Enhancement of the gelation properties of hairtail (Trichiurus haumela) muscle protein with curdlan and transglutaminase

被引：82
|
作者：
Hu, Yaqin [1 ]
Liu, Wenjuan [1 ]
Yuan, Chunhong [2 ]
Morioka, Katsuji [3 ]
Chen, Shiguo [1 ]
Liu, Donghong [1 ]
Ye, Xingqian [1 ]
机构：
[1] Zhejiang Univ, Coll Biosyst Engn & Food Sci, Fuli Inst Food Sci, Zhejiang Key Lab Agrofood Proc,Zhejiang R&D Ctr F, Hangzhou 310058, Zhejiang, Peoples R China
[2] Kagoshima Univ, Fac Fisheries, Kagoshima 8900056, Japan
[3] Kochi Univ, Lab Aquat Prod Utilizat, Kochi 7838502, Japan
来源：
FOOD CHEMISTRY | 2015年 / 176卷
关键词：
Hairtail; Muscle protein; Curdlan; Microbial transglutaminase; Gelation properties; CHICKEN PLASMA-PROTEIN; GEL-FORMING ABILITY; MICROBIAL TRANSGLUTAMINASE; CROSS-LINKING; GELLING PROPERTIES; BIGEYE SNAPPER; HEAT-TREATMENT; SURIMI; FISH; QUALITY;
D O I：
10.1016/j.foodchem.2014.12.006
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
The effects of curdlan in combination with microbial transglutaminase on the gelling properties of hairtail muscle protein were investigated. When curdlan of 4 g/100 g paste was combined with transglutaminase at a concentration of 0.4 units/g meat paste, the gel strength, water holding capacity and the whiteness of the heated gel were improved. Textural profiles, such as hardness, springiness, cohesiveness, guminess and chewiness, reached their peaks as well. The increased band intensity of cross-linked proteins, accompanied by weakened myosin heavy chain, was observed from the SDS PAGE pattern, indicating that curdlan might activate the formation of more s-(y-glutamyl) lysine cross-links induced by transglutaminase, especially at the level of 0.4 units/g paste, leading to a denser gel matrix. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码：115 / 122
页数：8
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