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Extracellular proteinase fromLactobacillus murinus

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Abstract

Lactobacillus murinus CNRZ 313 produced an extracellular proteinase irrespective of the Ca2+ content in the culture medium. Proteinase activity was optimal at 37 °C and pH 7.5 in phosphate buffer (0.2 mol/L). It was stimulated by Mg2+ and Mn2+ and was inhibited by Zn2+. Ca2+ did not affect the enzymic activity but the proteinase liberated in the presence of this ion is more stable. The enzyme was purified to homogeneity from cell-free culture medium.

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We want to thank Ms Ana María de Angelis de Comotti for her technical assistance. This work was partially supported by grants from CONICET and SECYT Argentina 1985.

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Strasser De Saad, A.M., Manca De Nadra, M.C., Pesce De Ruiz Holgado, A. et al. Extracellular proteinase fromLactobacillus murinus . Folia Microbiol 33, 96–100 (1988). https://doi.org/10.1007/BF02928074

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