Results 51 to 60 of about 5,064 (210)

Transglycosylation Activity ofDictyoglomus thermophilumAmylase A

open access: yesBioscience, Biotechnology, and Biochemistry, 2004
Amylase A from Dictyoglomus thermophilum is a thermophilic enzyme and has about 40% identity with 4-alpha-glucanotransferase (GTase) from Thermococcus litoralis, and both of these enzymes belong to family 57 glycosyl hydrolase. Since the transglycosylation activity of T.
NAKAJIMA, Masahiro   +4 more
openaire   +2 more sources

Cryo‐EM structure of GH43 β‐Xylosidase from Enterobacter cloacae provides insights into substrate specificity and the role of an auxiliary domain in enzymatic activity

open access: yesThe FEBS Journal, EarlyView.
Xylan, the second most abundant plant cell wall polysaccharide, is degraded by β‐xylanases and β‐xylosidases. Here, we present the 2.65 Å cryo‐EM structure of Enterobacter cloacae β‐xylosidase (EcXyl43, GH43) and the 2.4 Å X‐ray structure of its inactive F507A mutant.
Lorenzo Briganti   +8 more
wiley   +1 more source

Screening Systems for Detecting Inhibitors of Cell Wall Transglycosylation in Enterococcus.Cell Wall Transglycosylation Inhibitors in Enterococcus.

open access: yesThe Journal of Antibiotics, 1998
We devised two screening systems to detect cell wall transglycosylation inhibitors. One screen utilizes a mutant of Enterococcus faecalis strain A256 that is dependent on vancomycin or moenomycin for growth. In the absence of transglycosylation inhibitors the strain fails to grow, while in the presence of inhibitors, cells are rescued.
N, Mani   +10 more
openaire   +3 more sources

Shaping the Infant Microbiome With Non-digestible Carbohydrates

open access: yesFrontiers in Microbiology, 2019
Natural polysaccharides with health benefits are characterized by a large structural diversity and differ in building blocks, linkages, and lengths. They contribute to human health by functioning as anti-adhesives preventing pathogen adhesion, stimulate ...
Stella Verkhnyatskaya   +3 more
doaj   +1 more source

N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs

open access: yesFrontiers in Bioengineering and Biotechnology, 2020
Nucleoside-2′-deoxyribosyl-transferases (NDTs) catalyze a transglycosylation reaction consisting of the exchange of the 2′-deoxyribose moiety between a purine and/or pyrimidine nucleoside and a purine and/or pyrimidine base.
Javier Acosta   +5 more
doaj   +1 more source

Safety evaluation of the food enzyme cyclomaltodextrin glucanotransferase from the genetically modified Escherichia coli K12 strain DSM 34230

open access: yesEFSA Journal, Volume 24, Issue 10, October 2026.
Abstract The food enzyme cyclomaltodextrin glucanotransferase (1,4‐α‐d‐glucan 4‐α‐d‐[1,4α‐d‐glucano]‐transferase (cyclising); EC 2.4.1.19) is produced with the genetically modified strain Escherichia coli K12 DSM 34230 by Wacker Chemie AG. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Enzymes (FEZ)   +23 more
wiley   +1 more source

Purification and characterization of a novel glycosidase from the China white jade snail (Achatina fulica) showing transglycosylation activity

open access: yes, 2008
A broad specificity beta-D-glycosidase, designated G1, was purified to homogeneity from the viscera of the China white jade snail (Achatina fulica). The enzyme was a monomeric protein with molecular weight of 115 kDa.
Zhou, Kun   +6 more
core   +1 more source

Cyclodextrin Glycosyl Transferase and its application in industries

open access: yesJurnal Teknologi dan Industri Pangan, 2010
Cyclodextrin glycosyl transferase (CGT-ase) is mainly produced by Bacilli. Systematical name of the enzyme is E.C. 2.4.1.19 -1,4 glucan-4-glycosyl transferase.
Budiasih Wahyuntari
doaj  

A Novel Dimeric Exoglucanase (GH5_38): Biochemical and Structural Characterisation towards its Application in Alkyl Cellobioside Synthesis

open access: yesMolecules, 2020
An exoglucanase (Exg-D) from the glycoside hydrolase family 5 subfamily 38 (GH5_38) was heterologously expressed and structurally and biochemically characterised at a molecular level for its application in alkyl glycoside synthesis.
Mpho S. Mafa   +5 more
doaj   +1 more source

A BROAD-SPECIFICITY Β-GLUCOSIDASE FROM A WILD TYPE OF YEAST ISOLATE AND ITS POTENTIAL USE IN FOOD INDUSTRY [PDF]

open access: yesJournal of Food and Dairy Sciences, 2007
A novel intracellular β-glucosidase was isolated from a wild type of yeast Trichosporon sp. Production of enzyme was stimulated with highest level of production in medium containing 1 % lactose as a sole carbon source at pH 7 and 30 oC for 48 hr.
M. Salem, M. Korish
doaj   +1 more source

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