Results 31 to 40 of about 1,170 (199)

Challenges and Opportunities for the Large-Scale Chemoenzymatic Glycoengineering of Therapeutic N-Glycosylated Monoclonal Antibodies [PDF]

open access: yes, 2022
Variability in the glycosylation profile of therapeutic monoclonal antibodies (mAbs), due to recombinant production technologies, leads to inconsistencies in effector functions and pharmacokinetic properties, both batch-to-batch and within single batches.
Falcioni, Francesco, Ivanova, Adelina
core   +1 more source

Glycosynthase-catalysed formation of modified polysaccharide microstructures [PDF]

open access: yesBiochemical Journal, 2004
Glycosynthases are mutant glycosidases, genetically engineered to catalyse the synthesis of oligosaccharides. A study by Faijes et al. in this issue of the Biochemical Journal has expanded the ability of glycosynthases to catalyse the polymerization of carbohydrates to form unnatural oligosaccharide products that can attain unique crystalline forms ...
Andrew G, Watts, Stephen G, Withers
openaire   +2 more sources

Glycoside hydrolases from (hyper)thermophilic archaea: structure, function, and applications [PDF]

open access: yes, 2023
: (Hyper)thermophilic archaeal glycosidases are enzymes that catalyze the hydrolysis of glycosidic bonds to break down complex sugars and polysaccharides at high temperatures.
Cobucci-Ponzano B.   +4 more
core   +1 more source

Engineering the functional fitness of transglycosidases and glycosynthases by directed evolution [PDF]

open access: yes, 2013
The artificial implementation of the Darwinian theory of evolution to create new variants of functional proteins, a process referred to as directed evolution, has acquired many applications in biochemical engineering.
Bulimo, WD, Mulaa, FJ, Osanjo, GO
core   +2 more sources

Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum.

open access: yesOrganic and biomolecular chemistry, 2019
Lacto-N-biose 1,2-oxazoline was prepared chemo-enzymatically and shown to be a donor substrate for β-1,3-glycosylation of lactose by the wild-type and glycosynthase variants (D320E, D320A, Y419F) of Bifidobacterium bifidum β-N-hexosaminidase.
Katharina Schmölzer   +3 more
semanticscholar   +1 more source

Sugars : burden or biomaterials of the future? [PDF]

open access: yes, 2010
During the past few years, the field of tissue engineering (TE) has been shifting from replacement to regenerative strategies. Following this tendency, the requirements for biomaterials to be used in TE have been also changing.
Pashkuleva, I., Reis, R. L.
core   +1 more source

Endo-F3 Glycosynthase Mutants Enable Chemoenzymatic Synthesis of Core-fucosylated Triantennary Complex Type Glycopeptides and Glycoproteins*

open access: yesJournal of Biological Chemistry, 2016
Chemoenzymatic synthesis is emerging as a promising approach to the synthesis of homogeneous glycopeptides and glycoproteins highly demanded for functional glycomics studies, but its generality relies on the availability of a range of enzymes with high ...
John P. Giddens   +3 more
semanticscholar   +1 more source

Reagent Engineering for Group Transfer Biocatalysis

open access: yesAngewandte Chemie, Volume 136, Issue 7, February 12, 2024.
Biocatalytic group transfer reactions can efficiently generate highly complex molecules under mild and environmentally friendly conditions. This Minireview highlights inspiring examples of the development of non‐natural donor reagents to power such enzymatic transformations, while discussing the design aspects behind the choice of reagent.
John H. Reed, Florian P. Seebeck
wiley   +2 more sources

Correction: Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum.

open access: yesOrganic and biomolecular chemistry, 2019
Correction for 'Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum' by Katharina Schmölzer et al., Org. Biomol. Chem., 2019, DOI: 10.1039/c9ob00424f.
Katharina Schmölzer   +3 more
semanticscholar   +1 more source

Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans [PDF]

open access: yes, 2016
Endo-β-N-acetylglucosaminidase M (Endo-M), an endoglycosidase from the fungus Mucor hiemalis, is a useful tool for chemoenzymatic synthesis of glycoconjugates, including glycoprotein-based therapeutics having a precisely defined glycoform, by virtue of ...
Katayama, Takane   +6 more
core   +1 more source

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