Inhibition by chelating agents of the formation of active extracellular proteinase by XXXX 32A.

@entity11763 @entity36248 @entity6546 @entity3281 @entity1391 @entity2975 @entity141 @entity3151 @entity1098
The effect of chelating agents on extracellular proteinase production by @entity11763 32A was examined. Increasing concentrations of @entity6546 slightly stimulated growth while inhibiting proteinase synthesis. Fifty per cent inhibition was found at 35 and 28 mM- @entity6546 at 5 and 20 degrees C respectively. Extracellular protein concentration was reduced by 30% when cells were grown with 100 mM- @entity6546 . @entity2975 gel electrophoresis of the cell-free supernatants suggested that reduced enzyme synthesis had taken place as evidenced by the decrease in staining intensity of the protein band corresponding to the proteinase. Other @entity1391 compounds could replace @entity6546 as an inhibitor. Extent of inhibition was related to chain length; @entity36248 with 4-6 or 13-18 @entity3151 atoms were the most effective inhibitors. @entity1098 (0.5 mM) completely inhibited proteinase synthesis. This inhibition could be partly reversed by @entity141 and, to a lesser extent, @entity3281 . Proteinase production at 5 degrees C in skim milk was completely inhibited by @entity1391 glass (P13-P18). Control experiments showed that loss of activity with chelators was not due to inhibition of preformed enzyme. The results suggest a possible role for @entity36248 in controlling proteinase production in stored milk.
