African Journal of
Biotechnology

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12486

Full Length Research Paper

Partial purification and some physicochemical properties of Aspergillus flavus α-amylase isolated from decomposing cassava peels

Muinat Moronke Adeyanju*
  • Muinat Moronke Adeyanju*
  • Department of Biochemistry, Olabisi Onabanjo University, Ago-Iwoye, Ogun State, Nigeria.
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Oyesola Ojewunmi
  • Oyesola Ojewunmi
  • Department of Biochemistry, College of Medicine, University of Lagos, Lagos, Nigeria.
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Temitope Akande
  • Temitope Akande
  • Department of Biochemistry, Olabisi Onabanjo University, Ago-Iwoye, Ogun State, Nigeria.
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Esther Nkechi Ezima
  • Esther Nkechi Ezima
  • Department of Biochemistry, Olabisi Onabanjo University, Ago-Iwoye, Ogun State, Nigeria.
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Abosede Abolanle Akeredolu
  • Abosede Abolanle Akeredolu
  • Department of Microbiology, Biosciences and Biotechnology, School of Basic and Applied Sciences Babcock University, Ilishan, Ogun State, Nigeria.
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Bamidele Sanya Fagbohunka
  • Bamidele Sanya Fagbohunka
  • Department of Biochemistry, Olabisi Onabanjo University, Ago-Iwoye, Ogun State, Nigeria.
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  •  Received: 18 August 2014
  •  Accepted: 05 November 2014
  •  Published: 24 December 2014

Abstract

α-Amylase is one of the most important enzymes of great significance due to its wide area of potential application in food, fermentation, textile, paper, detergent and pharmaceutical industries. This study aimed at production of α-amylase from an indigenous fungal source and also ascertaining the properties of the enzyme for maximal activity. The enzyme was isolated from decomposing cassava peels, fractionated at 70% ammonium sulphate and characterized. The fungal isolate was characterized as Aspergillus flavus. The crude enzyme extract had a specific activity of 2.40 Umg-1 which increased to 7.88 Umg-1 on fractionation with ammonium sulphate with a yield of 11.10% and purification fold of 3.28. The Km and Vmax values of 0.52±0.009 g/dL and 62.57±0.23 U/min were obtained, respectively, at 2% cassava starch substrate. The enzyme also demonstrated maximum activity at 70°C and pH 5.0. It thus produces α-amylase which is thermostable, a property which could be exploited for industrial purposes where hydrolysis of starch and other complex carbohydrates are required.
 
Key words: Cassava, α-amylase, starch hydrolysis, Aspergillus species, industrial application.