食品科学 ›› 2019, Vol. 40 ›› Issue (12): 55-61.doi: 10.7506/spkx1002-6630-20180510-161

• 食品化学 • 上一篇    下一篇

预热处理大豆蛋白对鲤鱼肌原纤维蛋白凝胶和流变学特性的影响

杜洪振,陈 倩,杨 振,孙钦秀,孔保华*   

  1. 东北农业大学食品学院,黑龙江 哈尔滨 150030
  • 出版日期:2019-06-25 发布日期:2019-06-28
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2016YFD0401504)

Effect of Preheated Soy Proteins on Gelling and Rheological Properties of Common Carp Myofibrillar Protein

DU Hongzhen, CHEN Qian, YANG Zhen, SUN Qinxiu, KONG Baohua*   

  1. College of Food Science, Northeast Agricultural University, Harbin 150030, China
  • Online:2019-06-25 Published:2019-06-28

摘要: 以鲤鱼肌原纤维蛋白(myofibrillar protein isolate,MPI)为研究对象,研究经过预热处理的大豆分离蛋白(soy protein isolate,SPI)对MPI凝胶和流变学特性的影响。SPI在90 ℃热处理0(天然SPI)、30 min和180 min,分别与MPI以不同的比例(0∶1、1∶1、1∶2、1∶3、1∶4)混合,所有溶液总蛋白质量浓度均为40 mg/mL。结果表明,经过预热处理的SPI与MPI混合后其凝胶硬度、弹性、白度和持水性显著高于天然SPI与MPI混合所形成的蛋白凝胶(P<0.05),且预热处理时间越长的大豆蛋白(180 min)与短时间处理(30 min)相比增加得更为明显(P<0.05)。此外,随着SPI-MPI复配1∶1~1∶4,混合蛋白凝胶硬度、弹性、白度和持水性显著增大(P<0.05)。流变学研究表明,SPI添加到MPI溶液中能增加蛋白变性温度,而经过预热处理SPI能够显著地提高储能模量(G’)。热稳定性结果表明,MPI中添加天然SPI能够显著降低Tmax3(P<0.05)而对Tmax1和Tmax2无影响(P>0.05);当SPI经过热处理后添加到MPI中能够显著降低Tmax1(P<0.05)而提高Tmax3(P<0.05)。总之,与未经预热处理的SPI相比,经过预热处理后的SPI添加到MPI中能够改善蛋白凝胶特性和流变学特性。

关键词: 大豆蛋白, 肌原纤维蛋白, 凝胶性, 流变性, 热稳定性

Abstract: The aim of this study was to investigate the impact of preheated soy protein isolate (SPI) on the gelation and rheological properties of heat-induced myofibrillar protein isolate (MPI) extracted from common carp muscle. SPI heated at 90 ℃ for 0, 30 and 180 min were incorporated into MPI (0:1, 1:1, 1:2, 1:3, and 1:4), and protein content in the mixture solutions was kept at 40 mg/mL. Results showed that the gel hardness, springiness, whiteness, and water-holding capacity of MPI with preheated SPI were significantly higher than those with native SPI (P < 0.05), and a greater increase was observed with longer (180 min) versus shorter (30 min) heating time (P < 0.05). In addition, the hardness, springiness, whiteness and water-holding capacity of the mixed protein gels increased significantly with decreasing SPI/MPI ratio from 1:1 to 1:4 (P < 0.05). The rheological properties suggested that protein denaturation temperature increased after the addition of SPI, and preheated SPI significantly increased protein storage modulus (G’). The results of thermal stability suggested that the maximum transition temperature Tmax3 was significantly reduced with the addition of native SPI to MPI (P < 0.05) while the Tmax1 and Tmax2 were not affected (P > 0.05). However, the addition of preheated SPI to MPI significantly reduced the Tmax1 and increased the Tmax3 (P < 0.05). In short, compared with native SPI, preheated SPI can improve the gelling and rheological properties of myofibrillar proteins.

Key words: soy protein isolate, myofibrillar protein isolate, gelling properties, rheological properties, thermal stability

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