Effect of hydrostatic pressure on molecular conformation of tilapia (Orechromis niloticus) myosin

Abstract

Change in tilapia myosin molecular conformation due to pressurization at 50 to 200 MPa for 0 to 60 min was investigated. After a 50-MPa treatment, tilapia myosins slightly decreased their total sulfhydryl contents and exposed their hydrophobic residues. Experimental results indicated that 100- and 150-MPa treatments caused an apparent unfolding of myosins and a I-fold increase of their surface hydrophobicity (S(0)). Myosins mainly formed intermolecular disulfide bonds with pressures of 100 to 200 MPa. In addition, increasing pressures altered the myosin conformation and decreased its Ca-ATPase activity. Myosin apparently unfolded and formed disulfide bonds and hydrophobic interactions with pressurizing at 150 MPa.