PURIFICATION AND CHARACTERIZATION OF CELL WALL-ASSOCIATED N-ACETYLMURAMYL-L-ALANINE AMIDASE FROM ALKALIPHILIC BACILLUS-LENTUS C-125

Citation
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
Citations number
23
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
ISSN journal
09168451
Volume
60
Issue
7
Year of publication
1996
Pages
1140 - 1145
Database
ISI
SICI code
0916-8451(1996)60:7<1140:PACOCW>2.0.ZU;2-F
Abstract
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.