Intestinal heterophyidiasis: an emerging food-borne parasitic zoonosis in southern Philippines.

Heterophyidiasis is an infection of the small bowel by minute intestinal flukes of the genus Heterophyes or related members of the family Heterophyidae. To provide a better understanding of this rarely reported condition, this study attempted to determine the infection rate, intensity of infection as well as the clinical spectrum of heterophyid infection. A stool survey was conducted in barangay San Isidro, Monkayo, Compostela Valley. Thirty-six percent of patients with history of bowel disturbance (abdominal discomfort/pain and/or diarrhea) in the past 4 weeks were found to have heterophyidiasis. All age groups were infected, with the youngest patient being 1 year 7 months of age, while the oldest patient was 73 years of age. Prevalence was highest in the 15 to 30 years old group at 55.3%. The most common clinical manifestations of heterophyidiasis were signs and symptoms of acid peptic or peptic ulcer disease. Early diagnosis and treatment are important to ensure prompt resolution of heterophyid infection, hence, decreased morbidity and decreased chances for complications like heart or brain involvement. Proficiency of laboratory staff should be enhanced to ensure accurate diagnosis which will then make appropriate treatment possible.

Phenol degradation by Acinetobacter calcoaceticus NCIB 8250.

Acinetobacter calcoaceticus NCIB 8250 utilizes phenol as sole source of carbon and energy via an ortho-cleavage pathway. The presence of ethanol in mixed substrate cultivations repressed the utilization of phenol. In fed batch cultivation the phenol tolerance was increased at least 2-fold. Maximum degradation rates of 150 mg phenol/(1 h) and 280 mg phenol/(g h), respectively were observed. Phenol hydroxylase is induced by its substrate and in parallel the catechol-1,2-dioxygenase is detectable. The presence of active phenol hydroxylase is strongly connected with the phenol degradation. Using a spectrophotometric enzyme assay the partially purified phenol hydroxylase was characterized with respect to kinetic parameters. The apparent Km values for phenol, FAD and NADPH were estimated to be 147 microM, 35 microM and 416 microM, respectively. Both FAD and NADPH were essential for maximum activity of the cytoplasmically localized enzyme. No substrate inhibition of phenol hydroxylase by phenol was observed up to 0.8 mM. The pH and temperature optima were pH 7.8 and 33 degrees C, respectively. The partially purified enzyme showed a broad substrate specificity. It hydroxylated the three isomeric cresols, chlorophenols and methylated chlorophenols. Pyrogallol, 3,4-dihydroxy-L-phenylalanine and resorcinol were oxygenated with higher rates than phenol. With the exception of phenol all other enzyme substrates tested did not serve as growth substrates.