Amylosucrase as a Versatile Biocatalyst for Next‐Generation Functional Ingredients: Starch Modification and Glycoside Synthesis [PDF]
ABSTRACT Amylosucrase (ASase, E.C. 2.4.1.4) is a transglucosidase that catalyzes α‐glucan synthesis and transglycosylation reactions using sucrose as the sole substrate. Unlike Leloir glycosyltransferases requiring expensive nucleotide sugars, ASases utilize readily available sucrose as a cost‐effective glucose donor, offering economic advantages for ...
Dong‐Ho Seo +2 more
wiley +2 more sources
A structure-based high-efficiency homogeneous antibody platform by endoglycosidase Sz provides insights into its transglycosylation mechanism [PDF]
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 products generated by Talaromyces amestolkiae GH3 β-glucosidases: effect of hydroxytyrosol, vanillin and its glucosides on breast cancer cells [PDF]
Background Transglycosylation represents one of the most promising approaches for obtaining novel glycosides, and plant phenols and polyphenols are emerging as one of the best targets for creating new molecules with enhanced capacities.
Juan Antonio Méndez-Líter +10 more
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]
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
Microbial Biotechnology at the Frontiers of Innovation: Engineering Solutions for Health, Industry and Sustainability [PDF]
Microbial Biotechnology, Volume 19, Issue 9, September 2026.
Patricia Bernal, Juan Luis Ramos
wiley +2 more sources
Safety evaluation of the food enzyme cyclomaltodextrin glucanotransferase from the genetically modified Escherichia coli K12 strain DSM 34229 [PDF]
Abstract The food enzyme cyclomaltodextrin glucanotransferase (1,4‐α‐D‐glucan 4‐α‐D‐[1,4‐α‐D‐glucano]‐transferase, EC 2.4.1.19) is produced with the genetically modified Escherichia coli K12 strain DSM 34229 by Wacker Chemie AG. The genetic modifications did not give rise to safety concerns.
EFSA Panel on Food Enzymes (FEZ) +19 more
wiley +2 more sources
Studies on Lysozyme Catalyzed Transglycosylation [PDF]
The lysozyme catalyzed transglycosylation with glycol chitin or related oligosaccharides as substrate and p-nitrophenyl β-glycoside of 2-acetamido-2-deoxy-D-glucopyranoside as acceptor was studied in order to obtain basic information which is expected to
Hayashi, Katsuya +4 more
openaire +2 more sources
Studies on Lysozyme Catalyzed Transglycosylation
The lysozyme catalyzed transglycosylation with glycol chitin or related oligosaccharides as substrate and p-nitrophenyl β-glycoside of 2-acetamido-2-deoxy-D-glucopyranoside as acceptor was studied in order to obtain basic information which is expected to be available for the elucidation of the mechanism of lysozyme catalyzed reaction.
Hayashi, Katsuya +6 more
openaire +2 more sources
Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A. [PDF]
Endo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become the focus of intense research because of their potential for synthesis ...
Jie Yin +12 more
doaj +1 more source
Alkyl glycosides and sugars esters are non-ionic surfactants of interest for various applications (cosmetics, food, detergency,…). In the present study, xylans and cellulose from wheat bran were enzymatically converted into pentyl xylosides and glucose ...
Chloé Jocquel +3 more
doaj +1 more source

