A novel mucin sulphatase from human faeces: its identification, purification and characterization

Clin Sci (Lond). 1992 Apr;82(4):447-54. doi: 10.1042/cs0820447.


1. Colonic mucus is heavily sulphated and it is likely that this contributes considerably to its resistance to degradation by bacterial enzymes. The presence of a mucin-desulphating enzyme in faeces could therefore be very important in determining the rate of degradation of secreted mucus and hence the level of protection of the mucosa. 2. A novel assay for mucin sulphatase has been developed using biologically labelled human colonic [35S]sulphomucin as a substrate and a mucin sulphatase has been purified from faeces by sequential high-performance gel filtration and ion-exchange chromatography. 3. The mucin sulphatase has been shown to have a pH optimum of 4.5 and activity over the pH range 3-7. It has a pI of 4.0 and is inhibited by inorganic sulphate and phosphate. The purified enzyme preparation gave a single band on electrophoresis with a molecular mass of 15,000 Da. It has a Km of 41.9 mmol/l and a Vmax. of 1.17 katal/kg for glucose 6-sulphate. The enzyme was also shown to enhance fivefold the deglycosylation of [3H]glucosamine-labelled mucin by a faecal mucin glycosidase preparation. 4. Two bacteroides spp. isolated from normal human faeces, Bacteroides fragilis and B. thetaiotaomicron, were found to be producers of mucin-desulphating enzymes. 5. Mucin sulphatase is likely to be critical in determining the rate of enzymic degradation of secreted colonic mucin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteroides fragilis / isolation & purification
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Feces / enzymology*
  • Feces / microbiology
  • Glycoside Hydrolases / analysis
  • Humans
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Mucins / metabolism*
  • Sulfatases / isolation & purification*


  • Mucins
  • sulfomucin
  • Sulfatases
  • mucin sulfatase
  • Glycoside Hydrolases