The solubilisation of the membrane-bound D-alanyl-D-alanine carboxypeptidase of Bacillus coagulans NCIB 9365.
Protoplast membranes and the particulate D,D-carboxypeptidase of Bacillus coagulans NCIB 9365 were extremely resistant to disruption by either detergents or urea. A combination of urea and the non-ionic detergent Genapol X-100 was required to achieve a significant solubilisation of membrane protein and D,D-carboxypeptidase in an active form; the pH optimum for this treatment was pH 7.5. Solubilisation of the enzyme was accompanied by a two-fold enhancement of activity. Kinetic results indicated that the enhancement may be due to an alteration in the conformation of the enzyme following disruption of membrane structure.
D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D000440:Butanols; D002268:Carboxypeptidases / Q000302:isolation & purification*; D002462:Cell Membrane / Q000201:enzymology; D003902:Detergents; D006863:Hydrogen-Ion Concentration; D002267:Muramoylpentapeptide Carboxypeptidase / Q000302:isolation & purification* / Q000378:metabolism; D012995:Solubility; D013010:Sonication; D014508:Urea
D000440:Butanols; D003902:Detergents; D014508:Urea; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase