Correction for 'Enhanced transglycosylation activity of an Endo-F3 mutant by ligand-directed localization' by Xiangman Zou , , 2022, , 3086-3095, https://doi.org/10.1039/D2OB00030J.
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Maltotriosyl-erythritol, a transglycosylation product of erythritol by Thermus sp. amylomaltase and its application to prebiotic.
Food Chem
January 2025
Department of Biochemistry, Phramongkutklao College of Medicine, Phramongkutklao Hospital, Bangkok 10400, Thailand. Electronic address:
In this study, maltotriosyl-erythritol (EG) was synthesized as a novel prebiotic candidate via transglycosylation using recombinant amylomaltase (AMase) from Thermus sp. Tapioca starch served as the glucosyl donor, and erythritol as the acceptor. High-performance liquid chromatography (HPLC) revealed an EG yield of 14.
View Article and Find Full Text PDFHeterologous Production, Purification and Characterization of Two Cold-Active β-d-Galactosidases with Transglycosylation Activity from the Psychrotolerant Arctic Bacterium sp. S3* Isolated from Spitsbergen Island Soil.
Int J Mol Sci
December 2024
Department of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland.
Cold-adapted microorganisms possess cold-active enzymes with potential applications in different industries and research areas. In this study, two genes encoding β-d-galactosidases belonging to Glycoside Hydrolase families 2 and 42 from the psychrotolerant Arctic bacterium sp. S3* were cloned, expressed in and , purified and characterized.
View Article and Find Full Text PDFCharacterization of a maltononaose-producing amylopullulanase from Bacillus aryabhattai W310.
Int J Biol Macromol
December 2024
Faculty of Food Science and Engineering, Kunming University of Science and Technology, Kunming, Yunnan 650500, China. Electronic address:
The recombinated amylopullulanase of PulW310B, pullulanase from Bacillus aryabhattai W310, was characterized. Sequence analysis of PulW310B showed that PulW310B has type I pullulanase structures including its typical region and the conserved regions of glycoside hydrolase family 13. Moreover, PulW310B was predicted to has typical domains of pullulanase and SSF51445 belonging to tansglycosidase.
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 PDFStructural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.
FEBS J
December 2024
Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, DTU Bioengineering, Technical University of Denmark, Kgs. Lyngby, Denmark.
Article Synopsis
- GH29A α-l-fucosidases are enzymes that help break down specific sugars in glycoconjugates and can also be used to create human milk oligosaccharides (HMOs) through a process called transglycosylation.
- Researchers used bioinformatics tools and phylogenetic clustering to identify and analyze new microbial GH29A α-l-fucosidases from an underexplored group, as well as previously known enzymes, to determine their biochemical properties and behavior under different conditions.
- The study found that transglycosylation of certain substrates was most effective at neutral to alkaline pH levels and revealed new structural insights into how these enzymes function, particularly regarding regioselectivity in product formation.
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