“…23 (Varbanetes et al, 2001). Although the purified α-galactosidase didnot hydrolyze raffinose and stachyose, the culture hydrolyzed the RO (de Felix, 1997, 1999), indicating the ability of A. fumigatus to produce other α-galactosidase forms.…”
Section: Resultsmentioning
confidence: 99%
“…However, the affinity of the enzyme for melibiose was much lower than its affinity for ρNPGal. It is known (Varbanetes et al, 2001) that most microbial α-galactosidases hydrolyze the synthetic substrate ρNPGal more efficiently than the natural α-galactosides. Moreover, α-galactosidase from Aspergillus niger was reported (Kaneko et al, 1991) to hydrolyze exclusively the synthetic substrate and failed to split off the terminal α-1,6-bound galactose in linear structures like the melibiose, raffinose and stachyose.…”
Aspergillus fumigatus secreted invertase (β-fructofuranosidase) and α-galactosidase enzymatic activities able to hydrolyzing raffinose oligosaccharides (RO). α-Galactosidase was induced by galactose, melibiose and raffinose, but galactose was the most efficient inducer. It was purified by gel filtration and two ion exchange chromatographies and showed Mw of 54.7 kDa. The purified enzyme showed maximal activity against pnitrophenyl-α-D-galactopyranoside (pNPGal
“…23 (Varbanetes et al, 2001). Although the purified α-galactosidase didnot hydrolyze raffinose and stachyose, the culture hydrolyzed the RO (de Felix, 1997, 1999), indicating the ability of A. fumigatus to produce other α-galactosidase forms.…”
Section: Resultsmentioning
confidence: 99%
“…However, the affinity of the enzyme for melibiose was much lower than its affinity for ρNPGal. It is known (Varbanetes et al, 2001) that most microbial α-galactosidases hydrolyze the synthetic substrate ρNPGal more efficiently than the natural α-galactosides. Moreover, α-galactosidase from Aspergillus niger was reported (Kaneko et al, 1991) to hydrolyze exclusively the synthetic substrate and failed to split off the terminal α-1,6-bound galactose in linear structures like the melibiose, raffinose and stachyose.…”
Aspergillus fumigatus secreted invertase (β-fructofuranosidase) and α-galactosidase enzymatic activities able to hydrolyzing raffinose oligosaccharides (RO). α-Galactosidase was induced by galactose, melibiose and raffinose, but galactose was the most efficient inducer. It was purified by gel filtration and two ion exchange chromatographies and showed Mw of 54.7 kDa. The purified enzyme showed maximal activity against pnitrophenyl-α-D-galactopyranoside (pNPGal
“…in the pulp and paper industry α-galactosidase could enhance the bleaching effect of β-mannanases on softwood pulp (7). In human medicine this enzyme can be used for the treatment of Fabry's disease (3) or for the blood type conversion (25). Weignerova et al (2009) summarizes recent advances in the use of α-galactosidases in synthetic and biotransformation applications (28).…”
Section: Introductionmentioning
confidence: 99%
“…Abundant information is available on the biosynthesis of α-galactosidase from filamentous fungi belonging to the genera Penicillium and Aspergillus (1,4,6,8,9,16,18,21,23,25,26) during submerged fermentation.…”
“…In the food industry microbial α-galactosidases are used for different biotechnological applications, e.g., for the hydrolysis of raffinose in beet sugar syrups or galacto-oligosaccharides in soybean milk (20) and for the improvement of the gelling properties of galactomannans used as food thickeners (9). these enzymes are of interest in medicine, e.g., for the treatment of Fabry's disease by enzyme replacement therapy (16) or for the blood type conversion (B type cell to o type cell) (31).…”
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