Thermal denaturation of tilapia myosin and its subunits as affected by constantly increasing temperature.

Purified tilapia myosin was digested with α-chymotrypsin and purified to obtain heavy meromyosin (HMM) and light meromyosin (LMM). Biochemical properties of tilapia myosin, HMM, and LMM were characterized. Surface hydrophobicity (S(o) ) showed an increase for myosin and HMM between 30 and 40 °C and reached a plateau at 70 °C.