Identification of a Key Enzyme for the Hydrolysis of beta-(1 -> 3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide from Bifidobacterium Adolescentis

Kobayashi, Manami; Kumagai, Yuya; Yamamoto, Yohei; Yasui, Hajime; Kishimura, Hideki

Identification of a Key Enzyme for the Hydrolysis of beta-(1 -> 3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide from Bifidobacterium Adolescentis

Kobayashi, Manami; Kumagai, Yuya; Yamamoto, Yohei et al.

Marine drugs, 2020, 18(3), 174

Permalink : https://hdl.handle.net/2115/78490

このアイテムのアクセス数:794件（2026-08-25 04:13 集計）

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https://doi.org/10.3390/md18030174			34

論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/78490
タイトル	Identification of a Key Enzyme for the Hydrolysis of beta-(1 -> 3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide from Bifidobacterium Adolescentis
著者	Kobayashi, Manami ; Kumagai, Yuya ; Yamamoto, Yohei ; Yasui, Hajime ; Kishimura, Hideki
著者名 Kobayashi, Manami
e-Rad_Researcher 00589997 著者名 Kumagai, Yuya
著者名 Yamamoto, Yohei
e-Rad_Researcher 00200494 著者名 Yasui, Hajime
e-Rad_Researcher 50204855 著者名 Kishimura, Hideki
言語	英語
キーワード	red alga
	dulse
	xylooligosaccharide
	beta-(1 -> 3)/beta-(1 -> 4)-xylan
	Bifidobacterium
	GH43
	beta-xylosidase
発行日	2020-03
出版者	MDPI
収録物名	Marine drugs
巻(号)	18(3)
ページ	174
抄録	Red alga dulse possesses a unique xylan, which is composed of a linear beta-(1 -> 3)/beta-(1 -> 4)-xylosyl linkage. We previously prepared characteristic xylooligosaccharide (DX3, (beta-(1 -> 3)-xylosyl-xylobiose)) from dulse. In this study, we evaluated the prebiotic effect of DX3 on enteric bacterium. Although DX3 was utilized by Bacteroides sp. and Bifidobacterium adolescentis, Bacteroides Ksp. grew slowly as compared with beta-(1 -> 4)-xylotriose (X3) but B. adolescentis grew similar to X3. Therefore, we aimed to find the key DX3 hydrolysis enzymes in B. adolescentis. From bioinformatics analysis, two enzymes from the glycoside hydrolase family 43 (BAD0423: subfamily 12 and BAD0428: subfamily 11) were selected and expressed in Escherichia coli. BAD0423 hydrolyzed beta-(1 -> 3)-xylosyl linkage in DX3 with the specific activity of 2988 mU/mg producing xylose (X1) and xylobiose (X2), and showed low activity on X2 and X3. BAD0428 showed high activity on X2 and X3 producing X1, and the activity of BAD0428 on DX3 was 1298 mU/mg producing X1. Cooperative hydrolysis of DX3 was found in the combination of BAD0423 and BAD0428 producing X1 as the main product. From enzymatic character, hydrolysis of X3 was completed by one enzyme BAD0428, whereas hydrolysis of DX3 needed more than two enzymes.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
権利情報	Creative Commons Attribution 4.0 International
PISSN	1660-3397
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.3390/md18030174