@article{Mukherjee_Paul_Halder_Soren_Banerjee_Mondal_Pati_Mohapatra_2018, title={Characterization of an acidophilic α-amylase from Aspergillus niger RBP7 and study of catalytic potential in response to nutritionally important heterogeneous compound}, volume={62}, url={https://abs.bibl.u-szeged.hu/index.php/abs/article/view/2946}, DOI={10.14232/abs.2018.1.75-82}, abstractNote={<p>An acidophilic α-amylase from <em>Aspergillus niger</em> RBP7 was purified after solid state fermentation on potato peel substrate. Molecular mass of the purified α-amylase was 37.5 kDa and it exhibited 1.4 mg/ml and 0.992 μ/mol/min K<sub>m</sub> and V<sub>max</sub> values, respectively. The enzyme was stable in the pH range from 2.0 to 6.0, at high NaCl concentration (3 M) and at temperatures between 40 °C and 70 °C. The enzyme showed an optimal activity at pH 3.0 and at 45 °C. The enzyme was inhibited by Hg<sup>2+</sup> and was stable in the presence of different surfactants (Tween 60, Tween 80, and SDS at 1% level) and different inhibitory reagents (β-mercaptoethanol, phenylmethylsulfonyl fluoride, and sodium azide). This acidophilic amylase enzyme can digest heterogeneous food materials, <em>i.e.</em> the mixture of rice, fish, bread and curry with comparable activity to the commercial diastase enzymes available.</p>}, number={1}, journal={Acta Biologica Szegediensis}, author={Mukherjee, Riddha and Paul, Tanmay and Halder, Suman Kumar and Soren, Jyoti Prakash and Banerjee, Amrita and Mondal, Keshab Chandra and Pati, Bikash Ranjan and Mohapatra, Pradeep Kumar Das}, year={2018}, month={Aug.}, pages={75–82} }