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Abstract
Proline iminopeptidase was purified 76-fold from crude cell-free extracts of Lactobacillus casei ssp. casei LLG by ion-exchange chromatography (preparative and analytical) and gel filtration chromatography using fast protein liquid chromatography. The purified enzyme appeared as a single band on native- and SDS-PAGE and had a molecular mass of 46 kDa. Enzyme activity was maximal at pH 7.5 and 40°C with proline amino-methyl coumarin as substrate. The activity was inhibited by Fe3+ and Hg2+ ions. This enzyme evidently was sulfhydryl; p-chloromercuribenzoate caused complete inhibition at 10mM. The Michaelis-Menten constant and maximum velocity were .6mM and 1.7 nM/mg per min respectively, using the same substrate. This enzyme showed the ability to cleave the Pro-Pro bond, which is of significant importance in cheese ripening.
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