Galactooligosaccharides are well-known
functional food ingredients with prebiotic properties. Recent trend for the use
of galactooligosaccharides in the food industry leads the search for new
enzymes for their production. α-Galactosidase from Aspergillus fumigatus
IMI 385708, possessing a highly efficient debranching ability on polymeric
substrates, is also able to perform transgalactosylation. In this study,
recombinant α-galactosidase produced by Aspergillus sojae Ta1 was
purified 18.7-fold using anion exchange and hydrophobic interaction
chromatography with an overall yield of 56% and 64.7 U/mg protein specific
activity. The Vmax and Km values for the hydrolysis of pNPGal
were 78 U/mg protein and 0.45 mM, respectively. Optimum pH (pH 4.5) and
temperatures (50-60°C) for recombinant α-galactosidase activity were
determined. For the synthesis of oligosaccharides, purified and characterized
recombinant α-galactosidase was used in the transgalactosylation of various
mono- and disaccharides using pNPGal (p-nitrophenyl-α-D-galactopyranoside)
as galactose donor. Di- and trisaccharides obtained by transgalactosylation
were analysed by TLC, ESI-MS, and HPLC analysis. Among 12 acceptor candidates,
α-galactosidase transgalactosylated galactose, glucose, mannose, cellobiose,
lactose, maltose, and sucrose efficiently, however, did not transgalactosylate
xylose, arabinose, fucose, fructose, and melibiose.
α-Galactosidase Aspergillus Characterization Transgalactosylation Galactooligosaccharides Prebiotic
Birincil Dil | İngilizce |
---|---|
Konular | Yapısal Biyoloji , Gıda Mühendisliği |
Bölüm | Research Articles |
Yazarlar | |
Yayımlanma Tarihi | 1 Ocak 2019 |
Gönderilme Tarihi | 15 Mart 2018 |
Yayımlandığı Sayı | Yıl 2019Cilt: 5 Sayı: 1 |
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