Effect of sonication on thermolysin hydrolysis of ovotransferrin

The effect of sonication on proteolytic hydrolysis of ovotransferrin and bioactivities of the hydrolysates were investigated, and the large peptide fragments left in the hydrolysate were characterised. The results showed that sonication could increase the reactive sulphydryl groups in 5% ovotransferrin solution by 50%, although there were no improvements in the overall degree of hydrolysis. Furthermore, SDS-PAGE and reverse-phase HPLC profiles did not show difference of the treated samples. Angiotensin-converting enzyme (ACE) inhibitory activity, but not antioxidant activity, of the thermolysin hydrolysate was improved in a dose dependent manner at prolonged sonication time. Matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) analysis revealed that thermolysin hydrolysate was composed of 926 peptides, of 99% having masses lower than 10. kDa and of 1% larger than 10. kDa derived from both N- and C-lobes of ovotransferrin.