H. Abriouel et al., Influence of physico-chemical factors on the oligomerization and biological activity of bacteriocin AS-48, CURR MICROB, 42(2), 2001, pp. 89-95
Bacteriocin AS-48 forms a mixture of monomers and oligomers in aqueous solu
tions. Such oligomers can be clearly differentiated by SDS-PAGE after forma
ldehyde crosslinking, and we have verified that these associates are stable
to acid treatment after fixation. In addition, they show antimicrobial act
ivity and are recognized by anti-AS-48 antibodies. AS-48 oligomers can be d
issociated by the detergents SDS and Triton X-100. The degree of oligomeriz
ation of AS-48 depends on the pH of the solution and the protein concentrat
ion. At pH below 5, AS-48 is in the monomeric state at protein concentratio
ns below 0.55.mg ml(-1), but it also forms dimers above this protein concen
tration. This bacteriocin forms oligomers at pH values above 5, in agreemen
t with the observation that it is also more hydrophobic at neutral pH. AS-4
8 is stable to mild heat treatments irrespectively of pH. At 120 degreesC i
t is more heat resistant under acidic conditions, but it inactivates at neu
tral pH. Activity of AS-48 against E. faecalis is highest at neutral pH, bu
t it is highest at pH 4 for E. coli. The influence of pH on bacteriocin act
ivity could be owing to changes in the conformation/oligomerization of the
bacteriocin peptide as well as to changes in the surface charge of the targ
et bacteria.