Isolation of an 1,3-1,4-beta-glucan degrading Enterococcus faecium strain from the intestinal tract of chicken and partial characterization of its novel 1,3-1,4-beta-glucanase.
An Enterococcus faecium strain with a novel endo 1,3-1,4-endo-beta-glucanase (lichenase, E.C. 3.2.1.73) was isolated from the intestinal tract of broiler chicken. The enzyme was secreted into the culture medium and acted exclusively on mixed linked 1,3-1,4-beta-glucans as determined with a reducing sugar assay. The purified enzyme has its isoelectric point at pI 4.8, maximum activity was determined at pH 6.5 and 40 degrees C. Thermal stability of the enzyme was low, but high pH stability and high residual activity was observed after incubation in digesta samples from the chicken intestine. Multiple lichenase activities were obtained from culture supernatants on SDS/PAGE and native zymograms, but it is concluded that the lichenase consists of one active protein at 30.5 kD and additional polypeptides of unknown function.
Beckmann
L
L
Faculty of Veterinary Medicine, Free University of Berlin, Germany.
Vahjen
W
W
Simon
O
O
D000818:Animals; D002645:Chickens / Q000382:microbiology*; D016984:Enterococcus faecium / Q000145:classification / Q000201:enzymology* / Q000302:isolation & purification; D005936:Glucans / Q000737:chemistry / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007422:Intestines / Q000382:microbiology*; D007525:Isoelectric Focusing; D013696:Temperature; D047071:beta-Glucans
D005936:Glucans; D047071:beta-Glucans; C064197:beta-1,6-glucan; C067858:beta-glucan, (1-3)(1-4)-; D006026:Glycoside Hydrolases; C028020:licheninase