The enzymatic activity responsible for crystalline cellulose degradation (Avicelase activity) by a mesophilic clostridium (strain C7) was present in culture supernatant fluid but was not detected in significant amounts in association with whole cells or in disrupted cells. Cells of the mesophilic clostridium lacked cellosone clusters on their surface and did not adhere to cellulose fibers. The extracellular cellulase system of the mesophilic clostridium was fractionated by Sephacryl S-300 gel filtration, and the fractions were assayed for Avicelase and carboxymethylcellulase activities. The Avicelase activity coincided with an
A comparative evaluation of various biomaterials for their resistance to bacterial colonization and encrustation in infected urine is an important area in urological biomaterials research. This article describes an in vitro dynamic perfusion system that allows four reactors containing 24 1-in. catheter samples (6 per reactor) to be simultaneously perfused at a constant flow rate by synthetic urine. A common urease-producing urinary pathogen, Proteus mirabilis, was maintained at a level of 10(6) colony-forming units/mL for 7 days in the dynamic perfusion reactors. The pH and bacterial population were monitored every 24 h and the percentage of encrustation on latex and hydrogel-coated commercial catheter materials gave reproducible results in three different runs, 15.2 +/- 3.65% and 13.8 +/- 2.58%, respectively. A major issue of inlet clogging due to ascending bacteria or ammonia has been rectified using a dismountable inlet assembly. An incubator coupled with a cooling system allowed accurate temperature maintenance of 37 degrees C in all four reactors. Results from scanning electron microscopy of some latex samples are also presented.
Prevotella loescheii PK1295 produces at least 3 proteases that are separable by isoelectric focusing. One of these proteases, an enzyme with an isoelectric point at 8.5 and an M(r) of 36,000, hydrolyzes the fimbria-associated adhesin on P. loescheii responsible for coaggregation with Streptococcus oralis 34, as well as gelatin, casein and fibrin. The action of this protease may contribute to the detachment of P. loescheii from its streptococcal coaggregation partner and provide a mechanism for bacterial relocation in dental plaque.
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