reported that yellows tripe trevally natural actomyosin solutions became less negatively charged in the presence of ZnSO4 or ZnCl2. This behaviour could be attributed to ionic interactions between protein molecules and Zn2+ ions. The gelation of proteins is also induced by reducing the electrostatic repulsion between the aggregates by increasing the salt concentration. reported that bovine serum albumin gels added with ZnSO4 had higher clustered aggregates than the control.