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

Abstract

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). Biochemical characterization was performed on 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. Using soluble starch as the substrate, and were 5 mg mL and 1000 U mg, 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).

The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

“…Based on these results, the pNPG was chosen as the specific substrate of the PersiAlpha‐GL1 for further experiments. These results are in agreement with previous studies that used pNPG as the specific substrate for α‐glucosidase (da Silva et al, 2009; del Moral et al., 2018).…”

“…Addition of the cationic surfactant (CTAB) showed 70.53% α‐glucosidase activity and the enzyme was highly stable in the presence of the anionic surfactant (SDS) and non‐ionic surfactants (Tween 20 and TritonX100) showing 85.99%, 90.09%, and 92.51% activities, respectively. Similarly, the novel stable α‐glucosidase was not affected by surfactants and EDTA (del Moral et al., 2018). Moreover, addition of different chemical modulators (Urea, PMSF, NaN 3 ) did not inhibit the activity of the PersiAlpha‐GL1.…”

High Adsorption of α-Glucosidase on Polymer Brush-Modified Anisotropic Particles Acquired by Electrospraying—A Combined Experimental and Simulation Study

“…Hence, a significant binding and almost no release of the enzyme were observed at pH 6.8. Moreover, experiments at pH 4 were not successful as the enzyme did not display any significant activity at this pH, as reported by others also …”

Metabolite Profiling and Anti-Aging Activity of Rice Koji Fermented with Aspergillus oryzae and Aspergillus cristatus: A Comparative Study

“…Enzymatic activity assays for α-amylase, β-glucosidase, and α-glucosidase were performed according to previous studies [25,40,41]. A 10 g quantity of each rice koji sample was extracted in 90 mL of water by shaking on an orbital shaker at 120 rpm and 25 • C for 1 h. After filtering the samples, the supernatants were used to evaluate enzyme activities.…”