Literature DB >> 29259882

Production and biochemical characterization of α-glucosidase from Aspergillus niger ITV-01 isolated from sugar cane bagasse.

S Del Moral1,2, D M Barradas-Dermitz3, M G Aguilar-Uscanga2.   

Abstract

Aspergillus niger ITV-01 presents amylolytic activity, identified as α-glucosidase, an enzyme that only produces α-d-glucose from soluble starch and that presents transglucosylase activity on α-d-glucopyranosyl-(1-4)-α-d-glucopyranose (maltose) (200 gL-1). Biochemical characterization was performed on A. niger ITV-01 α-glucosidase; its optimum parameters were pH 4.3, temperature 80 °C but stable at 40 °C, with an energy of activation (Ea) 176.25 kJ mol-1. Using soluble starch as the substrate, Km and Vmax were 5 mg mL-1 and 1000 U mg-1, respectively. As α-glucosidase is not a metalloenzyme, calcium and EDTA did not have any effect on its activity. The molecular weight was estimated by SDS-PAGE to be about 75 kDa. It was also active in methanol and ethanol. When ammonium sulfate (AS) and yeast extract (YE) nitrogen sources and calcium effect were evaluated, the greatest activity occurred using YE and calcium, as opposed to AS media where no activity was detected. The results obtained showed that this enzyme has industrial application potential in the processes to produce either ethanol or malto-oligosaccharides from α-d-glucopyranosyl-(1-4)-α-d-glucopyranose (maltose).

Entities:  

Keywords:  Aspergillus niger; Calcium; Soluble starch; Yeast extract; α-glucosidase

Year:  2017        PMID: 29259882      PMCID: PMC5723575          DOI: 10.1007/s13205-017-1029-6

Source DB:  PubMed          Journal:  3 Biotech        ISSN: 2190-5738            Impact factor:   2.406


  22 in total

1.  Novel alpha-glucosidase from Aspergillus nidulans with strong transglycosylation activity.

Authors:  Naoki Kato; Sachie Suyama; Masao Shirokane; Masashi Kato; Tetsuo Kobayashi; Norihiro Tsukagoshi
Journal:  Appl Environ Microbiol       Date:  2002-03       Impact factor: 4.792

2.  Thermal stability of alpha-amylase from Aspergillus oryzae entrapped in polyacrylamide gel.

Authors:  Patcharin Raviyan; Juming Tang; Barbara A Rasco
Journal:  J Agric Food Chem       Date:  2003-08-27       Impact factor: 5.279

3.  Isolation and characterization of alpha-glucosidase from Aspergillus niger.

Authors:  K Brízová; B Králová; K Demnerová; I Vins
Journal:  J Chromatogr       Date:  1992-02-28

4.  Characteristics of alpha-glucosidase production from recombinant Aspergillus oryzae by membrane-surface liquid culture in comparison with various cultivation methods.

Authors:  Masakazu Morita; Hiroko Shimamura; Natsuko Ishida; Koreyoshi Imamura; Takaharu Sakiyama; Kazuhiro Nakanishi
Journal:  J Biosci Bioeng       Date:  2004       Impact factor: 2.894

5.  Thermal stability and energy of deactivation of free and immobilized amyloglucosidase in the saccharification of liquefied cassava starch.

Authors:  G M Zanin; F F De Moraes
Journal:  Appl Biochem Biotechnol       Date:  1998       Impact factor: 2.926

Review 6.  Molecular mechanism in alpha-glucosidase and glucoamylase.

Authors:  S Chiba
Journal:  Biosci Biotechnol Biochem       Date:  1997-08       Impact factor: 2.043

7.  Purification and characterization of an intracellular α-glucosidase with high transglycosylation activity from A. niger M-1.

Authors:  Yun-kai Zhang; Wei Li; Kong-yang Wu; Gui-guang Chen; Zhi-qun Liang
Journal:  Prep Biochem Biotechnol       Date:  2011       Impact factor: 2.162

Review 8.  α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.

Authors:  Masayuki Okuyama; Wataru Saburi; Haruhide Mori; Atsuo Kimura
Journal:  Cell Mol Life Sci       Date:  2016-04-30       Impact factor: 9.261

9.  Purification and biochemical characterization of an alpha-glucosidase from Xanthophyllomyces dendrorhous.

Authors:  Dolores Marín; Dolores Linde; María Fernández Lobato
Journal:  Yeast       Date:  2006-01-30       Impact factor: 3.239

10.  Aspergillus niger genome-wide analysis reveals a large number of novel alpha-glucan acting enzymes with unexpected expression profiles.

Authors:  Xiao-Lian Yuan; Rachel M van der Kaaij; Cees A M J J van den Hondel; Peter J Punt; Marc J E C van der Maarel; Lubbert Dijkhuizen; Arthur F J Ram
Journal:  Mol Genet Genomics       Date:  2008-03-05       Impact factor: 3.291

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