R. Aono et al., PURIFICATION AND CHARACTERIZATION OF CELL WALL-ASSOCIATED N-ACETYLMURAMYL-L-ALANINE AMIDASE FROM ALKALIPHILIC BACILLUS-LENTUS C-125, Bioscience, biotechnology, and biochemistry, 60(7), 1996, pp. 1140-1145
Cells of the facultative alkaliphile Bacillus sp, C-125 grown at neutr
al pH autolyze rapidly in alkaline buffers of pH 9-10, Alkaline autoly
tic activity has been found mainly in the tell wall fraction, A peptid
oglycan lytic enzyme nas extracted from the cell wall fraction suspend
ed in 4 M LiCl, Tile enzyme was identified as N-acetylmuramyl-L-alanin
e amidase, with a molecular mass of 58 kDa, At low salinity, the enzym
e formed an aggregate of high molecular mass, The peptidoglycan lytic
reaction of this enzyme happened at pH 9.0-10.5 at 37 degrees C, Optim
um pH for the reaction was 9.7-10.0, The enzyme was most active at 60
degrees C when assayed st pH 9.0.