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Gelling properties of vacuum-freeze dried surimi powder as influenced by heating method and microbial transglutaminase

文献类型： 外文期刊

作者： Guo, Xiujin 1 ; Shi, Liu 5 ; Xiong, Shanbai 2 ; Hu, Yang 2 ; You, Juan 2 ; Huang, Qilin 2 ; Yin, Tao 2 ;

作者机构： 1.Minist Agr & Rural Affairs, Key Lab Refrigerat & Conditioning Aquat Prod Proc, Xiamen 361026, Fujian, Peoples R China

2.Huazhong Agr Univ, Coll Food Sci & Technol, 1 Shizishan St, Wuhan 430070, Hubei, Peoples R China

3.Fujian Anjoy Food Co Ltd, Xiamen 361026, Fujian, Peoples R China

4.Natl R&D Branch Ctr Convent Freshwater Fish Proc, Wuhan 430070, Hubei, Peoples R China

5.Hubei Acad Agr Sci, Inst Agr Prod Proc & Nucl Agr Technol, Wuhan 430064, Hubei, Peoples R China

关键词： Vacuum-freeze drying; Surimi; Fish protein; Magnetic resonance imaging; Pre-mixed powder

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：4.952； 五年影响因子：5.383 ）

ISSN： 0023-6438

年卷期： 2019 年 99 卷

页码：

收录情况： SCI

摘要： Effects of heating method and addition of microbial transglutaminase (MTGase) on properties of gels made from vacuum-freeze dried silver carp surimi were investigated. After vacuum-freeze drying, surface hydrophobicity of surimi proteins obviously increased, Ca2+-ATPase activity slightly decreased, while alpha-helix percentage significantly decreased, indicating the surimi proteins were partially denaturated. Consequently, the dried surimi formed gels (D gel) with significantly lower breaking force, penetration distance and water holding capacity as compared with those of gels made from frozen surimi (F gel) under all the heating methods. With addition of MTGase, breaking force of the D gels heated at 40 degrees C/60 min and 90 degrees C/30 min was not significantly different from those of F gels, while was slightly lower under the heating of 40 degrees C/60 min + 90 degrees C/30 min. After adding MTGase, water holding capacity of the D gel under 90 degrees C heating increased significantly, while the gels under the other heating methods slightly deceased. Heating method obviously influenced color parameters of D gels while MTGase addition did not. Setting (40 degrees C) and MTGase addition induced covalent cross-linking of myosin heavy chains of D gels. MTGase addition reduced the uniformity of the water distribution in D gels.

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