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- W1556080378 abstract "β-Galactosidase (β-gal, EC 3.2.1.23) and β-D-phosphogalactoside galactohydrolase (β-Pgal) activities were observed in all of 13 Lactobacillus species studied except L. casei and L. buchneri . Only the latter enzyme was detected in nine strains of L. casei . The β-gal from L. thermophilus and the β-Pgal from L. casei were purified and characterized. In comparison with β-gal, the β-Pal was slightly less active ( V max values were 28.9 and 50.0 μmoles per mg per min, respectively), but the substrate affinitives were similar ( K m values were 1.69 × 10 -3 M and 1.59 × 10 -3 M, respectively). Although the two enzymes had similar amino acid compositions, the molecular weight of β-gal was 5.4 × 10 5 and that of β-Pgal was 1.3 × 10 5 . The β-gal from L. thermophilus and the β-Pgal from L. casei had optimal temperature and p H activity values of 55 C at p H 6.2 and 37 C at p H 5.0, respectively. The complete absence of β-gal from a homofermentative Lactobacillus species of industrial importance is further evidence of the heterogeneity of this genus." @default.
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- W1556080378 date "1972-07-01" @default.
- W1556080378 modified "2023-10-18" @default.
- W1556080378 title "Lactose-Hydrolyzing Enzymes of <i>Lactobacillus</i> Species" @default.
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- W1556080378 doi "https://doi.org/10.1128/am.24.1.51-57.1972" @default.
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