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

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

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)62-65
Number of pages4
JournalBioscience, biotechnology, and biochemistry
Volume56
Issue number1
DOIs
Publication statusPublished - 1992 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Purification and Some Properties of an Alkaline Pullulanase from Alkalophilic Bacillus sp. KSM-1876'. Together they form a unique fingerprint.

Cite this