NDLI: Purification and biochemical characterization of a novel α-glucosidase from Aspergillus niveus

Content Provider	Springer Nature Link
Author	Silva, Tony Marcio Michelin, Michele Lima Damásio, Andre Ricardo Maller, Alexandre Almeida, Fausto Bru Dos Reis Ruller, Roberto Ward, Richard John Rosa, José Cesar Jorge, João Atilio Terenzi, Héctor Francisco Lourdes Teixeira de Moraes Polizeli, Maria
Copyright Year	2009
Abstract	An extracellular α-glucosidase produced by Aspergillus niveus was purified using DEAE-Fractogel ion-exchange chromatography and Sephacryl S-200 gel filtration. The purified protein migrated as a single band in 5% PAGE and 10% SDS–PAGE. The enzyme presented 29% of glycosylation, an isoelectric point of 6.8 and a molecular weight of 56 and 52 kDa as estimated by SDS-PAGE and Bio-Sil-Sec-400 gel filtration column, respectively. The enzyme showed typical α-glucosidase activity, hydrolyzing p-nitrophenyl α-d-glucopyranoside and presented an optimum temperature and pH of 65°C and 6.0, respectively. In the absence of substrate the purified α-glucosidase was stable for 60 min at 60°C, presenting t 50 of 90 min at 65°C. Hydrolysis of polysaccharide substrates by α-glucosidase decreased in the order of glycogen, amylose, starch and amylopectin. Among malto-oligosaccharides the enzyme preferentially hydrolyzed malto-oligosaccharide (G10), maltopentaose, maltotetraose, maltotriose and maltose. Isomaltose, trehalose and β-ciclodextrin were poor substrates, and sucrose and α-ciclodextrin were not hydrolyzed. After 2 h incubation, the products of starch hydrolysis measured by HPLC and thin layer chromatography showed only glucose. Mass spectrometry of tryptic peptides revealed peptide sequences similar to glucan 1,4-alpha-glucosidases from Aspergillus fumigatus, and Hypocrea jecorina. Analysis of the circular dichroism spectrum predicted an α-helical content of 31% and a β-sheet content of 16%, which is in agreement with values derived from analysis of the crystal structure of the H. jecorina enzyme.
Starting Page	569
Ending Page	578
Page Count	10
File Format	PDF
ISSN	00036072
Journal	Antonie van Leeuwenhoek
Volume Number	96
Issue Number	4
e-ISSN	15729699
Language	English
Publisher	Springer Netherlands
Publisher Date	2009-09-10
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Aspergillus niveus α-Glucosidase Purification Thermostability Fungus Medical Microbiology Soil Science & Conservation Plant Sciences Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Microbiology

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