High-Yield Biosynthesis of Glucosylglycerol through Coupling Phosphorolysis and Transglycosylation Reactions

Autor: Chaoyu Tian, Chenxi Ren, Tong Zhang, Yuanxia Sun, Jiangang Yang, Yan Men, Peng Chen

Publikováno v: Journal of Agricultural and Food Chemistry. 68:15249-15256

Glucosylglycerol is a powerful osmolyte that has attracted attention as a useful moisturizing ingredient in the cosmetic industry. This study demonstrates two artificially designed synthetic routes for manufacturing glucosylglycerol by combining phos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3fd61367ca1a1c94133cf95dcd81c14
https://doi.org/10.1021/acs.jafc.0c04851

Discovery of a Kojibiose Hydrolase by Analysis of Specificity-Determining Correlated Positions in Glycoside Hydrolase Family 65

Autor: Emma De Beul, Jorick Franceus, Tom Desmet, Alana Jongbloet

Publikováno v: Molecules
Volume 26
Issue 20
MOLECULES
Molecules, Vol 26, Iss 6321, p 6321 (2021)

The Glycoside Hydrolase Family 65 (GH65) is an enzyme family of inverting α-glucoside phosphorylases and hydrolases that currently contains 10 characterized enzyme specificities. However, its sequence diversity has never been studied in detail. Here

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b4b0ab66269d50e35cdf7f87a21085f

Biochemical characteristics of maltose phosphorylase MalE from Bacillus sp. AHU2001 and chemoenzymatic synthesis of oligosaccharides by the enzyme

Autor: Wataru Saburi, Haruhide Mori, Yodai Taguchi, Yu Gao

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 83:2097-2109

Maltose phosphorylase (MP), a glycoside hydrolase family 65 enzyme, reversibly phosphorolyzes maltose. In this study, we characterized Bacillus sp. AHU2001 MP (MalE) that was produced in Escherichia coli. The enzyme exhibited phosphorolytic activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::326fdf4a50b5409b6b8b4a277690e39f
https://doi.org/10.1080/09168451.2019.1634516

An 1,4-α-Glucosyltransferase Defines a New Maltodextrin Catabolism Scheme in Lactobacillus acidophilus

Autor: Birte Svensson, Yong Jun Goh, Jens-Christian N. Poulsen, Susan Andersen, M.J. Pichler, Maher Abou Hachem, Leila Lo Leggio, Marie Sofie Møller

Publikováno v: Appl Environ Microbiol
Andersen, S, Møller, M S, Poulsen, J-C N, Pichler, M J, Svensson, B, Lo Leggio, L, Goh, Y J & Abou Hachem, M 2020, ' An 1,4-α-glucosyltransferase defines a new maltodextrin catabolism scheme in Lactobacillus acidophilus ', Applied and Environmental Microbiology, vol. 86, no. 15, e0061-20 . https://doi.org/10.1128/AEM.00661-20

The maltooligosaccharide (MOS) utilization locus in Lactobacillus acidophilus NCFM, a model for human small-intestine lactobacilli, encodes three glycoside hydrolases (GHs): a putative maltogenic α-amylase of family 13 subfamily 20 (LaGH13_20), a ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0283ae55a7e0a3bfd5d1e39c1b47073f
https://pubmed.ncbi.nlm.nih.gov/32444471

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