Three reducing oligosaccharides were formed as transfer products when melibiose was incubated with an α-galactosidase preparation from bottom yeast in the presence of a little galactose. No other products could be found. These products were isolated by column chromatography and identified as α-1, 6-galactobiose, manninotriose and verbascotetraose by means of paper chromatography and periodate oxidation. Their specific optical rotations were in accord with those reported in the literature. Even when the same enzyme preparation was incubated with p-nitrophenyl α-galactoside and methanol, galactobiose and p-nitrophenyl galactobioside were formed as predominant transfer products alongside methyl a-galactoside.Article信州大学工学部紀要 10: 14-29 (1960)de...
α-d-Galactosidases (α-d-galactoside galactohydrolase, E.C. 3.2.1.22) are exoglycosidases, which in v...
The last fifty years has seen an increase in the production of synthetic or artificial enzyme substr...
The transglycosylation activity of a novel commercial β-galactosidase from Bifidobacterium bifidum (...
The α-galactosidase from bottom yeast could be fractionated into at least three components by chroma...
Several glycosidases including the a-galactosidases of Taka-diastase, apricot kernel, malt and botto...
The α-galactosidase of brewer's bottom yeast has been resolved, using phosphate buffer of pH 7.0, an...
This study is divided into two parts. Part 1 describes the partial purification and characterization...
α-Galactosidase was purified to homogeneity from the culture fluid of the yeast Trichosporon cutaneu...
It was the purpose of this experiment to obtain unequivocal evidence for the suggested structures of...
\u3b1-Galactosidase purified from Lactobacillus helveticus ATCC 10797 by fast performance liquid chr...
Galactooligosaccharides (GalOS) were efficiently produced by partially purified β-galactosidase from...
The synthesis of galactooligosaccharides (GOS) catalyzed by β-galactosidase from Aspergillus oryzae ...
α−Galactosidase (α-D-galactoside galactohydrolase [EC 3.2.1.22]) was obtained from Lactobacillus aci...
The Xanthomonas manihotis /3-galactosidase (BgaX) is a 66 kDa retaining glycosidase that hydrolyzes...
The first gene (alpha-gal1) encoding an extracellular alpha-Dgalactosidase from the thermophilic fun...
α-d-Galactosidases (α-d-galactoside galactohydrolase, E.C. 3.2.1.22) are exoglycosidases, which in v...
The last fifty years has seen an increase in the production of synthetic or artificial enzyme substr...
The transglycosylation activity of a novel commercial β-galactosidase from Bifidobacterium bifidum (...
The α-galactosidase from bottom yeast could be fractionated into at least three components by chroma...
Several glycosidases including the a-galactosidases of Taka-diastase, apricot kernel, malt and botto...
The α-galactosidase of brewer's bottom yeast has been resolved, using phosphate buffer of pH 7.0, an...
This study is divided into two parts. Part 1 describes the partial purification and characterization...
α-Galactosidase was purified to homogeneity from the culture fluid of the yeast Trichosporon cutaneu...
It was the purpose of this experiment to obtain unequivocal evidence for the suggested structures of...
\u3b1-Galactosidase purified from Lactobacillus helveticus ATCC 10797 by fast performance liquid chr...
Galactooligosaccharides (GalOS) were efficiently produced by partially purified β-galactosidase from...
The synthesis of galactooligosaccharides (GOS) catalyzed by β-galactosidase from Aspergillus oryzae ...
α−Galactosidase (α-D-galactoside galactohydrolase [EC 3.2.1.22]) was obtained from Lactobacillus aci...
The Xanthomonas manihotis /3-galactosidase (BgaX) is a 66 kDa retaining glycosidase that hydrolyzes...
The first gene (alpha-gal1) encoding an extracellular alpha-Dgalactosidase from the thermophilic fun...
α-d-Galactosidases (α-d-galactoside galactohydrolase, E.C. 3.2.1.22) are exoglycosidases, which in v...
The last fifty years has seen an increase in the production of synthetic or artificial enzyme substr...
The transglycosylation activity of a novel commercial β-galactosidase from Bifidobacterium bifidum (...