Publications (2)3.39 Total impact
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Article: Heterologous expression and characterization of processing α-glucosidase I from Aspergillus brasiliensis ATCC 9642.
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ABSTRACT: A gene for processing α-glucosidase I from a filamentous fungus, Aspergillus brasiliensis (formerly called Aspergillus niger) ATCC 9642 was cloned and fused to a glutathione S-transferase tag. The active construct with the highest production level was a truncation mutant deleting the first 16 residues of the hydrophobic N-terminal domain. This fusion enzyme hydrolyzed pyridylaminated (PA-) oligosaccharides Glc(3)Man(9)GlcNAc(2)-PA and Glc(3)Man(4)-PA and the products were identified as Glc(2)Man(9)GlcNAc(2)-PA and Glc(2)Man(4)-PA, respectively. Saturation curves were obtained for both Glc(3)Man(9)GlcNAc(2)-PA and Glc(3)Man(4)-PA, and the K (m) values for both substrates were estimated in the micromolar range. When 1 μM Glc(3)Man(4)-PA was used as a substrate, the inhibitors kojibiose and 1-deoxynojirimycin had similar effects on the enzyme; at 20 μM concentration, both inhibitors reduced activity by 50%.Glycoconjugate Journal 12/2011; 28(8-9):563-71. · 2.12 Impact Factor -
Article: Heterologous expression, purification, and characterization of an α-mannosidase belonging to glycoside hydrolase family 99 of Shewanella amazonensis.
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ABSTRACT: Shewanella amazonensis α-mannosidase (Sama99), a member of glycoside hydrolase family 99, was expressed in Escherichia coli. The purified Sama99 hydrolyzed pyridylamino (PA)-sugars, Glc₁Man₉GlcNAc₂-PA, and Glc₃Man₉GlcNAc₂-PA, and the product was probably a pyridylamino-decasaccharide in both cases. The mode of action of Sama99 was found to be essentially identical to that of rat endo-α-1,2-mannosidase, but the specificity of Sama99 was low.Bioscience Biotechnology and Biochemistry 05/2011; 75(4):797-9. · 1.28 Impact Factor
