Detection, prevalence, purification and characterization of lecithinase of Klebsiella pneumoniae.
Lecithinase activity in Klebsiella is a rare trait as out of 208 strains of Klebsiella belonging to 3 species, viz. K. pneumoniae (168), K. planticola (29) and K. oxytoca (11), only 4 strains of K. pneumoniae produced lecithinase positive colonies on egg-yolk-agar. Although cell lysates of 16 K. pneumoniae yielded positive results for lecithinase assay on egg-yolk-agar, 19 strains were detected positive for lecithinase with ELISA using anti-lecithinase serum. Release of up to 52.12% cell-bound lecithinase could be achieved with polymyxin-B treatment at 100 micrograms/ml concentration. Purified lecithinase was determined to be a high molecular weight (70 kDa), crystalizable, anionic (pI, 3.5) protein. It possessed cytolytic, haemolytic and dermonecrotic activities but did not induce fluid accumulation in rabbit ileal loop or infant mouse guts. It was inactivated by boiling, trypsin and chymotrypsin treatment and alkaline pH. Serologically, it was related to lecithinase of Aeromonas caviae and phospholipase-C of Salmonella.
Singh
B R
BR
Department of Veterinary Microbiology and Immunology, College of Veterinary Sciences, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar, India.
Sharma
V D
VD
Chandra
R
R
D000818:Animals; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D051379:Mice; D010740:Phospholipases / Q000302:isolation & purification* / Q000378:metabolism; D011817:Rabbits
D010740:Phospholipases