書誌事項
- タイトル別名
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- Heterologous Production and Characterization of Arthrobacter globiformis T6 Isomalto-dextranase
抄録
Efficient production of an isomalto-dextranase from Arthrobacter globiformis T6 has been achieved in Escherichia coli. The combination of an expression vector lacking the region for the signal peptide, cultivation at 25°C, and optimization of E. coli cells allows us to produce the isomalto-dextranase at more than 1000 times the amount under the original conditions, which then enables us to characterize the enzyme in detail. The primary structure of the isomalto-dextranase from A. globiformis T6 has a distant similarity with enzymes belonging to glycosyl hydrolase family 27, which comprises mainly α-galactosidases and α-N-acetylgalactosaminidases. Therefore, the reaction of the isomalto-dextranase for melibiose, a substrate for α-galactosidases, has also been investigated. The isomalto-dextranase did not hydrolyze melibiose or p-nitrophenyl α-D-galactoside. The Ki values for isomaltose and maltose were 2.3 and 7.8 mM, respectively, while melibiose scarcely inhibited the activity of the isomalto-dextranase. Moreover, melibiose was a poor acceptor for the transglycosylation with dextran, and the maximum accumulation of the transglycosylation product was 12-fold less than that for isomaltose. The findings indicated here that the isomalto-dextranase is highly specific for the glucosyl moiety in both hydrolysis and transglycosylation.
収録刊行物
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 51 (1), 27-32, 2004
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
- 1390282681269523328
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- NII論文ID
- 130004480797
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- COI
- 1:CAS:528:DC%2BD2cXhtFajtLw%3D
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- ISSN
- 18807291
- 13447882
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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
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可