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- W1860373003 abstract "An extracellular α-galactosidase from Aspergillus niger v.Tiegh RM48 was purified to apparent homogeneity by ammonium sulfate(80% saturation)precipitation,Phenyl Sepharose CL-4B hydrophobic column chromatography and Sephadex G-100 filtration chromatography.The specific activity of the enzyme was increased approximately 103-fold,from 26.29 IU·mg-1 protein to 2722.3 IU·mg-1 protein.The molecular mass of the purified enzyme as determined by SDS-PAGE was 108 kDa.The optimum pH and temperature of this α-galactosidase were pH 4.5 and 60 ℃,respectively.The enzyme was stable between pH 3.0 and pH 6.0,however,its activity was inhibited by all tested metal ions.α-Galactosidase activity was strongly inhibited by Cu2+,Fe2+ and moderately inhibited by Li2+,Zn2+,Mn2+,K+,Na+,Ca2+,Mg2+ and Co2+.Kinetic studies of the α-galactosidase showed that the Km and the Vmax for 4-nitrophenyl-α-D-galactopyranoside(pNPG)were 7.37 mmol·L-1 and 5618 IU·mg-1·min-1,respectively.The N-terminal amino acids sequence of the α-galactosidase protein was determined as DEKAYSPCYY,no evidence showed the apparent sequence similarity between this enzyme and any other α-galactosidase listed in the database." @default.
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- W1860373003 date "2009-01-01" @default.
- W1860373003 modified "2023-09-26" @default.
- W1860373003 title "Purification and characterization of α-galactosidase from Aspergillus niger v.Tiegh RM48." @default.
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