title: Chitinolytic enzymes of the rumen ciliate Eudiplodinium maggii.
abstract: The ability of rumen ciliates to digest chitin is clearly recognized. We investigated the chitinolytic system of the rumen ciliate Eudiplodinium maggii. The ciliates were grown in a selectively faunated sheep. They were isolated from the rumen and purified by sedimentation. A crude enzyme preparation was prepared following incubation of ciliates with antibiotics. This was done in order to reduce their contamination with intracellular bacteria. The activity of particular enzymes was examined by quantification of the products released from specific substrates. It was stated that the optimum conditions for the detected activities varied between 4.5 and 5.5 pH, and 45 and 55 °C. β-N-Acetylglucosaminidase was found as an enzyme of the highest activity (4.2 μmol/l released product per mg protein per h). The activities of endochitinase and exochitinase were almost two times lower than that of β-N-acetylglucosaminidase. Zymographic studies revealed the presence of two endochitinases, two exochitinases and two β-N-acetylglucosaminidases in the examined preparation.
authors.affiliation: The Kielanowski Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, Instytucka 3, 05-110, Jabłonna near Warsaw, Poland. r.miltko@ifzz.pan.pl
authors.forename: R
authors.initials: R
authors.lastname: Miltko
authors.forename: G
authors.initials: G
authors.lastname: Belzecki
authors.forename: T
authors.initials: T
authors.lastname: Michalowski
mesh_terms: D000818:Animals; D002686:Chitin / Q000378:metabolism*; D016798:Ciliophora / Q000737:chemistry / Q000201:enzymology* / Q000302:isolation & purification / Q000378:metabolism; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D015800:Protozoan Proteins / Q000737:chemistry / Q000378:metabolism*; D012417:Rumen / Q000378:metabolism / Q000382:microbiology*; D012756:Sheep
chemical_list: D015800:Protozoan Proteins; D002686:Chitin