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Transglycosylation behavior of Mucor hiemalis endo-β-N-acetylglucosaminidase to β-cyclodextrin derivatives with multivalent glucose moieties for synthesizing cyclodextrin-based oligosaccharide clusters.
Carbohydr Res
February 2025
Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama, 350-0295, Japan. Electronic address:
We investigated the transglycosylation reaction of two types of oligosaccharide acceptors, i.e., β-cyclodextrin (CD) derivatives 1 and 2 conjugated with multiple glucose (Glc) units, catalyzed by endo-β-N-acetyl-glucosaminidase from Mucor hiemalis (Endo-M) using the oligosaccharide donor sialoglycopeptide (SGP).
View Article and Find Full Text PDFCompartmentalized co-immobilization of cellulase and cellobiose phosphorylase within zeolitic imidazolate framework efficiently synthesizes 1-p-Glc: Glycosylation of FDG.
Int J Biol Macromol
December 2024
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China. Electronic address:
Enzymatic glycosylation is an efficient and biocompatible approach to enhance natural product bioavailability. Cellobiose phosphorylase, a novel glycosyltransferase, utilizes 1-phospho-glucose (1-p-Glc) as a glycosyl donor for regioselective glycosylation of various natural substrates. However, the high cost of 1-p-Glc limits the economic feasibility of the process.
View Article and Find Full Text PDFSustainable and Scalable Enzymatic Production, Structural Elucidation, And Biological Evaluation of Novel Phlorizin Analogues.
ChemSusChem
November 2024
Université de Reims Champagne-Ardenne, CNRS, ICMR 7312, 51097, Reims, France.
It is not unusual for naturally occurring compounds to be limited for their use in cosmetics due to their low water solubility. Recently, aiming at accessing novel phlorizin (a glycosylated bioactive recovered from apple tree wood and already used in cosmetics as antioxidant ingredient) analogues, we reported the synthesis of very promising - but low water-soluble - biomass-derived chalcones (CHs) and dihydrochalcones (DHCs) exhibiting antioxidant and anti-tyrosinase activities. Glycosylating bioactive compounds being one of the most common strategies to increase their water solubility, herein we report the enzymatic glycosylation of the CHs mentioned above, as well as DHC using cyclodextrin glycosyltransferases (CGTase), enzymes well-known for catalyzing the selective α(1→4) transglycosylation.
View Article and Find Full Text PDFSite-directed mutagenesis leads to the optimized transglycosylation activity of endo-beta-N-acetylglucosaminidase from Trypanosoma brucei.
Glycoconj J
October 2024
Key Laboratory of Carbohydrate Chemistry and Biotechnology, School of Biotechnology, Ministry of Education, Jiangnan University, Wuxi, 214122, China.
Endo-β-N-acetylglucosaminidases (ENGases) are pivotal enzymes in the degradation and remodeling of glycoproteins, which catalyze the cleavage or formation of β-1,4-glycosidic bond between two N-acetylglucosamine (GlcNAc) residues in N-linked glycan chains. It was investigated that targeted mutations of amino acids in ENGases active site may modulate their hydrolytic and transglycosylation activities. Endo-Tb, the ENGase derived from Trypanosoma brucei, belongs to the glycoside hydrolase family 85 (GH85).
View Article and Find Full Text PDFAdvancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products.
Molecules
August 2024
Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
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 specificity. This enzyme has found extensive utility in the fields of food, medicine, and cosmetics, and has garnered significant attention as a focal point of research in transglycosylation enzymes. Nevertheless, SPase encounters numerous obstacles in industrial settings, including low enzyme yield, inadequate thermal stability, mixed regioselectivity, and limited transglycosylation activity.
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