Abstract
This study investigated the influence of sarcoplasmic proteins (SPs) treated by the oxidation system (0.1mmol/L FeCl3 , 0.1mmol/L ascorbic acid, and 0, 1, 5, 10mmol/L H2 O2 ) on the properties of pork myofibrillar proteins (MPs) gel. After oxidation treatment, the SPs showed an increased in carbonyl content and a decreased in total sulfhydryl content, coupled with the cross-linking of protein components by disulfide bonds and covalent bonds. The MPs gel with SPs oxidized at 1mmol/L H2 O2 exhibited the maximal strength while the minimal water holding capacity (WHC). The WHC of MPs gel was significantly decreased with increasing SPs oxidation, leading to the increase of free water and the decrease of immobilized water in the gel system. The microstructures of MPs gels with moderately (1mmol/L H2 O2 ) oxidized SPs showed a more compact and smaller pore gel network than MPs alone, suggesting adding oxidized SPs can expel water trapped in the gel. Furthermore, the environmental polarity of aliphatic C-H groups increased with SPs oxidation.
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