Abstract
The cell-wall crude extract from Lactobacillus casei NCDO 151 was partially purified by DEAE-Sephacel chromatography. Three active fractions were eluted. Two major peaks (eluted with 0.05 M and 0.27 M phosphate buffer) were further investigated. Peak I represented enzymatic activity with an optimum temperature of 40°C, an optimum pH of 7.0 and was strongly inhibited by the serine proteinase inhibitor phenylmethylsulfonylfluoride. Peak II represented an enzymatic activity with an optimum temperature of 45°C, an optimum pH of 7.5 and was totally inhibited by p-hydroxymercuribenzoate. None of the enzymes was affected by the metal chelator ethylenediaminetetraacetic acid at a concentration up to 1 × 10 −2.
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