期刊
JOURNAL OF FOOD SCIENCE
卷 86, 期 5, 页码 1835-1844出版社
WILEY
DOI: 10.1111/1750-3841.15687
关键词
gel properties; myofibrillar proteins; protein oxidation; sarcoplasmic proteins
资金
- National Natural Science Foundation of China [31771993]
This study found that the oxidation of SPs enhanced the cross-linking of protein components in MPs gel, significantly reduced the water holding capacity of the gel, and altered the microstructure of the gel.
This study investigated the influence of sarcoplasmic proteins (SPs) treated by the oxidation system (0.1 mmol/L FeCl3, 0.1 mmol/L ascorbic acid, and 0, 1, 5, 10 mmol/L H2O2) 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 1 mmol/L H2O2 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 (1 mmol/L H2O2) 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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