- 著者
- Awanthi Mahanama Geegana Gamage Saki Nagamoto Hirosuke Oku Kanefumi Kitahara Teruko Konishi
- 出版者
- The Japanese Society of Applied Glycoscience
- 雑誌
- Journal of Applied Glycoscience (ISSN:13447882)
- 巻号頁・発行日
- pp.jag.JAG-2022_0004, (Released:2022-11-01)
Algal sulfated polysaccharides are known to be effective hyaluronidase inhibitors. We evaluated hyaluronidase inhibitory activity of sulfated polysaccharide (SP) from Caulerpa lentillifera. Results showed that SP with IC50 of 163 μg/mL appears to allosterically inhibit the hyaluronidase activity. Main sugar composition and sulfate content of SP was estimated to be Gal, Glc, Xyl, Man, uronic acids and sulfate in the weight percent of 27.7: 28.9: 14.6: 22.5: 3.4: 21.7. We modified the SP by desulfation and partial hydrolysis with trifluoroacetic acid (TFA) to investigate the effect of sulfate content and molecular weight on inhibition. Hyaluronidase inhibitory activity of desulfated SP, 0.1 M TFA-hydrolyzed SP and 0.5 M TFA-hydrolyzed SP were significantly lower than that of native SP, revealing that sulfate content or molecular weight is important for hyaluronidase inhibition.
- 著者
- Yuki Sasaki Nami Togo Kanefumi Kitahara Kiyotaka Fujita
- 出版者
- The Japanese Society of Applied Glycoscience
- 雑誌
- Journal of Applied Glycoscience (ISSN:13447882)
- 巻号頁・発行日
- vol.65, no.2, pp.23-30, 2018-05-20 (Released:2018-05-20)
- 参考文献数
- 27
- 被引用文献数
- 5
β-L-Arabinopyranosidases are classified into the glycoside hydrolase family 27 (GH27) and GH97, but not into GH36. In this study, we first characterized the GH36 β-L-arabinopyranosidase BAD_1528 from Bifidobacterium adolescentis JCM1275. The recombinant BAD_1528 expressed in Escherichia coli had a hydrolytic activity toward p-nitrophenyl (pNP)-β-L-arabinopyranoside (Arap) and a weak activity toward pNP-α-D-galactopyranoside (Gal). The enzyme liberated L-arabinose efficiently not from any oligosaccharides or polysaccharides containing Arap-β1,3-linkages, but from the disaccharide Arap-β1,3-L-arabinose. However, we were unable to confirm the in vitro fermentability of Arap-β1,3-Ara in B. adolescentis strains. The enzyme also had a transglycosylation activity toward 1-alkanols and saccharides as acceptors.
- 著者
- Michiko Shimokawa Kanefumi Kitahara Kiyotaka Fujita
- 出版者
- 日本応用糖質科学会
- 雑誌
- Journal of Applied Glycoscience (ISSN:13447882)
- 巻号頁・発行日
- pp.jag.JAG-2014_006, (Released:2014-11-04)
- 被引用文献数
- 5
We characterized a β-L-arabinopyranosidase AbpBL (BLLJ_1823) belonging to the glycoside hydrolase family 27 (GH27) from Bifidobacterium longum subsp. longum JCM1217. The recombinant AbpBL expressed in Escherichia coli hydrolyzed pNP-β-L-arabinopyranoside but not pNP-α-D-galactopyranoside. The enzyme also liberated L-arabinose from the β-L-arabinopyranosyl side chain of larch wood arabinogalactan. However, we could not detect any β-L-arabinopyranosidase activity or remarkable transcriptional induction in cultured cells of B. longum subsp. longum. Mutagenesis experiments revealed that I56D and I56A mutants both exhibited β-L-arabinopyranosidase and α-D-galactopyranosidase activities. AbpBL Ile-56 residue is a critical residue for the specificity of β-L-arabinopyranosidase.