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.
Similar content being viewed by others
References
Argyle P.J., Mathison G.E., Chandas R.C.: Production of cell-bound proteinase byLactobacillus bulgaricus and its location in the bacterial cell.J. Appl. Bacteriol.41, 175–184 (1976).
Chandan R.C., Argyle P.J., Mathison G.E.: Action ofLactobacillus bulgaricus proteinaso preparations on milk proteins.J.Dairy Sci.65, 1408–1413 (1982).
Citti J.E., Sandine W.E., Elliker P.R.: Some observations on the Hull method for measurement of proteolysis in milk.J. Dairy Sci.46, 337–342 (1963).
Cowman R.A., Speck M.L.: Proteinase enzyme system of lactic streptococci. I. Isolation and partial characterization.J. Appl. Microbiol.15, 851–856 (1967).
Hemme D., Raibaud P., Ducluzeau R., Galpin J.V., Sicar P., Van Heigenoort J.:Lactobacillus murinus n.sp., une nouvelle espéce de la flore dominante autochtone du tube digestif du rat et de la souris.Ann. Microbiol.131A, 297–308 (1980).
Hull M.E.: Studies on milk proteins. II. Colorimetric determination of the partial hydrolysis of the proteins milk.J. Dairy Sci.30, 881–884 (1947).
Law B.A.: Transport and utilization of proteins by bacteria, p. 381–409 inMicroorganisms and Nitrogen Sources (J.W. Payne, Ed.). John Wiley and Sons, Chichester 1980.
Ornstein L., Davis B.J.: Disc electrophoresis.Ann.N.Y.Acad.Sci.121, 321–349 and 404-427 (1964).
Pollock M.R.:Exoenzymes, Vol. IV, p. 121–178 inThe Bacteria (I.C. Gunsalus, R.Y. Stainer, Eds.). Academic Press, New York 1962.
Raibaud P., Galpin J.V., Ducluzeau R., Mocquot G., Oliver G.: La genreLactobacillus dans le tube digestif du rat. I. Caracteres des souches homofermentaires isolées de rats holo et gnotoxéniques.Ann. Microbiol.124A, 83–109 (1973).
Sato Y., Nakashima T.: Studies on the proteolytic action of lactic acid bacteria and their action on casein. I. Sonicated preparation of intracellular protease and their action on casein.J. Agr. Chem. Soc. Japan39, 299–306 (1965).
Searles M.A., Argyle P.J., Chandan R.C., Gordon J.F.: Lipolytic and proteolytic activities of lactic cultures, Vol. 1E, p. 111, inProc. 18th Internal. Dairy Congress, Brief Communication, Sydney 1970.
Strasser de Saad A.M., Manca de Nadra M.C., Pesce de Ruiz Holgado A.A., Oliver G.: Effect of cultural conditions on proteinase production byLactobacillus murinus.Folia Microbiol.32, 85–88 (1987).
Thomas T.D., Jarvis B.D.W., Skipper N.A.: Localization of proteinase(s) near the cell surface ofStreptococcus lactis.J. Bacteriol.118, 329–333 (1974).
Vescovo M., Bottazzi V.: Caratteristiche dei bacilli lattici presenti nelle colture naturali in siero. 6° parte: Localizzazione citologica del sistema proteolytico inL. helveticus.Sciencia e Tecnica Lattiero Casearia30, 434–437 (1979).
Williamson W.T., Tove S.B., Speck M.L.: Extracellular proteinase ofStreptococcus lactis.J.Bacteriol.87, 49–53 (1964).
Author information
Authors and Affiliations
Additional information
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.
Rights and permissions
About this article
Cite this article
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
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02928074