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

2010; Academic Journals; Volume: 4; Issue: 6 Linguagem: Inglês

10.5897/ajbr.9000198

1996-0778

Tahar Nouadri, Zahia Meraïhi, Djekrif-Dakhmouche Shahrazed, Leila Bennamoun,

Phytase and its Applications

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.