Cloning and Nucleotide Sequence of the β-D-Glucosidase Gene from Bifidobacterium breve clb,and Expression of β-D-Glucosidase Activity in Escherichia coli
書誌事項
- タイトル別名
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- Cloning and Nucleotide Sequence of the .BETA.-D-Glucosidase Gene from Bifidobacterium breve clb, and Expression of .BETA.-D-Glucosidase Activity in Escherichia coli.
- Cloning and Nucleotide Sequence of the
- Cloning and Nucleotide Sequence of the<i>β</i>-<scp>d</scp>-Glucosidase Gene from<i>Bifidobacterium breve</i>clb, and Expression of<i>β</i>-<scp>d</scp>-Glucosidase Activity in<i>Escherichia coli</i>
- Cloning and nucleotide sequence of the β-D-glucosidase gene from Bifidobacterium breve clb, and expression of β-D-glucosidase activity in Escherichia coli.
- 公開日
- 1996
- 資源種別
- journal article
- DOI
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- 10.1271/bbb.60.2011
- 公開者
- 公益社団法人 日本農芸化学会
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説明
Genomic DNA encoding a β-D-glucosidase (EC 3.2.1.21), which has β-D-fucosidase activity, was cloned from Bifidobacterium breve clb. We sequenced a 1.9-kbp cloned DNA fragment that contained a single open reading frame encoding 460 amino acids with a calculated molecular mass of 51, 513 Da. A putative ribosome binding site was found 5 bp upstream of the initiation codon. The amino acid sequence of this β-D-glucosidase from Bifidobacterium breve clb had 46% identity with that of β-glucosidase from Microbispore bispore. The enzyme of Bifidobacterium breve clb was expressed in Escherichia coli. A cell-free extract prepared from the recombinant strain showed 80 to 90-fold more β-D-glucosidase activity than that from Bifidobacterium breve clb. The recombinant enzyme was purified to homogeneity from cell-free extracts of the recombinant strain using 4 column chromatographies. The recovery of enzyme from the recombinant strain was about 138-fold-higher than that of Bifidobacterium breve clb. The enzymatic properties were similar to those of Bifidobacterium breve clb. For application of this recombinant enzyme, we attempted to synthesize a disaccharide that seemed to be specifically assimilated by Bifidobacteria using the condensation activity of the enzyme.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 60 (12), 2011-2018, 1996
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681452807296
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- NII論文ID
- 110002678423
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DyaK2sXis1Klsw%3D%3D
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- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/09168451
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- NDL書誌ID
- 4109625
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- PubMed
- 8988633
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- JaLC
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- Crossref
- PubMed
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