Characterization of neoagarooligosaccharide hydrolase BpGH117 from a human gut bacterium bacteroides plebeius

Yerin Jin, Sora Yu, Dong Hyun Kim, Eun Ju Yun, Kyoung Heon Kim

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

α-Neoagarobiose (NAB)/neoagarooligosaccharide (NAO) hydrolase plays an important role as an exo-acting 3,6-anhydro-α-(1,3)-L-galactosidase in agarose utilization. Agarose is an abun-dant polysaccharide found in red seaweeds, comprising 3,6-anhydro-L-galactose (AHG) and D-galactose residues. Unlike agarose degradation, which has been reported in marine microbes, recent metagenomic analysis of Bacteroides plebeius, a human gut bacterium, revealed the presence of genes encoding enzymes involved in agarose degradation, including α-NAB/NAO hydrolase. Among the agarolytic enzymes, BpGH117 has been partially characterized. Here, we characterized the exo-acting α-NAB/NAO hydrolase BpGH117, originating from B. plebeius. The optimal temperature and pH for His-tagged BpGH117 activity were 35 C and 9.0, respectively, indicative of its unique origin. His-tagged BpGH117 was thermostable up to 35 C, and the enzyme activity was maintained at 80% of the initial activity at a pre-incubation temperature of 40 C for 120 min. Km and Vmax values for NAB were 30.22 mM and 54.84 U/mg, respectively, and kcat /Km was 2.65 s−1 mM−1 . These results suggest that His-tagged BpGH117 can be used for producing bioactive products such as AHG and agarotriose from agarose efficiently.

Original languageEnglish
Article number271
JournalMarine drugs
Volume19
Issue number5
DOIs
Publication statusPublished - 2021 May 13

Keywords

  • 3,6-anhydro-L-galactose
  • Agarose
  • Bacteroides plebeius
  • BpGH117
  • Exo-acting 3,6-anhydro-α-(1,3)-L-galactosidase
  • Human gut bacterium
  • α-neoagarooligosaccharide hydrolase

ASJC Scopus subject areas

  • Drug Discovery

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