Purification and Properties of Mycodextranase from Bacillus circulans NHB-1
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概要
- 論文の詳細を見る
A Gram-positive bacterium, Bacillus circulans, isolated from soil was found to produce an enzyme hydrolyzing nigeran (mycodextran, alternating α-1,3- and α-1,4-linked glucan). The molecular weight of the purified enzyme was 120,000 and its isoelectric point was 8.30. The optimum pH and temperature for the enzyme activity were 6.0 and 50℃, respectively. The enzyme was stable in the pH range from 6.0 to 7.0 and up to 50℃. The K_m (mg/ml) for nigeran was 1.37. The enzyme specifically hydrolyzed the nigeran into nigerose and nigeran tetrasaccharide by an endo-type action, indicating that it is a mycodextranase (EC 3.2.1.61) cleaving only the α-1,4-glucosidic linkages in nigeran. The N-terminal amino acid sequence of the purified enzyme of B.circulans (APTVYEAESAAKTGGV) was different froom that of the mycodexstranase purified from Streptomyces sp. J-13-3 (XDPGDPTDPDPSGVGATLPF).
- 社団法人日本生物工学会の論文
- 1995-04-25
著者
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Hayakawa Shigeru
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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JIN Sheng
Department of Plastic Surgery, Inha University College of Medicine
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OKAZAKI Katsuichiro
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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SAWAMURA Yutaka
Department of Neurosurgery, Hokkaido University Hospital
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Hayakawa Shigeru
Department Of Applied Biological Science Faculty Of Agriculture Kagawa University
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Jin Sheng
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Sawamura Yutaka
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Okazaki Katsuichiro
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Okazaki Katsuichiro
Department Of Applied Biological Science Faculty Of Agriculture Kagawa University
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