Hydrolysis of oxidized phosphatidylcholines by crude enzymes from chicken, pork and beef muscles.

Crude enzymes were extracted from beef, pork and chicken and were employed to hydrolyze 1-palmitoyl-2-linoleoyl-phosphatidylcholine (PLPC) and oxidized PLPC, i.e. hydroperoxide of PLPC (PLPC-OOH) and hydroxide of PLPC (PLPC-OH). HPLC-ELSD and ESI-MS were used to characterize and determinate hydrolytic products. After hydrolysis at 37 °C for 180 min, 26.8 ~ 27.4%, 21.6 ~ 22.8% and 17.8 ~ 19.0% of substrates were hydrolyzed by crude enzymes from beef, pork and chicken, respectively. Phospholipase A2 (PLA2) was the major contributor to hydrolysis, which accounted for 47.8 ~ 49.6%, 45.8 ~ 48.7% and 46.6 ~ 46.8% of hydrolysis of PLPC, PLPC-OOH and PLPC-OH, respectively. Crude enzymes demonstrated almost same specificities towards PLPC, PLPC-OOH and PLPC-OH. Under actions of crude enzymes, hydroperoxyoctadecadienoic acids (HpODE) and hydroxyoctadecadienoic acids (HODE) were yielded as hydrolytic products of PLPC-OOH and PLPC-OH, respectively. These finding would be helpful to better understand the fate of hydroperoxides of phospholipids and formation of HODE during meat products manufacturing.