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In the present experiments, the proteinase, aminopeptidase and x-prolyl-dipeptidyl aminopeptidase activitives were measured at 513±11.9, 376±9.3 and 23.6±1.6 units per gramme of cell-free extract of Lactobacillus helveticus JCM1004. ACE-inhibitory activity of skimmed milk hydrolysate produced by cell-free extract of L. helveticus JCM1004 was determined, and the optimum pH and hydrolysis time for the...
An aminopeptidase was purified to homogeneity from a cell-free extract of Lactobacillus helveticus JCM 1004 by ammonium sulfate precipitation and chromatography on DEAE-Sepharose, Sephacryl S-300 HR, HiLoad 26/60 Superdex 200pg and Mono-Q 10/10. The purified aminopeptidase had a trimeric structure and a molecular mass of ~129 kDa. The enzyme was optimally active at pH 7.0 and 40 o C. The enzyme...
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