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The filamentous fungi from the Huanghai sea sludge were screened according to their ability to produce cold-active α-amylase. The strain with the highest amylase activity was identified as Penicillium species. The α-amylase purified by ammonium sulphate precipitation and column chromatography on DEAE-sepharose and sephadex G-100 shows a molecular weight of about 55000 and a pI of 4.38. The enzyme is stable in a pH range of 5.5—8.0 and has a maximum activity at pH 6.0. Compared with the α-amylase from mesophiles and thermophiles, the cold-active enzyme shows a high enzyme activity at lower temperatures and a high sensitivity at temperatures higher than 50 ℃. The optimal temperature is 40 ℃ and the activity decreases dramatically at temperatures above 50 ℃. Ca 2+ shows a significant effect on maintaining the structure and the activity of the enzyme. EDTA and Cu 2+ are its inhibitors. The products from the hydrolysis of soluble starch with the cold-active enzyme are maltose and other oligosaccharides.
The strain with the highest amylase activity was identified as Penicillium species. The α-amylase purified by ammonium sulphate precipitation and column chromatography on DEAE -sepharose and sephadex G-100 shows a molecular weight of about 55000 and a pI of 4.38. The enzyme is stable in a pH range of 5.5-8.0 and has a maximum activity at pH 6.0. Compared with α-amylase from mesophiles and thermophiles, the cold-active enzyme shows a high enzyme activity at lower temperatures and a high sensitivity at temperatures higher than 50 ° C. The optimal temperature is 40 ° C. and the activity decreases dramatically at temperatures above 50 ° C. Ca 2+ shows a significant effect on maintaining the structure and activity of the enzyme. EDTA and Cu 2+ are its inhibitors. The products from the hydrolysis of soluble starch with the cold-active enzyme are ma ltose and other oligosaccharides.