食品科学 ›› 2018, Vol. 39 ›› Issue (5): 20-25.doi: 10.7506/spkx1002-6630-201805004

• 基础研究 • 上一篇    下一篇

转谷氨酰胺酶诱导调质大豆分离蛋白凝胶的水分分布及凝胶特性

田海娟1,2,3,胡耀辉1,3,*,于寒松1,3,王玉华1,3,朴春红1,3,刘俊梅1,3,代伟长1,3,刘景圣1,4   

  1. 1.吉林农业大学食品科学与工程学院,吉林 长春 130118;2.吉林工商学院 粮油食品深加工吉林省高校重点实验室,吉林 长春 130507;3.国家大豆产业技术体系研发中心加工实验室,吉林 长春 130118;4.小麦和玉米深加工国家工程实验室,吉林 长春 130118
  • 出版日期:2018-03-15 发布日期:2018-03-14
  • 基金资助:
    国家现代农业(大豆)产业技术体系建设专项(CARS-04)

Moisture Distribution and Texture Properties of Transglutaminase-Induced Soybean Protein Isolate Gels

TIAN Haijuan1,2,3, HU Yaohui1,3,*, YU Hansong1,3, WANG Yuhua1,3, PIAO Chunhong1,3, LIU Junmei1,3, DAI Weichang1,3, LIU Jingsheng1,4   

  1. 1. College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118; 2. Jilin Province Key Laboratory of Grain and Oil Processing, Jilin Business and Technology College, Changchun 130507, China; 3. Division of Soybean Processing, Soybean Research & Development Center, Chinese Agricultural Research System, Changchun 130118, China; 4. National Engineering Laboratory of the Wheat-Corn Deep Processing, Changchun 130118, China
  • Online:2018-03-15 Published:2018-03-14

摘要: 利用低场核磁共振技术、质构仪、差示扫描量热仪等对调质大豆分离蛋白凝胶水分分布、凝胶特性及微观 结构进行测定,研究调质大豆分离蛋白的蛋白组成对转谷氨酰胺酶诱导的蛋白凝胶的影响。结果表明:调质大豆分 离蛋白中11S球蛋白所占比例对蛋白凝胶水分分布、凝胶特性及微观结构有显著相关性。11S球蛋白的质量分数由 60%提高到80%时,蛋白凝胶的横向弛豫时间T2先缩短后延长;凝胶的硬度、黏性、咀嚼性3 项指标值均有不同程 度的降低;蛋白凝胶的热稳定性先提高后降低,70%的11S球蛋白蛋白凝胶ΔH最低,凝胶中水分不易失去;11S球 蛋白质量分数分别为60%与70%的大豆分离蛋白凝胶形成的微观结构表面较平整,孔洞较小且相对均匀。

关键词: 调质大豆分离蛋白, 低场核磁共振, 水分分布, 质构特性, 微观结构

Abstract: The water distribution, texture properties and microstructure of modified soybean protein isolate (SPI) gels induced by transglutaminase (TGase) were detected using a low-field nuclear magnetic resonance (LF-NRM) instrument, a texture profile analyzer (TPA), and a differential scanning calorimeter (DSC). The obtained results showed that increasing percentage of 11S globulin in modified SPI was significantly correlated with the moisture distribution, texture properties and microstructure of SPI gels. The transverse relaxation time (T2) decreased first and then increased with increasing the 11S globulin percentage from 60% to 80% (m/m). Besides, the viscosity, hardness and chewiness all declined. The thermal stability of SPI gels showed an initial increase followed by a decrease, and the lowest enthalpy change (ΔH) was observed with 70% 11S globulin, indicating reduced water loss. The microstructure of SPI gels with 60% and 70% 11S globulin presented a flat surface with smaller and relatively homogenous pits.

Key words: modified soybean protein isolate, low-field nuclear magnetic resonance, moisture distribution, texture profile analysis properties, microstructure

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