Due to different techniques used in the actual production process, the structure and properties of soy protein isolate (SPI) were quite different, which affect the gel-like products induced by transglutaminase (TG). In order to investigate the effect of SPIs with different structures on enzyme-induced protein gels, SPIs with different degrees of denaturation by heat treatment were prepared. The protein composition, surface hydrophobicity, solubility, particle size distribution, gel strength, water holding capacity and gel morphology were studied. The results showed that heat treatment exacerbate the dissociation and aggregation of SPI subunits, resulting in enhanced surface hydrophobicity and decreased solubility of SPI. The particle size increased with the increase of temperature, but decreased when it rose to 95 ℃. The protein gel strength was lowest at 85 ℃ and highest at 95 ℃. For the gel of heat-treated protein at 95 ℃, with the increasing of protein concentration, the gel strength and the number of pores increased. The gel strength increased with the increase of TG concentration, while the water holding capacity was the lowest at TG concentration of 1.80 U/g, and the pores increased. SPI gels incubated at 50 ℃ are stronger than samples incubated at 4 ℃. The results demonstrated that a certain degree of heating denaturation of SPI (especially heat treatment at 95 ℃) is conducive to the formation of protein gels induced by TG, which provides a certain theoretical basis for industrial production.
ZHAO Jiansheng
,
MA Xiangjie
,
MENG Shaohua
,
XU Jiao
,
LI Xin
,
ZOU Shenzhong
,
JIANG Yuqin
,
YUAN Jingyao
,
ZENG Maomao
,
CHEN Jie
. Effect of heating denaturation degree on gel properties of soy protein induced by transglutaminase[J]. Food and Fermentation Industries, 2023
, 49(2)
: 99
-105
.
DOI: 10.13995/j.cnki.11-1802/ts.031543
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