Characterization of an acidophilic α-amylase from Aspergillus niger RBP7 and study of catalytic potential in response to nutritionally important heterogeneous compound

Authors

  • Riddha Mukherjee
  • Tanmay Paul
  • Suman Kumar Halder
  • Jyoti Prakash Soren
  • Amrita Banerjee
  • Keshab Chandra Mondal
  • Bikash Ranjan Pati
  • Pradeep Kumar Das Mohapatra

DOI:

https://doi.org/10.14232/abs.2018.1.75-82

Keywords:

characterization, digestion of food material, molecular weight determination, purification

Abstract

An acidophilic α-amylase from Aspergillus niger 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 Km and Vmax 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 Hg2+ 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, i.e. the mixture of rice, fish, bread and curry with comparable activity to the commercial diastase enzymes available.

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References

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Published

2018-08-23

How to Cite

Mukherjee, R., Paul, T., Halder, S. K., Soren, J. P., Banerjee, A., Mondal, K. C., Pati, B. R. and Mohapatra, P. K. D. (2018) “Characterization of an acidophilic α-amylase from Aspergillus niger RBP7 and study of catalytic potential in response to nutritionally important heterogeneous compound”, Acta Biologica Szegediensis, 62(1), pp. 75–82. doi: 10.14232/abs.2018.1.75-82.

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