Effect of the interaction between myofibrillar protein and heat-induced soy protein isolates on gel properties

被引:68
作者
Wang, Zhongjiang [1 ]
Liang, Jing [1 ]
Jiang, Lianzhou [1 ]
Li, Yang [1 ]
Wang, Jing [1 ]
Zhang, Hui [2 ]
Li, Dan [1 ]
Han, Feifei [1 ]
Li, Qiuhui [1 ]
Wang, Rui [1 ]
Qi, Baokun [1 ]
Sui, Xiaonan [1 ]
机构
[1] Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China
[2] Rural Technol Dev Ctr, Beijing 100045, Peoples R China
关键词
myofibrillar; soy protein; interaction; heat treatment; gel properties; miofibrilar; proteina de soja; interaccion; tratamiento de calor; propiedades del gel; IONIC-STRENGTH; MICROBIAL TRANSGLUTAMINASE; INDUCED GELATION; MYOSIN; PH; AGGREGATION; FISH; FUNCTIONALITY; DENATURATION; GLYCININ;
D O I
10.1080/19476337.2015.1011240
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The effect of the interaction between myofibrillar protein (MP) and heat-induced soy protein isolates (SPI) on gel properties was examined. To enhance the interaction between MP and SPI, SPI was subjected to thermal treatments at 60, 80, and 95 degrees C. The results showed that hydrophobic interactions played the most important role in MP-heated SPI (HSPI) gels. Hydrogen bonds played an important role in stabilizing the mixed gels, but this decreased with increasing heat treatment temperature of SPI. Disulfide bonds were not a significant force stabilizing the mixed gels. The gel properties of HSPI-MP were enhanced significantly (P<0.05) by the inclusion of preheated SPI (95 degrees C, 30min), including hardness, springiness, and water-holding capacity (WHC). Dynamic rheological analysis showed that heat treatment decreased the onset temperature of mixed gels and significantly increased the final G'. Notable cross-linked strands formed in MP-HSPI (80 degrees C) and MP-HSPI (95 degrees C) gels, while the smoothest and most ordered gel network structure was observed in the MP-HSPI (95 degrees C) gel. Se ha examinado el efecto de la interaccion entre la proteina miofibrilar y aislados proteicos de soja inducidos con calor en las propiedades del gel. Para mejorar la interaccion entre MP y SPI, SPI estuvo sujeto a tratamiento termico a 60, 80 y 95 oC. Los resultados mostraron que la interaccion hidrofobica jugo el papel mas importante en el gel MP-soja climatizada aislado de proteina (HSPI). Los enlaces de hidrogeno jugaron un papel importante estabilizando la mezcla de geles, aunque disminuyeron con la temperatura del tratamiento de calor de SPI. Los enlaces de disulfuro no fueron una fuerza significativa a la hora de estabilizar la mezcla de geles. Las propiedades del gel de HSPI-MP fueron mejoradas significativamente (P<0,05), incluida la dureza, la ligereza y WHC mediante la inclusion de SPI precalentado (95 oC, 30 min). El analisis reologico dinamico mostro que el tratamiento de calor redujo las temperaturas de inicio de la mezcla de gel y aumento significativamente la G' final. Se formaron areas de enlaces entrecruzados notables en geles MP-HSPI (80 oC) y MP-HSPI (95 oC), mientras que una estructura mas ordenada y lisa de gel se observo en el gel MP-HSPI (95 oC).
引用
收藏
页码:527 / 534
页数:8
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