Purification of an X-prolyl-dipeptidyl aminopeptidase from the cell wall proteolytic system of Lactococcus lactis subsp. cremoris |
| |
Authors: | Barbara Kiefer-Partsch Wilhelm Bockelmann Arnold Geis Michael Teuber |
| |
Institution: | (1) Bundesanstalt für Milchforschung, Institut für Mikrobiologie, Hermann-Weigmann-Strasse 1, D-2300 Kiel 1, Federal Republic of Germany |
| |
Abstract: | Summary The -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 -casein, as shown by the degradation of -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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|