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Published on: May 1, 2011
Temperature-dependent in vitro digestion properties of isoelectric solubilization/precipitation (ISP)-isolated
Xue Zhao1, Xinglian Xu1, Guanghong Zhou1
1Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Key Laboratory of Animal Products Processing, MOA, Key Lab of Meat Processing and Quality Control, MOE, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China.
Abstract:
The effects of various heating strategies (72 °C-20 min, 100 °C-60 min) on the digestibility of isoelectric solubilization/precipitation (ISP)-isolated pale, soft, exudative (PSE)-like chicken protein in an in vitro simulated gastrointestinal model were studied. Untreated PSE-like meat protein was used as the control. The hydrophobic groups were much more exposed in ISP-isolated protein than in the control protein, and the difference diminished after heating. The results of SDS-PAGE analyses and digestion kinetic parameters show the ISP isolates had higher digestibility than the control group when heated at 72 °C for 20 min (P < 0.05), but there was no significant difference between the 100 °C heated groups (P > 0.05). Additionally, all ISP-isolated groups showed higher peptide abundance than the control groups. In summary, heating at 72 °C for 20 min is beneficial to increase the digestion properties of ISP-isolated PSE-like chicken protein, but its gel properties are weaker than those of protein heated at 100 °C for 60 min.

