Molecular Properties and Activity of a Carboxyl-Terminal Truncated Form of Xylanase 3 from Aeromonas caviae W-61
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概要
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Aeromonas caviae W-61 produces five species of xylanases, xylanases 1,2,3,4,and 5 [Nguyen, V.D. et al., Biosci. Biotechnol. Biochem., 56,1708-1712 (1993) and Appl. Environ. Microbiol., 57,445-449 (1991)]. While preserving a purified xylanase 3 preparation from A. caviae in solution at 4℃, the xylanase 3 was found to be proteolyzed to give a truncated form with a smaller molecular mass than that of the intact one. It appears likely that the truncated form of xylanase 3 was produced in this particular purification experiment by the action of a contaminating protease. We isolated the truncated form of xylanase 3 (Xyn3tr), of which the C-terminal 102-residue segment is missing. By the chemical analysis of the N-and C-terminal amino acid residues of Xyn3tr and the DNA sequencing analysis of the xylanase 3 gene (xyn3), the N-terminal 398th proline residue of xylanase 3 was found to be the Cterminus of Xyn3tr. Xyn3tr had the activity to form xylotriose (X3), xylotetraose (X4), xylopentaose (X5), and xylohexaose (X6) as main final products from oat spelt xylan. In contrast, intact xylanase 3 released X6 and higher xylo-oligosaccharides as main products. Xylanase 3 hydrolysed X4 through X6. However, Xyn3tr had no activity towards X4 and X5. The recombinant Xyn3tr (XYN3tr) and recombinant xylanase 3 (XYN3) were purified homogeneously from the periplasmic space of E. coli harboring the plasmids pXYN3 and pXYN3tr, which include xyn3 and xyn3tr genes, respectively, and their enzymatic activities were measured. The cleavage patterns of oat spelt and xylo-oligosaccharides by XYN3tr were identical with that by intact Xyn3tr. Thus, we conclude that the C-terminal region comprising a 102-residue segment in xylanase 3 is involved in governing the molecular size of xylo-oligosaccharides cleaved from β-1,4-xylan by the enzyme and in the hydrolytic activity towards X4 and X5.
- 社団法人日本農芸化学会の論文
- 1998-08-23
著者
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Kamio Yoshiyuki
Laboratory Of Applied Microbiology Department Of Molecular And Cell Biology Graduate School Of Agric
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Kawai Yasushi
東北大学 農学研究科
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MURAMOTO Koji
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University
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金子 淳
東北大学大学院農学研究科応用微生物学分野
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Kaneko Jun
Tohoku Univ. Sendai Jpn
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村本 光二
Lab. Of Functional Biomolecules Graduate School Of Life Sciences Tohoku Univ.
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Muramoto Koji
Laboratory Of Applied Phytochemistry Tohoku University Graduate School Of Agricultural Science
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Muramoto Koji
Department Biomolecular Science Tohoku University
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金子 淳
東北大農化
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Kaneko Jun
Laboratory Of Applied Microbiology Department Of Microbial Biotechnology Graduate School Of Agricult
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Kaneko Jun
Department Of Applied Microbiology Graduate School Of Agricultural Science Tohoku University
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TOMITA Toshio
Department of Applied Microbiology, Graduate School of Agricultural Science, Tohoku University
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KAMIO Yoshiyuki
Department of Applied Microbiology, Graduate School of Agricultural Science, Tohoku University
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OKAI Naoko
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University
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FUKASAKU Masashi
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University
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OKAI Naoko
Laboratory of Applied Microbiology Tohoku University Graduate School of Agricultural Science
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Tomita T
Showa Sangyo Co. Ltd.
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Tomita Toshio
Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University
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Kamio Yoshiyuki
Department Of Agricultural Chemistry Tohoku University
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Fukasaku Masashi
Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University
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