Purification and Some Properties of Ichoimo β-Amylase(Biological Chemistry)
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概要
- 論文の詳細を見る
An amylase was purified from tubers of ichoimo, a cultivar of yam (Dioscorea batatas), and its basic properties were investigated. The enzyme was purified by acid treatment of crude extracts at pH4.5, DEAE-Toyopearl 650S ion-exchange chromatography, and hydrophobic chromatography using Butyl-Toyopearl 650S to a state showing a single band on SDS polyacrylamide gel electrophoresis (PAGE). The purified enzyme had a specific activity of 161U/mg protein. It has a molecular mass of 60,000 Da on SDS-PAGE, optimum pH of 6.0, optimum temperature of 55℃, and a stable pH range of 4.3 to 8.5. On isoelectric focusing PAGE it gave two protein bands with pI's of 5.0 and 5.2. It produced maltose as a sole low molecular weight product from soluble starch and did not act on cyclodextrins. The anomeric form of the maltose was identified as the β-form. These results confirmed that the purified enzyme is a β-amylase.
- 社団法人日本農芸化学会の論文
- 1991-02-23
著者
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Taniguchi Hajime
National Food Research Institute
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Kawabata Akiko
Tokyo University Of Agriculture
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ARAI Teiko
Toyokogakuen Women's Junior College
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Arai Teiko
Toyokogakuen Women's Junior College
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Taniguchi Hajime
National Food Research Insitute, Ministry of Agricultuer, Forestry and Fisheries
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