<i>Vibrio</i> sp. AP-2の産生するβ-アガラーゼの精製と特性
書誌事項
- タイトル別名
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- Purification and characterization of .BETA.-agarases from Vibrio sp. AP-2.
- Vibrio sp.AP-2の産生するβ-アガラーゼの精製と特性〔英文〕
- Vibrio sp.AP-2 ノ サンセイスル ベータ アガラーゼ ノ セイセ
- Purification and characterization of β-agarases from Vibrio sp. AP-2
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抄録
β-Agarases were purified from the culture fluid of a marine bacterium, Vibrio sp. AP-2, by am-monium sulfate precipitation, successive column chromatography, and nuclease treatment. The final enzyme preparations appeared to be homogeneous on polyacrylamide gel electrophoresis. The enzymes (agarases-a, -b, and-c) had molecular weight of 34, 000, 20, 000, and 18, 000 daltons, and the pH optimum of 6.5, 5.5, 7.0, respectively, and were stable in a pH region from 4.0 to 9.0, and at temperatures below 45°C. The agarases were β-agarase which degraded agar to yield neoagaro-oligosaccharides. Agarase-a and agarase-c hydrolyzed agar to give neoagarotetraose as the pre-dominant product, agarase-b gave neoagarobiose as the predominant product. The three enzymes did not react with κ-carrageenan.
収録刊行物
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- 日本水産学会誌
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日本水産学会誌 56 (5), 825-830, 1990
公益社団法人 日本水産学会
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詳細情報
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- CRID
- 1390001206412747136
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- NII論文ID
- 130001545036
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- NII書誌ID
- AN00193422
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- COI
- 1:CAS:528:DyaK3cXlsVOlu7k%3D
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- ISSN
- 1349998X
- 00215392
- http://id.crossref.org/issn/00215392
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- NDL書誌ID
- 3671230
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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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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可