Abstract
An extracellular acid stable α-amylase from Paecilomyces variotii ATHUM 8891 (PV8891 α-amylase) was purified to homogeneity applying ammonium sulfate fractionation, ion exchange and gel filtration chromatography and exhibited a reduced molecular weight of 75 kDa. The purified enzyme was optimally active at pH 5.0 and 60 °C and stable in acidic pH (3.0–6.0). Km, vmax and kcat for starch hydrolysis were found 1.1 g L−1, 58.5 μmole min−1 (mg protein)−1, and 73.1 s−1, respectively. Amylase activity was marginally enhanced by Ca2+ and Fe2+ ions while Cu2+ ions strongly inhibited it. Thermodynamic parameters determined for starch hydrolysis (Εα, ΔH*, ΔG*, ΔS*, \({\Delta G}_{\mathrm{E}-\mathrm{S}}^{\mathrm{*}}\) and \({\Delta G}_{\mathrm{E}-\mathrm{T}}^{\mathrm{*}}\)) suggests an effective capacity of PV8891 α-amylase towards starch hydrolysis. Thermal stability of PV8891 α-amylase was assessed at different temperatures (30–80 οC). Thermodynamic parameters (\({E}_{\left(a\right)d}\), ΔH*, ΔG*, ΔS*) as well as the integral activity of a continuous system for starch hydrolysis by the PV8891 α-amylase revealed satisfactory thermostability up to 60 °C. The acidic nature and its satisfactory performance at temperatures lower than the industrially used amylases may represent potential applications of PV8891 α-amylase in starch processing industry.
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Conceptualization: DM, DH and DK; Methodology: DM, DH; Formal analysis and investigation: MEA, SK; Writing—original draft preparation: DM; Writing—review and editing: all authors.
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Apostolidi, M.E., Kalantzi, S., Hatzinikolaou, D.G. et al. Catalytic and thermodynamic properties of an acidic α-amylase produced by the fungus Paecilomyces variotii ATHUM 8891. 3 Biotech 10, 311 (2020). https://doi.org/10.1007/s13205-020-02305-2
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DOI: https://doi.org/10.1007/s13205-020-02305-2