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| Content Provider | Springer Nature Link |
|---|---|
| Author | Chandra, Muniramanna Gari Subohsh Mangamuri, Usha Kiranmayi Rather, Gulam Choi, Yong Lark Gurramkonda, Chandrasekhar Podha, Shdhakar Gudi, Satheesh Kumar |
| Copyright Year | 2013 |
| Abstract | Glucoamylase (EC 3.2.1.3) is an important group of enzymes in starch processing, also referred to as amyloglucosidases, which are exo-acting amylases that release glucose from the nonreducing end of starch and related oligosaccharides. The glucoamylase newly isolated from the Aspergillus niger FME) was reported for the first time. This enzyme was produced by detergent-mediated release and purified to ∼9.11 fold using Sephadex-G 100 and ion-exchange chromatography. Molecular mass of the glucoamylase was ∼36 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The product of starch hydrolysis, analysed by thin-layer chromatography, showed the presence of glucose. The optimum pH and temperature for glucoamylase activity was 5.0 and 45°C, respectively. The K $_{m}$ and V $_{max}$ values of the enzyme were also determined using soluble starch as substrate as 94 μg/mL and 39.02 U/mg, respectively. Moreover, glucoamylase was slightly activated by presence of Na and K ions and 10–20% inhibition was observed in presence of Zn$^{2+}$, Sn$^{2+}$, Mg$^{2+}$, Ni$^{2+}$, Mn$^{2+}$, and almost 80% with Cu$^{2+}$ ions, whereas the presence of ethylene diamine tetra acetic acid (EDTA) did not show significant inhibition. Glucoamylase, also assayed for surfactant property, shows significant surfactant tolerance at high concentrations of detergent and can retain 90% of its activity. Finally, secondary structure analysis of glucoamylase by circular dichroism spectroscopy showed the presence of 48% α-helix, 11% β-sheet, and 41% random structure. |
| Starting Page | 427 |
| Ending Page | 433 |
| Page Count | 7 |
| File Format | |
| ISSN | 17382203 |
| Journal | Journal of the Korean Society for Applied Biological Chemistry |
| Volume Number | 56 |
| Issue Number | 4 |
| e-ISSN | 2234344X |
| Language | English |
| Publisher | Springer Netherlands |
| Publisher Date | 2013-08-31 |
| Publisher Place | Dordrecht |
| Access Restriction | Subscribed |
| Subject Keyword | diethylaminoethyl cellulose column Aspergillus niger detergent-mediated production Applied Microbiology Biological Techniques SephadexG-100 circular dichroism enzyme kinetics Bioorganic Chemistry glucoamylase |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Biochemistry, Genetics and Molecular Biology |
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