Purification and Some Properties of an Alkaline Pullulanase from Alkalophilic Bacillus sp. KSM-1876

Katsutoshi Ara, Kazuaki Igarashi, Katsuhisa Saeki, Shuji Kawai, Susumu Ito

研究成果: Article査読

42 被引用数 (Scopus)

抄録

A novel alkaline pullulanase (pullulan 6-glucanohydrolase, EC 3.2.1.41) was purified to homogeneity from the culture filtrate of the alkalophilic Bacillus sp. KSM-1876. The pullulanase had an optimum pH for activity of around 10.0-10.5, which is the highest pH for optimum activity of any pullulanases reported to date. The optimum temperature at pH 10 was around 50°C. The enzyme had a molecular mass of 120 kDa and an isoelectric point of pH 5.2. The enzyme acted specifically on pullulan to generate maltotriose as the major end product; the Km for pullulan was 1.8mg/ml. N-Bromosuccinimide abolished the enzymatic activity, and pullulan protected the enzyme from inactivation by this tryptophan-specific oxidant, suggesting that a tryptophan residue(s) is involved in the mechanism of action of the pullulanase from Bacillus sp. KSM-1876.

本文言語English
ページ(範囲)62-65
ページ数4
ジャーナルBioscience, biotechnology, and biochemistry
56
1
DOI
出版ステータスPublished - 1992 1 1
外部発表はい

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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