Results 41 to 50 of about 602 (161)
An Update: Enzymatic Synthesis for Industrial Applications
Angewandte Chemie International Edition, Volume 64, Issue 27, July 1, 2025.Biocatalysis has become a sustainable and cost‐competitive alternative to established chemical synthesis, enabling the enzyme‐based production of not only commodity chemicals but (non‐natural) amino acids, (rare) sugars, as well as synthetic nucleotides.
Thomas Bayer +4 more
wiley +1 more source
Mass Spectrometry Reviews, Volume 44, Issue 3, Page 213-453, May/June 2025.Abstract The use of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry for the analysis of carbohydrates and glycoconjugates is a well‐established technique and this review is the 12th update of the original article published in 1999 and brings coverage of the literature to the end of 2022.
David J. Harvey
wiley +1 more source
, 2007 International audienceGlycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G.
Ibatullin, Farid M +23 more
core +1 more source
Bottom‐Up Synthesized Glucan Materials: Opportunities from Applied Biocatalysis
Advanced Materials, Volume 36, Issue 27, July 4, 2024.Linear d‐glucans, simple yet versatile polysaccharides, shape nanostructures crucial for biomaterial development. Shifting from top‐down to bottom‐up synthesis using natural and engineered enzymes provides meticulous control over polymer structures, fostering diversification for macromolecular materials.
Chao Zhong, Bernd Nidetzky
wiley +1 more source
, 2016 Understanding how enzymes mediate catalysis is a key to their reprogramming for biotechnological applications. The family 3 retaining glycosidase postulated to be involved in erythromycin self-resistance was cloned, recombinantly expressed in Escherichia
David L. Jakeman (1411447) +1 more
core +1 more source
The First Glycosynthase Derived from an Inverting Glycoside Hydrolase [PDF]
Journal of Biological Chemistry, 2006 Reducing end xylose-releasing exooligoxylanase (Rex, EC 3.2.1.156) is an inverting GH that hydrolyzes xylooligosaccharides (> or = X3) to release X1 at their reducing end. The wild-type enzyme exhibited the Hehre resynthesis hydrolysis mechanism, in which alpha-X2F was hydrolyzed to X2 and HF in the presence of X1 as an acceptor molecule.
Yuji, Honda, Motomitsu, Kitaoka
openaire +2 more sources
, 2015 The current drive for applications of biomass-derived compounds, for energy and advanced materials, has led to a resurgence of interest in the manipulation of plant polymers.
Gustav Sundqvist (1278813) +9 more
core +1 more source
Chemistry & Biology, 2008 Glycosynthases are catalytic mutants of mainly retaining glycoside hydrolases that catalyze the synthesis of oligosaccharides from their corresponding glycosyl-fluoride donors and suitable acceptors. Here we describe the development of a general, high-throughput screening procedure for glycosynthase activity, which is based on the release of ...
Ben-David, Alon +2 more
openaire +2 more sources
National audienceMost antibiotics used in human medicine inhibit the biosynthesis of peptidoglycan, an essential component of the bacterial cell wall.
Fort, S.
core +3 more sources
, 2019 Glycosynthases are promising enzyme catalysts for glycoside synthesis. Derived from glycoside hydrolases by mechanistic repurposing of their active site, glycosynthases utilize suitably activated glycosyl donors for glycosylation, yet they are unable to ...
Kai Baldenius (6703340) +7 more
core +1 more source