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dc.contributor.authorMontel, E.-
dc.contributor.authorHrmova, M.-
dc.contributor.authorFincher, G.-
dc.contributor.authorDriguez, H.-
dc.contributor.authorCottaz, S.-
dc.identifier.citationAustralian Journal of Chemistry: an international journal for chemical science, 2009; 62(6):575-584-
dc.description.abstract3II-O-Allyl-α-laminaribiosyl fluoride was prepared as a key synthon for the enzymatic synthesis of β(1→3)-glucan oligosaccharides, catalyzed by a mutated β(1→3)-glucanase (E231G) from barley (Hordeum vulgare L.). A strategy was developed for enzymatic elongation of the β(1→3)-glucan chain from the reducing end, using a single glucoside acceptor. When β-glucoside phenyl disulfide was used as the acceptor, this methodology generated laminari-oligosaccharides conjugatable at both their reducing and non-reducing ends.-
dc.description.statementofresponsibilityEmilie Montel, Maria Hrmova, Geoffrey B. Fincher, Hugues Driguez and Sylvain Cottaz-
dc.publisherC S I R O Publishing-
dc.titleA chemoenzymatic route to conjugatable beta(1 -> 3)-glucan oligosaccharides-
dc.typeJournal article-
dc.identifier.orcidHrmova, M. [0000-0002-3545-0605]-
Appears in Collections:Agriculture, Food and Wine publications
Aurora harvest

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