1887

Abstract

The exudate of fully germinated spores of IFO 13597 in 0.25 M sodium phosphate buffer, pH 7·0, was found to contain a spore-lytic enzyme. This enzyme was found to cause loss of absorbance in coat-stripped spore suspensions and phase-darkening of the spores but had minimal activity on isolated peptidoglycan substrates. The enzyme was purified in an active form and identified as a 24 kDa protein which is either an amidase or a peptidase. The amino-terminal 19 residues had the following sequence: FSNQVIQRGASGEKVIELQ. The spore-lytic enzyme retained its activity in a medium of a relatively high ionic strength containing a non-ionic surfactant such as nonaethyleneglycol -dodecyl ether. This activity was optimum at a salt concentration of about 30 mM in assay buffer at neutral pH. In contrast to the enzyme in a spore-bound form, the enzyme in solution was shown to be heat-sensitive and was readily inactivated by thiol reagents.

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/content/journal/micro/10.1099/00221287-140-6-1403
1994-06-01
2019-11-14
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-140-6-1403
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