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

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

doi:10.1271/bbb.56.62

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 journal › Article › peer-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 language	English
Pages (from-to)	62-65
Number of pages	4
Journal	Bioscience, biotechnology, and biochemistry
Volume	56
Issue number	1
DOIs	https://doi.org/10.1271/bbb.56.62
Publication status	Published - 1992 Jan 1
Externally published	Yes

ASJC Scopus subject areas

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

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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.",

author = "Katsutoshi Ara and Kazuaki Igarashi and Katsuhisa Saeki and Shuji Kawai and Susumu Ito",

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

Abstract

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