Cited by 237Gut microbiota and healthClostridium difficile and Clostridium perfringens researchEnzyme Production and Characterization

Contribution of the microflora to proteolysis in the human large intestine

Macfarlane, G. T., Allison, C., Gibson, S. A. W., Cummings, J. H.·1988·Journal of Applied Bacteriology

Abstract

Protease activities in human ileal effluent were approximately 20-fold greater than in normal faeces. Comparative studies with faeces from a person who did not have a pancreas suggested that a substantial proportion of the proteolytic activity in normal faeces was of bacterial origin. Thimerosal, iodoacetate, EDTA and cysteine significantly inhibited proteolysis in faeces, but not in small intestinal contents, showing that cysteine and metalloproteases were produced by bacteria in the large gut. These results, together with results from studies using p-nitroanilide substrates, demonstrated that faecal proteolysis was both qualitatively and quantitatively different from that in the small intestine. Studies with pure cultures of proteolytic gut bacteria indicated that the cell-bound proteases of Bacteroides fragilis-type organisms were likely to contribute significantly towards proteolytic activity associated with the washed cell fraction and washed particulate fraction of faeces. Extracellular proteases were formed by Streptococcus faecalis ST6, Propionibacterium acnes P6, Clostridium perfringens C16, Cl. bifermentans C21 and Cl. sporogenes C25. Inhibition results suggested that these bacteria, and similar organisms, may be partly responsible for the extracellular proteolytic activity found in the cell-free supernatant fraction of faeces.

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Registry

Crossref · 10.1111/j.1365-2672.1988.tb02427.x

Cites

16 of 16 references verified0 citation errors · 0 not checkable

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  • Some taxa within the intestinal microbiota possess enzymatic capacity to degrade dietary protein, which could play especially important roles in protein-rich, low-fiber diets where microbial energy harvest shifts from carbohydrate to protein sources.

    “Some taxa within the intestinal microbiota possess the enzymatic capacity (i.e., proteases) to degrade dietary protein (e.g., Bacteroides, Clostridium, Fusobacterium, Streptococcus), which could play especially important roles in protein-rich, low-fiber diets, in which microbial energy harvest shifts from carbohydrate to protein sources (373, 374).”

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Authors
Macfarlane, G. T., Allison, C., Gibson, S. A. W., & Cummings, J. H.
Affiliations
Medical Research Council (GB)
Venue
Journal of Applied Bacteriology
Publisher
Wiley
Published
1988-01
Volume
64
Issue
1
Pages
37-46
ISSN
0021-8847 (ISSN-L)
OpenAlex
W2015925270
Cited by
237
References
16
Citations by year
2026: 7 · 2025: 13 · 2024: 15 · 2023: 13 · 2022: 10 · 2021: 18 · 2020: 19 · 2019: 20 · 2018: 13 · 2017: 4 · 2016: 4 · 2015: 6 · 2014: 9 · 2013: 12 · 2012: 6
FWCI
1.54
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Applied Bacteriology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gut microbiota and health
  • Health Sciences › Medicine › Infectious Diseases › Clostridium difficile and Clostridium perfringens research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
gut microbiota, bacterial proteases, extracellular protease, cysteine, metalloproteinases, Bacteroides fragilis, Enterococcus faecalis, Propionibacterium acnes, Clostridium perfringens, Clostridium bifermentans, Clostridium sporogenes, protease inhibition
MeSH terms
Aminopeptidases, Bacteria, Bacteroides, Clostridium, Feces, Humans, Ileum, Intestine, Large, Peptide Hydrolases, Propionibacterium acnes, Protease Inhibitors, Enterococcus faecalis

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