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- Padmajanti Anastasia
- Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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- 殿塚 隆史
- 東京農工大学農学部応用生物科学科
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- 坂野 好幸
- 東京農工大学農学部応用生物科学科
書誌事項
- タイトル別名
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- Deglycosylated Isopullulanase Retains Enzymatic Activity.
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抄録
Isopullulanase (IPU) from Aspergillus niger ATCC 9642 is a cell-bound glycoprotein that hydrolyzes pullulan into isopanose. The sugar content of the recombinant enzyme expressed in Aspergillus oryzae M-2-3 decreased from 33.8 to 2.1% by 13 h-treatment with endoglycosidase H (Endo H), and deglycosylated rec-IPU had 65% of the original activity. 3 Deg-IPU (prepared by 3 h-treatment of Endo H; 6.8% sugar) showed the same substrate specificities, optimum pH and optimum temperature as native IPU and rec-IPU, while its kinetic parameters, ko and ko/Km values for pullulan, and Km, ko and ko/Km values for panose decreased with deglycosylation, except Km for pullulan. The oligosaccharide chains of rec-IPU were typed using lectin-peroxidase reagents and classified as hybrid- and/or high-mannose types.
収録刊行物
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- Ｊｏｕｒｎａｌ ｏｆ Ａｐｐｌｉｅｄ Ｇｌｙｃｏｓｃｉｅｎｃｅ
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Ｊｏｕｒｎａｌ ｏｆ Ａｐｐｌｉｅｄ Ｇｌｙｃｏｓｃｉｅｎｃｅ 47 (3/4), 287-292, 2000
日本応用糖質科学会
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詳細情報 詳細情報について
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- CRID
- 1390001206292560896
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- NII論文ID
- 10008252053
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- NII書誌ID
- AN10453916
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- COI
- 1:CAS:528:DC%2BD3cXmvVahsr0%3D
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- ISSN
- 18807291
- 13447882
- http://id.crossref.org/issn/13447882
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- NDL書誌ID
- 5521363
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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
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可