为阐明超高压对藏羊肉肌原纤维蛋白特性的改善作用,该研究以欧拉藏羊肉肌原纤维蛋白为研究对象,对其进行不同压力强度(0、150、250、350、450、550 MPa,保压10 min)处理后,测定肌原纤维蛋白的乳化性、起泡性、溶解度、浊度、巯基和羰基含量,并对其进行分析。结果表明,肌原纤维蛋白的总巯基含量随着压力强度增加而显著降低(P<0.05),而羰基和活性巯基含量显著上升(P<0.05),在压力强度为550 MPa时,肌原纤维蛋白的总巯基含量比对照组低30.3%,羰基和活性巯基含量分别比对照组高54.8%、56.7%。处理后肌原纤维蛋白的乳化性、乳化稳定性、溶解度、起泡性、起泡稳定性及表面疏水性呈先上升后下降的趋势,压力强度为350 MPa时,乳化性、溶解度、起泡稳定性、表面疏水性分别比对照组高56.6%、54.8%、26.7%、39.8%。此外,处理后肌原纤维蛋白的浊度呈先下降后保持稳定,在450 MPa时,比对照组低20%。超高压处理改善了藏羊肉肌原纤维蛋白的乳化特性、溶解度、起泡特性、表面疏水性、羰基、巯基和浊度。
This paper aims to clarify the effect of ultra-high pressure on the properties of myofibrillar proteins from Tibetan sheep meat. Myofibrillar proteins of Oula Tibetan sheep meat was treated at 0, 150, 250, 350, 450, and 550 MPa for 10 min, respectively. The emulsibility, foamability, solubility, turbidity, sulfhydryl, and carbonyl content of myofibrillar proteins were determined to investigate the influences of ultra-high pressure on its properties. Results showed that with the increase in pressure intensity, myofibrillar proteins significantly reduced (P<0.05) in the total sulfhydryl content and increased (P<0.05) the carbonyl and active sulfhydryl content. Under the pressure of 550 MPa, the total sulfhydryl content of the treatment group decreased 30.3% than control group, and the contents of carbonyl and active sulfhydryl were 54.8% and 56.7% higher, respectively. The emulsibility, emulsifying stability, solubility, foamability, foaming stability, and surface hydrophobicity of myofibrillar proteins first increased and then declined with the enlargement of pressure. When the pressure strength was 350 MPa, the emulsification, solubility, foaming stability, and surface hydrophobicity were 56.6%, 54.8%, 26.7%, and 39.8% higher than those of the control group, respectively. Furthermore, the turbidity of myofibrillar proteins first decreased and then remained constantly with the increase of pressure, and was 20% lower than the control group at 450 MPa. Ultra-high pressure improved the emulsifying properties, solubility, foaming properties, surface hydrophobicity, carbonyl groups, sulfhydryl groups, and turbidity of myofibrillar proteins from Oula Tibetan sheep meat.
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