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

doi:10.3390/md19050271

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

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

7 Citations (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. K_m and V_max values for NAB were 30.22 mM and 54.84 U/mg, respectively, and k_cat /K_m 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 language	English
Article number	271
Journal	Marine drugs
Volume	19
Issue number	5
DOIs	https://doi.org/10.3390/md19050271
Publication status	Published - 2021 May 13

Bibliographical note

Funding Information:
This work was supported by the Mid-career Researcher Program (2020R1A2B5B02002631) through the National Research Foundation of Korea (NRF), the Ministry of Oceans and Fisheries of Korea (20200367), and by the Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry, and Fisheries, funded by the Ministry of Agriculture, Food, and Rural Affairs (321036051SB010). D.H.K. acknowledges the grant support from the NRF (2020R1C1C1008196). This work was performed at the Institute of Biomedical and Food Safety at the CJ Food Safety Hall, Korea University.

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.

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

Pharmaceutical Science
Drug Discovery
Pharmacology, Toxicology and Pharmaceutics (miscellaneous)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.3390/md19050271

Cite this

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title = "Characterization of neoagarooligosaccharide hydrolase BpGH117 from a human gut bacterium bacteroides plebeius",

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.",

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",

author = "Yerin Jin and Sora Yu and Kim, {Dong Hyun} and Yun, {Eun Ju} and Kim, {Kyoung Heon}",

note = "Funding Information: This work was supported by the Mid-career Researcher Program (2020R1A2B5B02002631) through the National Research Foundation of Korea (NRF), the Ministry of Oceans and Fisheries of Korea (20200367), and by the Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry, and Fisheries, funded by the Ministry of Agriculture, Food, and Rural Affairs (321036051SB010). D.H.K. acknowledges the grant support from the NRF (2020R1C1C1008196). This work was performed at the Institute of Biomedical and Food Safety at the CJ Food Safety Hall, Korea University. Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2021",

month = may,

day = "13",

doi = "10.3390/md19050271",

language = "English",

volume = "19",

journal = "Marine drugs",

issn = "1660-3397",

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T1 - Characterization of neoagarooligosaccharide hydrolase BpGH117 from a human gut bacterium bacteroides plebeius

AU - Jin, Yerin

AU - Yu, Sora

AU - Kim, Dong Hyun

AU - Yun, Eun Ju

AU - Kim, Kyoung Heon

N1 - Funding Information: This work was supported by the Mid-career Researcher Program (2020R1A2B5B02002631) through the National Research Foundation of Korea (NRF), the Ministry of Oceans and Fisheries of Korea (20200367), and by the Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry, and Fisheries, funded by the Ministry of Agriculture, Food, and Rural Affairs (321036051SB010). D.H.K. acknowledges the grant support from the NRF (2020R1C1C1008196). This work was performed at the Institute of Biomedical and Food Safety at the CJ Food Safety Hall, Korea University. Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2021/5/13

Y1 - 2021/5/13

N2 - 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.

AB - 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.

KW - 3,6-anhydro-L-galactose

KW - Agarose

KW - Bacteroides plebeius

KW - BpGH117

KW - Exo-acting 3,6-anhydro-α-(1,3)-L-galactosidase

KW - Human gut bacterium

KW - α-neoagarooligosaccharide hydrolase

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DO - 10.3390/md19050271

M3 - Article

C2 - 34068166

AN - SCOPUS:85107410487

SN - 1660-3397

VL - 19

JO - Marine drugs

JF - Marine drugs

IS - 5

M1 - 271

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

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