Cloning of the phospho-β-galactosidase gene inEscherichia colifrom lactose-negative mutants ofStreptococcus mutansisolated following random mutagenesis with plasmid pVA891 clone banks [PDF]
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
openaire +1 more source
A data comparison between a traditional and the single-step β-galactosidase assay
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
doaj +1 more source
Screening of β-galactosidase enzyme production by probiotic lactic acid bacteria isolated from raw and fermented milk [PDF]
β-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
doaj +1 more source
β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release [PDF]
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
doaj +1 more source
Characterization and molecular cloning of a heterodimeric β-galactosidase from the probiotic strainLactobacillus acidophilusR22 [PDF]
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
openaire +2 more sources
Antigenicity of a viral peptide displayed on β-galactosidase fusion proteins is influenced by the presence of the homologous partner protein [PDF]
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
openaire +2 more sources
High gene expression inEscherichia coliof recombinant alginate lyase as a fused protein with β-galactosidase α-peptide [PDF]
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
openaire +2 more sources
Lactobacillus fermentumCRL 722 is able to deliver active α-galactosidase activity in the small intestine of rats [PDF]
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
openaire +6 more sources
Background The spore-forming lactic acid bacterium Bacillus coagulans MA-13 has been isolated from canned beans manufacturing and successfully employed for the sustainable production of lactic acid from lignocellulosic biomass. Among lactic acid bacteria,
Martina Aulitto +9 more
semanticscholar +1 more source
The vast majority of proteins functions in complex with one or more of the same or other proteins, indicating that protein−protein interactions play crucial roles in biology.
Bart Devreese (146471) +4 more
core +2 more sources

