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Identification of a Key Enzyme for the Hydrolysis of beta-(1 -> 3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide from Bifidobacterium Adolescentis
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| Title: | Identification of a Key Enzyme for the Hydrolysis of beta-(1 -> 3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide from Bifidobacterium Adolescentis |
| Authors: | Kobayashi, Manami Browse this author | | Kumagai, Yuya Browse this author →KAKEN DB | | Yamamoto, Yohei Browse this author | | Yasui, Hajime Browse this author →KAKEN DB | | Kishimura, Hideki Browse this author →KAKEN DB |
| Keywords: | red alga | | dulse | | xylooligosaccharide | | beta-(1 -> 3)/beta-(1 -> 4)-xylan | | Bifidobacterium | | GH43 | | beta-xylosidase |
| Issue Date: | Mar-2020 |
| Publisher: | MDPI |
| Journal Title: | Marine drugs |
| Volume: | 18 |
| Issue: | 3 |
| Start Page: | 174 |
| Publisher DOI: | 10.3390/md18030174 |
| Abstract: | 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. |
| Rights: | https://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/78490 |
| Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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