Purification, biochemical characterization, and genetic cloning of the phytase produced by <i>Burkholderia</i> sp. strain a13
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- Graminho Eduardo Rezende
- Faculty of Life and Environmental Sciences, University of Tsukuba
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- Takaya Naoki
- Faculty of Life and Environmental Sciences, University of Tsukuba
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- Nakamura Akira
- Faculty of Life and Environmental Sciences, University of Tsukuba
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- Hoshino Takayuki
- Faculty of Life and Environmental Sciences, University of Tsukuba
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説明
A phytase-producing bacterium, Burkholderia sp. a13 (JCM 30421), was isolated from Lake Kasumigaura by enrichment cultivation using minimum medium containing phytic acid as the sole phosphorus source. The phytase production by strain a13 was induced by the presence of phytic acid and repressed by the addition of glucose. The purified enzyme had a molecular weight of 44 kDa and a phytase activity of 174 μmol min–1 mg–1. The enzyme showed broad substrate specificity, but the highest activity was observed with phytic acid. The enzyme activity was strongly inhibited by Cu2+, Zn2+, Hg2+, and iodoacetic acid, indicating the requirement of a thiol group for the activity. Genetic cloning reveals that the mature portion of this enzyme consists of 428 amino acids with a calculated molecular weight of 46 kDa. The amino acid sequence showed the highest similarity to the phytase produced by Hafnia alvei with 48% identity; it also contained histidine acid phosphatase (HAP) motifs (RHGXRXP and HD), indicating the classification of this enzyme in the HAP phytase family. We have successfully expressed the cloned gene in Escherichia coli from its putative initiation codon, showing that the gene actually encodes the phytase.
収録刊行物
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- The Journal of General and Applied Microbiology
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The Journal of General and Applied Microbiology 61 (1), 15-23, 2015
公益財団法人 応用微生物学・分子細胞生物学研究奨励会
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詳細情報 詳細情報について
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- CRID
- 1390282679124727296
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- NII論文ID
- 130005061415
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- NII書誌ID
- AA00698664
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- ISSN
- 13498037
- 00221260
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- HANDLE
- 2241/00125308
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- PubMed
- 25833676
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- 本文言語コード
- en
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- データソース種別
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- IRDB
- Crossref
- PubMed
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