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Hydrolysis of β-casein(193-209) Fragment by Whole Cells and Fractions of lactobacillus casei an Lactococcus lactis

机译:β-酪蛋白(193-209)片段的水解及干酪乳杆菌乳球菌各部分的水解

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摘要

Whole cells and fractions of Lactococcus lactis subsp. lac- tis IFPL 359 and Lactobacillus casei subsp. casie IFPL731 wer studied. Hydrolysis productes were separated by re- versed-phase, high-performance liquid chromatogaphy (RP- HPLC). Under conditions, pH 5.2 and 3 /100 NaCl, L. casei IFPL 731 was more active in hydrolysis of the β-casein (f193-209) peptide than was L. lactis IFPL 359. This hydrolyzing activ- ity was attributed for L. casei IFPL 731 by the cell-wall pro- teinase.
机译:乳酸乳球菌亚种的全细胞和部分。乳酸IFPL 359和干酪乳杆菌亚种。 casie IFPL731进行了研究。通过反相高效液相色谱(RP-HPLC)分离水解产物。在pH 5.2和3/100 NaCl的条件下,干酪乳杆菌IFPL 731在水解β-酪蛋白(f193-209)肽方面比乳酸乳杆菌IFPL 359更有活性。这种水解活性归因于乳杆菌。酪蛋白IFPL 731是细胞壁蛋白酶。

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