Production and characterization of active soluble human beta 1, 4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal beta 1 -> 4 GlcNAc linkage

Authors
Shibatani, S Fujiyama, K Nishiguchi, S Seki, T Maekawa, Y
Citation
S. Shibatani et al., Production and characterization of active soluble human beta 1, 4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal beta 1 -> 4 GlcNAc linkage, J BIOSCI BI, 91(1), 2001, pp. 85-87
Citations number
13
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
13891723 → ACNP
Volume
91
Issue
1
Year of publication
2001
Pages
85 - 87
Database
ISI
SICI code
1389-1723(200101)91:1<85:PACOAS>2.0.ZU;2-2
Abstract
An active and soluble human beta1,4-galactosyltransferase (beta -GT) was pr oduced in Escherichia coli using a maltose-binding protein fusion system. T he purified recombinant beta -GT has a K-m value of 0.035 mM for UDP-galact ose and a V-max of 643 x 10(3) nmol/mg/h. The enzyme catalyzes the transfer of galactose from UDP-galactose to N-linked oligosaccharides. The properti es of the purified enzyme were identical to those of bovine milk beta -GT.