Results 1 to 10 of about 3,426 (160)

Comprehensive study on transglycosylation of CGTase from various sources

open access: yesHeliyon, 2021
Transglycosylation is the in-vivo or in-vitro process of transferring glycosyl groups from a donor to an acceptor, which is usually performed by enzymatic reactions because of their simplicity, low steric hindrance, high region-specificity, low ...
Chin Hui Lim, Babak Rasti
exaly   +3 more sources

Transglycosylation: A mechanism for RNA modification (and editing?) [PDF]

open access: yesBioorganic Chemistry, 2005
The vast majority of the ca. 100 chemically distinct modified nucleosides in RNA appear to arise via the chemical transformation of a genetically encoded nucleoside. Two notable exceptions are queuosine and pseudouridine, which are incorporated into tRNA via transglycosylation.
George A Garcia
exaly   +3 more sources

A structure-based high-efficiency homogeneous antibody platform by endoglycosidase Sz provides insights into its transglycosylation mechanism [PDF]

open access: yesStructural Dynamics
Monoclonal antibodies (mAbs) have gradually dominated the drug markets for various diseases. Improvement of the therapeutic activities of mAbs has become a critical issue in the pharmaceutical industry.
Chun-Jung Chen
doaj   +2 more sources

Transglycosylation Capabilities of Wild‐Type α‐l‐Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides [PDF]

open access: yesMicrobial Biotechnology
To enhance the yield of l‐fucosylated molecules synthesized via transfucosylation, we employed α‐l‐transfucosidases, enzymes engineered from α‐l‐fucosidases to favour transglycosylation over hydrolysis.
Patricie Vodičková   +8 more
doaj   +2 more sources

Characterization of a β-Galactosidase from Kosakonia oryzendophytica and Its Heterologous Expression in Bacillus subtilis for Galactooligosaccharides Production [PDF]

open access: yesMolecules
Galactooligosaccharides (GOS) typically consist of 2-8 D-galactose units linked together, terminating in a D-glucose unit. GOS are commonly used in dairy products, infant formulas, and functional foods. GOS offer beneficial properties for food processing,
Zhuo Cheng   +7 more
doaj   +2 more sources

Advancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products [PDF]

open access: yesMolecules
Sucrose phosphorylase (SPase), a member of the glycoside hydrolase GH13 family, possesses the ability to catalyze the hydrolysis of sucrose to generate α-glucose-1-phosphate and can also glycosylate diverse substrates, showcasing a wide substrate ...
Hongyu Zhang   +6 more
doaj   +2 more sources

Improvement of the Transglycosylation Efficiency of a Lacto-N-Biosidase from Bifidobacterium bifidum by Protein Engineering

open access: yesApplied Sciences, 2021
The lacto-N-biosidase LnbB from Bifidobacterium bifidum JCM 1254 was engineered to improve its negligible transglycosylation efficiency with the purpose of enzymatically synthesizing lacto-N-tetraose (LNT; Gal-β1,3-GlcNAc-β1,3-Gal-β1,4-Glc) in one ...
Marlene Vuillemin   +7 more
doaj   +1 more source

Engineering the GH1 β-glucosidase from Humicola insolens: Insights on the stimulation of activity by glucose and xylose. [PDF]

open access: yesPLoS ONE, 2017
The activity of the GH1 β-glucosidase from Humicola insolens (Bglhi) against p-nitrophenyl-β-D-glucopyranoside (pNP-Glc) and cellobiose is enhanced 2-fold by glucose and/or xylose.
Luana Parras Meleiro   +7 more
doaj   +1 more source

Manipulation of an α-glucosidase in the industrial glucoamylase-producing Aspergillus niger strain O1 to decrease non-fermentable sugars production and increase glucoamylase activity

open access: yesFrontiers in Microbiology, 2022
Dextrose equivalent of glucose from starch hydrolysis is a critical index for starch-hydrolysis industry. Improving glucose yield and decreasing the non]-fermentable sugars which caused by transglycosylation activity of the enzymes during the starch ...
Wenzhu Guo   +16 more
doaj   +1 more source

The characterisation of an alkali-stable maltogenic amylase from Bacillus lehensis G1 and improved malto-oligosaccharide production by hydrolysis suppression. [PDF]

open access: yesPLoS ONE, 2014
A maltogenic amylase (MAG1) from alkaliphilic Bacillus lehensis G1 was cloned, expressed in Escherichia coli, purified and characterised for its hydrolysis and transglycosylation properties. The enzyme exhibited high stability at pH values from 7.0 to 10.
Nor Hasmaliana Abdul Manas   +3 more
doaj   +1 more source

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