African Journal of
Biochemistry Research

  • Abbreviation: Afr. J. Biochem. Res.
  • Language: English
  • ISSN: 1996-0778
  • DOI: 10.5897/AJBR
  • Start Year: 2007
  • Published Articles: 424

Full Length Research Paper

Purification and characterization of the α-amylase isolated from Penicillium camemberti PL21

Tahar Nouadri*, Zahia Meraihi, Djekrif-Dakhmouche Shahrazed and Bennamoun Leila
Research Laboratory in Enzymatic Engineering, Department of Biochemistry and Microbiology, Mentouri- University, Constantine- Algeria.
Email: [email protected]

  •  Accepted: 11 June 2010
  •  Published: 30 June 2010


The amylase family of enzymes is a great significance due to its wide area of potential application. α-amylase from Penicillium camemberti PL21 obtained from I. N. A. (The technological laboratory of Agriculture National Institute Paris- France) and using orange waste as substrates was produced under optimum conditions, after 168 h of incubation and subjected for purification and characterization. The enzyme was purified by ammonium sulfate precipitation, dialysis, Sephadex G-100 and DEAE-Sepharose CL-6B column chromatography. A trial for the purification of α-amylase resulted in an enzyme with specific activity of (154.2 units/ml/mg protein) with (38.5 folds) purification .The α-amylase activity increased by enzyme concentration rise. The optimum substrate concentration for soluble starch was 1 % (w/v) while the optimum incubation temperature was 30ºC. The purified α-amylase enzyme had a maximum activity at pH 6 and the Km value for solublestarch was 0.92 mg/ml. Analyses of this enzyme for molecular mass was  carried out by SDS-PAGE electrophoresis, which revealed one band 60. 5 Kda.


Key words: Penicillium camemberti PL21, α-amylase, purification, SDS-PAGE electrophoresis.