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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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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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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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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High gene expression inEscherichia coliof recombinant alginate lyase as a fused protein with β-galactosidase α-peptide [PDF]
FEMS Microbiology Letters, 1995 Escherichia coli LE392 (pAL28) was previously isolated as a positive clone harboring the alginate lyase gene (aly) from an alginate-degrading strain, Pseudomonas sp. OS-ALG-9. The plasmid pAL205, one of the constructs obtained after successive subcloning of pAL28, gave the highest expression of aly in E. coli cells.
K, Fujiyama +3 more
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Lactobacillus fermentumCRL 722 is able to deliver active α-galactosidase activity in the small intestine of rats [PDF]
FEMS Microbiology Letters, 2005 alpha-galactooligosaccharides (alpha-GOS) found in legumes such as soybeans can cause gastrointestinal disorders since mammals lack alpha-galactosidase (alpha-Gal) in the small intestine which is necessary for their hydrolysis. Lactobacillus fermentum CRL 722 is a lactic acid bacterium (LAB) capable of degrading alpha-GOS due to its elevated alpha-Gal ...
Leblanc, Jean Guy +3 more
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Evaluation of beta-galactosidase activity in tissue in the presence of blood [PDF]
, 2000 The reporter gene for beta -galactosidase is frequently used to determine the efficiency of gene transfer in arteries. However, blood is often present in arterial explants and may compromise the results by the presence of hemoglobin. The light absorption
Pelisek, Jaroslav +2 more
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Insertion of a 27 amino acid viral peptide in different zones ofEscherichia coliβ-galactosidase: Effects on the enzyme activity [PDF]
FEMS Microbiology Letters, 1994 Seven internal, putatively exposed regions of Escherichia coli beta-galactosidase have been explored regarding their tolerance to insertions of large foreign peptides. Small sequence modifications, including amino acid substitutions and small deletions, were introduced into the lacZ gene to generate unique BamHI restriction sites. By using these mutant
A, Benito, A, Villaverde
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