Nucleotide sequence of the LacN gene encoding thermostable β-galactosidase of a thermophilic anaerobe, strain NA10

Saito, Takao; Kato, Katsuya; Suzuki, Tohru; Iijima, Shinji; Kobayashi, Takeshi

doi:10.1016/0922-338x(92)90231-i

Journal of Fermentation and Bioengineering

1992

DOI: 10.1016/0922-338x(92)90231-i

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Nucleotide sequence of the LacN gene encoding thermostable β-galactosidase of a thermophilic anaerobe, strain NA10

Takao Saito¹,

Katsuya Kato²,

Tohru Suzuki³

et al.

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Cited by 5 publications

(1 citation statement)

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“…Some papers present enzyme properties but do not contain sequence data (2,7,29). Others report sequences but often contain rudimentary enzymatic characterization (20,32). The biochemical characterization and evolutionary relatedness of these enzymes is rarely discussed in the same forum.…”

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confidence: 99%

Biochemical and Phylogenetic Analyses of a Cold-Active β-Galactosidase from the Lactic Acid Bacterium Carnobacterium piscicola BA

Coombs

Brenchley

1999

Appl Environ Microbiol

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We are investigating glycosyl hydrolases from new psychrophilic isolates to examine the adaptations of enzymes to low temperatures. A β-galactosidase from isolate BA, which we have classified as a strain of the lactic acid bacterium Carnobacterium piscicola, was capable of hydrolyzing the chromogen 5-bromo-4-chloro-3-indolyl β-d-galactopyranoside (X-Gal) at 4°C and possessed higher activity in crude cell lysates at 25 than at 37°C. Sequence analysis of a cloned DNA fragment encoding this activity revealed a gene cluster containing three glycosyl hydrolases with homology to an α-galactosidase and two β-galactosidases. The larger of the two β-galactosidase genes, bgaB, encoded the 76.8-kDa cold-active enzyme. This gene was homologous to family 42 glycosyl hydrolases, a group which contains several thermophilic enzymes but none from lactic acid bacteria. The bgaB gene from isolate BA was subcloned in Escherichia coli, and its enzyme, BgaB, was purified. The purified enzyme was highly unstable and required 10% glycerol to maintain activity. Its optimal temperature for activity was 30°C, and it was inactivated at 40°C in 10 min. TheKm of freshly purified enzyme at 30°C was 1.7 mM, and the V max was 450 μmol · min−1 · mg−1 with o-nitrophenyl β-d-galactopyranoside. This cold-active enzyme is interesting because it is homologous to a thermophilic enzyme fromBacillus stearothermophilus, and comparisons could provide information about structural features important for activity at low temperatures.

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confidence: 99%

Biochemical and Phylogenetic Analyses of a Cold-Active β-Galactosidase from the Lactic Acid Bacterium Carnobacterium piscicola BA

Coombs

Brenchley

1999

Appl Environ Microbiol

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Immobilization and characterization of a thermostable β-galactosidase from a thermophilic anaerobe on a porous ceramic support

Saito¹,

Yoshida

Kawashima³

et al. 1994

Appl Microbiol Biotechnol

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Overproduction of thermostable β-galactosidase in Escherichia coli, its purification and molecular structure

Saito

Kato

Maeda

et al. 1992

Journal of Fermentation and Bioengineering

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Nucleotide sequence of the LacN gene encoding thermostable β-galactosidase of a thermophilic anaerobe, strain NA10

Cited by 5 publications

References 10 publications

Biochemical and Phylogenetic Analyses of a Cold-Active β-Galactosidase from the Lactic Acid Bacterium Carnobacterium piscicola BA

Biochemical and Phylogenetic Analyses of a Cold-Active β-Galactosidase from the Lactic Acid Bacterium Carnobacterium piscicola BA

Immobilization and characterization of a thermostable β-galactosidase from a thermophilic anaerobe on a porous ceramic support

Overproduction of thermostable β-galactosidase in Escherichia coli, its purification and molecular structure

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