4.7 Article

Characterization of BpGH16A of Bacteroides plebeius, a key enzyme initiating the depolymerization of agarose in the human gut

期刊

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 105, 期 2, 页码 617-625

出版社

SPRINGER
DOI: 10.1007/s00253-020-11039-3

关键词

Red seaweeds; Agarose; Agarase; Gut bacterium; Bacteroides plebeius

资金

  1. Mid-career Researcher Program - National Research Foundation of Korea (NRF) [2020R1A2B5B02002631]
  2. Ministry of Oceans and Fisheries, Korea [20200367]
  3. NRF [2020R1C1C1008048, 2020R1A6A3A01100292]
  4. Korea University
  5. National Research Foundation of Korea [2020R1C1C1008048, 2020R1A6A3A01100292, 2020R1A2B5B02002631] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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This study focuses on the application of seaweeds as sources of dietary fiber and biomass, particularly the utilization of red seaweed polysaccharides by the human gut bacterium Bacteroides plebeius. A key enzyme, BpGH16A, has been identified in B. plebeius, demonstrating the ability to depolymerize agarose and agar into smaller oligosaccharides, making it an important player in the human gut microbiome. Further research on the characteristics and functions of BpGH16A will provide insights into the depolymerization pathway of red seaweed polysaccharides in the human gut and its industrial applications.
Seaweeds have received considerable attention as sources of dietary fiber and biomass for manufacturing valuable products. The major polysaccharides of red seaweeds include agar and porphyran. In a marine environment, marine bacteria utilize agar and porphyran through the agarase and porphyranase genes encoded in their genomes. Most of these enzymes identified and characterized so far originate from marine bacteria. Recently, Bacteroides plebeius, a human gut bacterium isolated from seaweed-eating Japanese individuals, was revealed to contain a polysaccharide utilization locus (PUL) targeting the porphyran and agarose of red seaweeds. For example, B. plebeius contains an endo-type beta-agarase, BpGH16A, belonging to glycoside hydrolase family 16. BpGH16A cleaves the beta-1,4-glycosidic linkages of agarose and produces neoagarooligosccharides from agarose. Since it is crucial to study the characteristics of BpGH16A to understand the depolymerization pathway of red seaweed polysaccharides by B. plebeius in the human gut and to industrially apply the enzyme for the depolymerization of agar, we characterized BpGH16A for the first time. According to our results, BpGH16A is an extracellular endo-type beta-agarase with an optimal temperature of 40 degrees C and an optimal pH of 7.0, which correspond to the temperature and pH of the human colon. BpGH16A depolymerizes agarose into neoagarotetraose (as the main product) and neoagarobiose (as the minor product). Thus, BpGH16A is suggested to be an important enzyme that initiates the depolymerization of red seaweed agarose or agar in the human gut by B. plebeius.

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