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 language | English |
|---|---|
| Pages (from-to) | 62-65 |
| Number of pages | 4 |
| Journal | Bioscience, biotechnology, and biochemistry |
| Volume | 56 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1992 Jan 1 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
Cite this
Purification and Some Properties of an Alkaline Pullulanase from Alkalophilic Bacillus sp. KSM-1876. / Ara, Katsutoshi; Igarashi, Kazuaki; Saeki, Katsuhisa; Kawai, Shuji; Ito, Susumu.
In: Bioscience, biotechnology, and biochemistry, Vol. 56, No. 1, 01.01.1992, p. 62-65.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and Some Properties of an Alkaline Pullulanase from Alkalophilic Bacillus sp. KSM-1876
AU - Ara, Katsutoshi
AU - Igarashi, Kazuaki
AU - Saeki, Katsuhisa
AU - Kawai, Shuji
AU - Ito, Susumu
PY - 1992/1/1
Y1 - 1992/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0001763247&partnerID=8YFLogxK
U2 - 10.1271/bbb.56.62
DO - 10.1271/bbb.56.62
M3 - Article
AN - SCOPUS:0001763247
VL - 56
SP - 62
EP - 65
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 1
ER -