lysed. Strains of three species of Leuconostoc, two species of Lactobacillus, one strain of Escherichia coli and of Micrococcus lysodeikticus were apparently resistant. Analysis of cell wall degradation products gave results which were consistent with the lysin having the specificity of an N-acetylmuramidase.

Type
Original Articles
Information
Journal of Dairy Research , Volume 52 , Issue 1 , February 1985 , pp. 123 - 138
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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