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A Pasteurella multocida sialyltransferase displaying dual trans-sialidase activities for production of 3′-sialyl and 6′-sialyl glycans.
- Source :
-
Journal of Biotechnology . Jan2014, Vol. 170, p60-67. 8p. - Publication Year :
- 2014
-
Abstract
- Highlights: [•] PmST, a Pasteurella multocida sialyltransferase expressed in Escherichia coli exhibited both α-2,3- and α-2,6-trans-sialidase activities. [•] Optimum conditions were identified for maximum production of 3′- and 6′-sialyllactoses by PmST-catalyzed trans-sialylation using casein glycomacropeptide as the donor for sialic acid. [•] The regioselective synthesis of sialyllactose could be achieved by regulating reaction time. [•] The kinetic parameter for α-2,6-trans-sialidase activity of PmST was estimated. [•] PmST catalyzed α-2,3 as well as α-2,6 sialylation of prebiotic galactooligosaccharides. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01681656
- Volume :
- 170
- Database :
- Academic Search Index
- Journal :
- Journal of Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 93417791
- Full Text :
- https://doi.org/10.1016/j.jbiotec.2013.11.013