Kang Zhuang-Li, Zhang Xue-Hua, Li Xiang, Song Zhao-Jun, Ma Han-Jun, Lu Fei, Zhu Ming-Ming, Zhao Sheng-Ming, Wang Zheng-Rong
School of Food Science, Henan Institute of Science and Technology, Xinxiang, 453003 People's Republic of China.
J Food Sci Technol. 2021 Jun;58(6):2258-2264. doi: 10.1007/s13197-020-04736-4. Epub 2020 Aug 25.
The objective of this study was to evaluate relationship with aggregation, secondary structures and gel properties of pork myofibrillar protein with different sodium chloride (1%, 2% and 3%). When the sodium chloride increased from 1 to 3%, the active sulfhydryl, surface hydrophobicity, hardness and cooking yield of myofibrillar protein were increased significantly ( < 0.05), the particle size, total sulfhydryl and Zeta potential were decreased significantly ( < 0.05), these meant the aggregations of pork myofibrillar protein were decreased. The changes of proteins aggregation induced the strongest intensity band of Amide I shifted up from 1660 cm to 1661 cm, meanwhile, the β-sheet structure content was increased significantly ( < 0.05) with the sodium chloride increased. From the above, the lower proteins aggregation and higher β-sheet structure content could improve the water holding capacity and texture of pork myofibrillar protein gel.
本研究的目的是评估不同氯化钠浓度（1%、2%和3%）下猪肉肌原纤维蛋白的聚集、二级结构和凝胶特性之间的关系。当氯化钠浓度从1%增加到3%时，肌原纤维蛋白的活性巯基、表面疏水性、硬度和蒸煮得率显著增加（<0.05），粒径、总巯基和Zeta电位显著降低（<0.05），这意味着猪肉肌原纤维蛋白的聚集减少。蛋白质聚集的变化导致酰胺I最强吸收带从1660 cm上移至1661 cm，同时，随着氯化钠浓度的增加，β-折叠结构含量显著增加（<0.05）。综上所述，较低的蛋白质聚集和较高的β-折叠结构含量可以提高猪肉肌原纤维蛋白凝胶的保水能力和质地。
