Results 11 to 20 of about 2,910 (220)

Structure and function of a β-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium [PDF]

open access: yesCommunications Biology
Galactosides are major carbohydrates that are found in plant cell walls and various prebiotic oligosaccharides. Studying the detailed biochemical functions of β-galactosidases in degrading these carbohydrates is important.
Yutaka Nakazawa   +14 more
doaj   +2 more sources

A robust enzymatic reporter system for the extremely thermophilic anaerobic bacterium Anaerocellum bescii [PDF]

open access: yesFrontiers in Microbiology
Thermophilic anaerobic organisms, particularly species that can naturally degrade lignocellulosic biomass, show great promise for next generation bioprocessing.
Joey L. Galindo   +6 more
doaj   +2 more sources

In vitro investigations on the impact of fermented dairy constituents on fecal microbiota composition and fermentation activity [PDF]

open access: yesMicrobiology Spectrum
Fermented dairy constitutes a major dietary source and contains lactose as the main carbohydrate and living starter cultures, which can encounter the intestinal microbiota after ingestion.
Qing Li   +6 more
doaj   +2 more sources

Purification and characterization of a β-galactosidase fromSclerotinia sclerotiorum [PDF]

open access: yesFEMS Microbiology Letters, 1992
Sclerotinia sclerotiorum secretes β-galactosidase, giving very low activity when cultivated in a medium with glucose as the carbon source. This production is greatly enhanced during growth on different pectin related polysaccharides. An extracellular β-galactosidase was purified 26-fold by ammonium sulfate precipitation, gel filtration and ion exchange
Christine Riou   +2 more
openaire   +1 more source

The occurrence of β-galactosidase and β-phosphogalactosidase inLactobacillus caseistrains [PDF]

open access: yesFEMS Microbiology Letters, 1984
Several strains of Lactobacillus casei of different origins were compared and it was observed that lactose metabolism varied from one strain to the other. Certain strains contained a β-galactosidase, others a β-phosphogalactosidase and others contain both.
J. Jimeno, M. Casey, F. Hofer
openaire   +1 more source

Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). [PDF]

open access: yesPLoS ONE, 2016
In this work we report a detailed analysis of the topology and phylogenetics of family 2 glycoside hydrolases (GH2). We distinguish five topologies or domain architectures based on the presence and distribution of protein domains defined in Pfam and ...
David Talens-Perales   +4 more
doaj   +1 more source

Galacto-Oligosaccharide (GOS) Synthesis during Enzymatic Lactose-Free Milk Production: State of the Art and Emerging Opportunities

open access: yesBeverages, 2022
Much attention has recently been paid to β-Galactosidases (β-D-galactoside galactohidrolase; EC 3.2.1.23), commonly known as lactases, due to the lactose intolerance of the human population and the importance of dairy products in the human diet.
Katia Liburdi, Marco Esti
doaj   +1 more source

Identification, Characterization, and Expression of a β-Galactosidase from Arion Species (Mollusca)

open access: yesBiomolecules, 2022
β-Galactosidases (β-Gal, EC 3.2.1.23) catalyze the cleavage of terminal non-reducing β-D-galactose residues or transglycosylation reactions yielding galacto-oligosaccharides.
Julia Thoma   +3 more
doaj   +1 more source

Effect of tunicamycin on α-galactosidase secretion byAspergillus nidulansand the importance ofN-glycosylation [PDF]

open access: yesFEMS Microbiology Letters, 1994
Aspergillus nidulans released α-galactosidase into the culture medium during the exponential growth on either lactose or galactose as the only carbon source. This enzyme is a glycoprotein. Its treatment with endoglycosidases produces a reduction in its molecular mass but the resulting enzyme conserved some of their carbohydrate components in addition ...
Santiago Ríos   +2 more
openaire   +1 more source

Thermostable α-galactosidase fromThermotoga neapolitana: cloning, sequencing and expression [PDF]

open access: yesFEMS Microbiology Letters, 1998
A gene encoding a thermostable alpha-galactosidase from the hyperthermophile Thermotoga neapolitana was cloned and sequenced. Sequence analysis showed that the 552-amino acid protein is similar to Escherichia coli Raf type alpha-galactosidase and belongs to Family 36 of the glycosyl hydrolases. Recombinant alpha-galactosidase expressed in E. coli has a
M R, King   +3 more
openaire   +2 more sources

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