Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Ogliosaccharide"'
Autor:
Vy Ha Nguyen Tran, Thuan Thi Nguyen, Sebastian Meier, Jesper Holck, Hang Thi Thuy Cao, Tran Thi Thanh Van, Anne S. Meyer, Maria Dalgaard Mikkelsen
Publikováno v:
Tran, V H N, Nguyen, T T, Meier, S, Holck, J, Cao, H T T, Van, T T T, Meyer, A S & Mikkelsen, M D 2022, ' The Endo-α(1,3)-Fucoidanase Mef2 Releases Uniquely Branched Oligosaccharides from Saccharina latissima Fucoidans ', Marine Drugs, vol. 20, no. 5, 305 . https://doi.org/10.3390/md20050305
Marine Drugs; Volume 20; Issue 5; Pages: 305
Marine Drugs; Volume 20; Issue 5; Pages: 305
Fucoidans are complex bioactive sulfated fucosyl-polysaccharides primarily found in brown macroalgae. Endo-fucoidanases catalyze the specific hydrolysis of α-L-fucosyl linkages in fucoidans and can be utilized to tailor-make fucoidan oligosaccharide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a2fdc6529839c6d34ee61fcbab80f56
https://orbit.dtu.dk/en/publications/12f6a95d-52c4-46e3-b895-09a4d0397782
https://orbit.dtu.dk/en/publications/12f6a95d-52c4-46e3-b895-09a4d0397782
Autor:
Rossana Lupo, Eva Nordberg Karlsson, David Teze, Mette Errebo Rønne, Henrik Stålbrand, Jens Ø. Duus, Birgitte Zeuner, Birte Svensson, Régis Fauré, Mathias Wiemann, Jiao Zhao, Marlene Vuillemin, Göran Carlström, Yves-Henri Sanejouand, Zubaida Gulshan Kazi, Michael J. O’Donohue
Publikováno v:
Chemistry-A European Journal
Chemistry-A European Journal, In press, ⟨10.1002/chem.202100110⟩
Chemistry-A European Journal, Wiley-VCH Verlag, In press, ⟨10.1002/chem.202100110⟩
Teze, D, Zhao, J, Wiemann, M, Kazi, Z G A, Lupo, R, Zeuner, B, Vuillemin, M, Rønne, M E, Carlström, G, Duus, J Ø, Sanejouand, Y-H, O'Donohue, M J, Nordberg Karlsson, E, Fauré, R, Stålbrand, H & Svensson, B 2021, ' Rational Enzyme Design without Structural Knowledge: A Sequence-Based Approach for Efficient Generation of Transglycosylases ', Chemistry-A European Journal, vol. 27, no. 40, pp. 10323-10334 . https://doi.org/10.1002/chem.202100110
Chemistry-A European Journal, In press, ⟨10.1002/chem.202100110⟩
Chemistry-A European Journal, Wiley-VCH Verlag, In press, ⟨10.1002/chem.202100110⟩
Teze, D, Zhao, J, Wiemann, M, Kazi, Z G A, Lupo, R, Zeuner, B, Vuillemin, M, Rønne, M E, Carlström, G, Duus, J Ø, Sanejouand, Y-H, O'Donohue, M J, Nordberg Karlsson, E, Fauré, R, Stålbrand, H & Svensson, B 2021, ' Rational Enzyme Design without Structural Knowledge: A Sequence-Based Approach for Efficient Generation of Transglycosylases ', Chemistry-A European Journal, vol. 27, no. 40, pp. 10323-10334 . https://doi.org/10.1002/chem.202100110
International audience; Glycobiology is dogged by the relative scarcity of synthetic, defined oligosaccharides. Enzyme-catalysed glycosylation using glycoside hydrolases is feasible but is hampered by the innate hydrolytic activity of these enzymes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6f715607b890e69302d079c5337f20e
https://hal.inrae.fr/hal-02906907v2/document
https://hal.inrae.fr/hal-02906907v2/document
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
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