Summary
The β-casein specific cell wall proteolytic system of Lactococcus lactis subsp. cremoris P8-2-47 contains a metal-independent X-prolyl-dipeptidyl-aminopeptidase. Suitable substrates for its assay are Gly-Pro-nitroanilide and Ala-Pronitroanilide. It is suggested that the function of the enzyme is to cleave the proline-rich sequences of β-casein, as shown by the degradation of β-casomorphin. It is a serine proteinase with a monomer molecular mass of about 90 000 daltons, a temperature optimum of 45°–50°C, and a pH optimum of about 7.
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Kiefer-Partsch, B., Bockelmann, W., Geis, A. et al. Purification of an X-prolyl-dipeptidyl aminopeptidase from the cell wall proteolytic system of Lactococcus lactis subsp. cremoris . Appl Microbiol Biotechnol 31, 75–78 (1989). https://doi.org/10.1007/BF00252531
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DOI: https://doi.org/10.1007/BF00252531