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KMID : 0380020040190040301
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Korean Journal of Biotechnology and Bioengineering
2004 Volume.19 No. 4 p.301 ~ p.307
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Characteristics of α-Amylase of, a New Species, Aspergillus coreanus NR 15-1
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Lee Sang-Hoon
Jung Hyuk-Jun
Yeo Soo-Hwan
Kim Hyun-Su
Yoo Dae-Sik
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Abstract
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The characteristics of the a-amylase of Aspergillus coreanus NR 15-1 isolated from traditional Korean Nuruk have been carried out. The a-amylase of A. coreanus NR 15-1 was purified by ammonium sulfate precipitation followed by column chromatographies on CM-cellulose, DEAE-cellulose, Sephadex G-100 gel filtration and hydroxyapatite. The a-amylase was purified 78-fold with a yield of 8.7%. The molecular weight of the a-amylase was estimated to be 49 kDa by Sephadex G-100 gel filtration and 51 kDa by SDS-polyacrylamide gel eletrophoresis. These experimental results suggested that the purified enzyme might be monomer. The enzyme was stable between pH 4 and 11. The optimum pH was 5.0. The optimum temperature for enzyme was 45 and the enzyme was stable up to 50. The enzyme was significantly inhibited by 1 mM N-bromosuccinimide. These results suggested that tryptophan residue was involved in the active site of a-amylase. The enzyme was identified as a-amylase because the reaction products of soluble starch hydrolyzed by the purified enzyme was oligosaccharide by thin layer chromatography.
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KEYWORD
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Aspergillus coreanus NR 15-1, α-amylase
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