Chitinolytic activities inTrichomonas vaginalis

Abstract

Summary :Chitinolytic activities were identified in the Protozoa Trichomonas vaginalis. Overall chitinase activity assessed using chitine-azure as substrate was 10.93 ± 1.21 nmoles/min/mg prot. End nonreducing chitobiosidase (exochitinase) and chitotriosidase (endochitinase) activities were shown using p-nitrophenyl-substrates and had specific activities of 4.55 ± 0.53 and 0.47 ± 0.06 nmol/min/mg prot, K m app.= 1.32 mM and 5 μM and pH optimum = 7.0 and 6.1 respectively. ß-N-acetylhexosaminidase (NAHase) activity was also detected with a specific activity of 5.40 ± 0.65 nmol/min/mg prot., K m app = 0.656 mM and pH optimum at 7.0. No release ol these enzymes into the culture medium was found. The possible role of chitinases in T. vaginalis remains to be investigated.

A novel serum chitinase that is expressed in bovine liver

“…Overall chitinase activity was determined using chitin azure as a substrate, suspended in McIlvaine buffer (100 mM citric acid, 200 mM sodium phosphate) at the indicated pH, as previously reported [5].…”