Transcriptional analysis of the β-galactosidase gene (pbg) inClostridium perfringens [PDF]
FEMS Microbiology Letters, 1995 The mode of expression of the beta-galactosidase gene (pbg) of Clostridium perfringens was examined. The pbg gene was transcribed on a single 3.7-kb mRNA. The transcript contained a message for ORF54, located upstream of the pbg gene in the chromosome, indicating that ORF54 and the pbg gene comprise one operon (pbg operon). Expression of the pbg operon
T, Kobayashi, T, Shimizu, H, Hayashi
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Thermostable α-galactosidase fromBacillus stearothermophilusNUB3621: cloning, sequencing and characterization [PDF]
FEMS Microbiology Letters, 1999 An alpha-galactosidase gene from the thermophilic bacterium Bacillus stearothermophilus NUB3621 was cloned, sequenced, expressed in Escherichia coli and the recombinant protein was purified. The Bacillus enzyme, designated AgaN, is similar to alpha-galactosidases of family 36 in the classification of glycosyl hydrolases.
O, Fridjonsson +3 more
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Anaerobic expression of thegyrAgene demonstrated by β-galactosidase activity ingyrA::Mu-lacfusion derivatives ofEscherichia coli [PDF]
FEMS Microbiology Letters, 1988 E. coli C600Δ lac was infected with a Mu- lac defective phage. Lysogens resistant to ampicillin (25 µg/ml) and nalidixic acid (20 µg/ml) were unable to grow anaerobically and insensitive to nalidixic acid (150 µg/ml), indicating formation of gyrA ::Mu- lac fusions.
Nobuto Yamamoto, Mary L. Droffner
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Experimental conditions may affect reproducibility of the beta-galactosidase assay [PDF]
FEMS Microbiology Letters, 1992 Several experimental conditions and parameters contributing to the determination of beta-galactosidase activity, as proposed in Miller's assay, were studied. Use of the absorbance correction factor and the nature and concentration of permeabilizing agents were taken into account as different experimental conditions.
GIACOMINI, ALESSIO +4 more
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Cloning of the phospho-β-galactosidase gene inEscherichia colifrom lactose-negative mutants ofStreptococcus mutansisolated following random mutagenesis with plasmid pVA891 clone banks [PDF]
FEMS Microbiology Letters, 1992 In order to mutagenize Streptococcus mutans a marker rescue plasmid, pVA891, was employed. The plasmid was ligated with Sau3AI digested chromosomal DNA fragments from S. mutans GS-5IS3 and the resultant plasmids were amplified in Escherichia coli.
Yutaka Sato +3 more
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A data comparison between a traditional and the single-step β-galactosidase assay
Data in Brief, 2016 This article describes reproducibility of a single-step automated β-galactosidase, and the equivalence of its data to the traditional assay (“Experiments in Molecular Genetics” [1]).
Jorrit Schaefer +3 more
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β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release [PDF]
Anais da Academia Brasileira de Ciências, 2020 The present study investigated the encapsulation of β-galactosidase in carrageenan, pectin and its hybrid hydrogels by using the ionotropic gelation method.
RENATA CRISTINA SILVA +2 more
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Characterization and molecular cloning of a heterodimeric β-galactosidase from the probiotic strainLactobacillus acidophilusR22 [PDF]
FEMS Microbiology Letters, 2007 Beta-galactosidase from the probiotic strain Lactobacillus acidophilus R22 was purified to apparent homogeneity by ammonium sulphate fractionation, hydrophobic interaction, and affinity chromatography. The enzyme is a heterodimer consisting of two subunits of 35 and 72 kDa, as determined by gel electrophoresis.
Thu-Ha, Nguyen +6 more
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Screening of β-galactosidase enzyme production by probiotic lactic acid bacteria isolated from raw and fermented milk [PDF]
Archives of Agriculture Sciences Journalβ-Galactosidase is a glycoside hydrolase enzyme that catalyzes the hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides. This study aimed to isolate β-galactosidase-producing bacteria from different types of milk.
M. Hassan, M. Hussein, E. Bakhiet
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Antigenicity of a viral peptide displayed on β-galactosidase fusion proteins is influenced by the presence of the homologous partner protein [PDF]
FEMS Microbiology Letters, 1996 Several beta-galactosidase fusion proteins have been constructed containing the entire VP1 protein from foot-and-mouth disease virus (FMDV) [Corchero et al. (1996) J. Biotechnol. in press]. The antigenicity of the major immunodominant site A (13 amino acids in length) within the VP1 protein has been studied in competitive ELISA using a panel of seven ...
J L, Corchero, A, Villaverde
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