Results 1 to 10 of about 19,658 (332)

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

open access: goldBiomolecules, 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   +2 more sources

Identification and characterization of a novel β-galactosidase active at low temperatures from the Antarctic fungus Tetracladium sp., expressed in Saccharomyces cerevisiae [PDF]

open access: yesMicrobial Cell Factories
Background β-Galactosidases are widely used in the dairy industry to produce lactose-free milk and prebiotics such as galacto-oligosaccharides and lactulose.
Fernando Gutierrez   +3 more
doaj   +2 more sources

Synthesis of Oligosaccharides Derived from Lactulose (OsLu) Using Soluble and Immobilized Aspergillus oryzae β-Galactosidase [PDF]

open access: gold, 2016
β-Galactosidase from Aspergillus oryzae offers a high yield for the synthesis of oligosaccharides derived from lactulose (OsLu) by transgalactosylation.
Batista-Viera, F.   +6 more
core   +6 more sources

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

Cold-Active β-Galactosidases: Insight into Cold Adaptation Mechanisms and Biotechnological Exploitation

open access: yesMarine Drugs, 2021
β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor.
Marco Mangiagalli, Marina Lotti
doaj   +1 more source

Proteomic analysis of Bifidobacterium longum subsp. infantis reveals the metabolic insight on consumption of prebiotics and host glycans. [PDF]

open access: yes, 2013
Bifidobacterium longum subsp. infantis is a common member of the intestinal microbiota in breast-fed infants and capable of metabolizing human milk oligosaccharides (HMO).
An, Hyun Joo   +5 more
core   +7 more sources

Infant-Associated Bifidobacterial β-Galactosidases and Their Ability to Synthesize Galacto-Oligosaccharides

open access: yesFrontiers in Microbiology, 2021
Galacto-oligosaccharides (GOS) represent non-digestible glycans that are commercially produced by transgalactosylation of lactose, and that are widely used as functional food ingredients in prebiotic formulations, in particular in infant nutrition.
Valentina Ambrogi   +14 more
doaj   +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

Role of glycosylation in secretion and stability of micromycetes α-galactosidase [PDF]

open access: yesThe Ukrainian Biochemical Journal, 2014
The effect of the glycosylation inhibitors (tunicamycin and 2-deoxy-D-glucose) on the activity, stabili­ty and production of fungal glycosidases has been studied.
N. V. Borzova   +2 more
doaj   +1 more source

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