Abstract:

beta-Galactosidase (beta-gal, EC 3.2.1.23) and beta-D-phosphogalactoside galactohydrolase (beta-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 beta-gal from L. thermophilus and the beta-Pgal from L. casei were purified and characterized. In comparison with beta-gal, the beta-Pal was slightly less active (V(max) values were 28.9 and 50.0 mumoles per mg per min, respectively), but the substrate affinitives were similar (K(m) values were 1.69 x 10(-3) M and 1.59 x 10(-3) M, respectively). Although the two enzymes had similar amino acid compositions, the molecular weight of beta-gal was 5.4 x 10(5) and that of beta-Pgal was 1.3 x 10(5). The beta-gal from L. thermophilus and the beta-Pgal from L. casei had optimal temperature and pH activity values of 55 C at pH 6.2 and 37 C at pH 5.0, respectively. The complete absence of beta-gal from a homofermentative Lactobacillus species of industrial importance is further evidence of the heterogeneity of this genus.

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Lactose-Hydrolyzing Enzymes of <em>Lactobacillus</em> Species<sup><a href="#fn1" rid="fn1" class=" fn">1</a></sup>

L Premi

W Sandine

P Elliker

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^{M and 1.59 × 10}^{M, respectively). Although the two enzymes had similar amino acid compositions, the molecular weight of β-gal was 5.4 × 10}^{and that of β-Pgal was 1.3 × 10}^{. The β-gal from}L. thermophilus and the β-Pgal from L. casei had optimal temperature and pH activity values of 55 C at pH 6.2 and 37 C at pH 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.

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^{Department of Microbiology, Oregon State University, Corvallis, Oregon 97331}

^{Present address: Dairy Research Department, Catholic University of Milan, Piacenza, Italy.}

^{Technical Paper no. 3310, Oregon Agricultural Experiment Station.}

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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^{M and 1.59 × 10}^{M, respectively). Although the two enzymes had similar amino acid compositions, the molecular weight of β-gal was 5.4 × 10}^{and that of β-Pgal was 1.3 × 10}^{. The β-gal from}L. thermophilus and the β-Pgal from L. casei had optimal temperature and pH activity values of 55 C at pH 6.2 and 37 C at pH 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.

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