Purification and characterization of an oligo-isomaltosaccharide synthase from a Streptococcus sobrinus glucosyltransferase-I deficient mutant.

Citation
N. Shinozaki-kuwahara et al., Purification and characterization of an oligo-isomaltosaccharide synthase from a Streptococcus sobrinus glucosyltransferase-I deficient mutant., BIOS BIOT B, 65(6), 2001, pp. 1290-1295
Citations number
26
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Agricultural Chemistry","Biochemistry & Biophysics
Journal title
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
ISSN journal
0916-8451 → ACNP
Volume
65
Issue
6
Year of publication
2001
Pages
1290 - 1295
Database
ISI
SICI code
0916-8451(200106)65:6<1290:PACOAO>2.0.ZU;2-8
Abstract
One glucosyltransferase (GTF) -I deficient mutant of Streptococcus sobrinus strain B13N was isolated through chemical mutagenesis with ethyl methanesu lfonate, and characterized. This mutant, designated as B13N-Id, readily all owed us to purify a homogeneous oligo-isomaltosaccharide synthase (GTF-S) f rom its culture fluid, The purified GTF-S was only recognized with rabbit polyclonal antibody agai nst recombinant GTF-S from an Ecsherichia coli MD124 clone expressing the B 13N gtfS gene, and showed the almost same enzymatic properties as the recom binant enzyme. A double reciprocal plot of the B13N GTF-S for sucrose was b iphasic, and the affinity for this substrate was high compared to that of G TF-S enzymes from other strains,