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Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating

机译:肌原纤维蛋白的凝胶化和流变特性受添加大豆蛋白分离物的影响,所述大豆蛋白分离物经过酸性pH处理并温和加热

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摘要

Soy protein isolates prepared by a highly acidic treatment (pH 1.5) combined with a mild heat (60 degrees C) treatment (AH-SPI) were incorporated into myofibrillar protein (MP, 40 mg/mL in 0.6 M NaCl at pH 6.25 degrees C) to investigate their potential as meat processing ingredients. Compared to native soybean protein isolates (N-SPI), the addition of AH-SPI significantly increased the gel penetration force, storage modulus values (G'), and loss modulus values (G") of MP upon heating (P < 0.05). This effect was predominantly attributable to the stronger interaction between AH-SPI and muscle proteins through hydrophobic association, hydrogen bonding and disulphide linkages. The SDS-PAGE pattern of the expressed liquid from the mixed MP gels indicated that the AH-SPI easily interacted with muscle proteins. Moreover, the AH-SPI clearly improved the water holding capacity (WHC) of the MP gels (P < 0.05), and low-field nuclear magnetic resonance (LF-NMR) confirmed that the incorporated AH-SPI restricted the mobility of the aqueous phase prior to the gelation of MP. Analysis by scanning electron microscopy (SEM) revealed that the incorporation of AH-SPI facilitates the formation of an MP gel with a more continuous and homogeneous gel network structure. Overall, an acidic pH combined with a mild heat treatment could offer great potential for the development of soy protein with enhanced functionality suitable for comminuted meat products. (C) 2017 Elsevier Ltd. All rights reserved.
机译:将通过强酸处理(pH 1.5)和中度加热(60摄氏度)处理(AH-SPI)制备的大豆分离蛋白掺入肌原纤维蛋白(MP,40 mg / mL,在0.6 M NaCl中,pH 6.25摄氏度) )以研究其作为肉类加工成分的潜力。与天然大豆分离蛋白(N-SPI)相比,AH-SPI的添加显着增加了加热后MP的凝胶渗透力,储能模量值(G')和损失模量值(G“)(P <0.05)这种作用主要归因于AH-SPI与肌肉蛋白之间通过疏水缔合,氢键和二硫键之间更强的相互作用,混合MP凝胶中所表达液体的SDS-PAGE图谱表明AH-SPI容易与此外,AH-SPI明显改善了MP凝胶的持水量(WHC)(P <0.05),低场核磁共振(LF-NMR)证实掺入的AH-SPI限制了迁移率通过扫描电子显微镜(SEM)分析发现,AH-SPI的掺入有助于形成具有更连续和均质凝胶网络结构的MP凝胶。 pH值与温和的热处理相结合可以为大豆蛋白的开发提供巨大的潜力,其具有增强的功能,适用于肉糜产品。 (C)2017 Elsevier Ltd.保留所有权利。

著录项

  • 来源
    《Food Hydrocolloids》 |2017年第9期|269-276|共8页
  • 作者单位

    Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China;

    Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China;

    Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China;

    Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China|Synerget Innovat Ctr Food Safety & Nutr, Wuxi, Peoples R China;

    Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China|Synerget Innovat Ctr Food Safety & Nutr, Wuxi, Peoples R China;

  • 收录信息 美国《科学引文索引》(SCI);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    Myofibrillar protein; Soy protein isolate; Gelation; Rheological properties; Microstructure;

    机译:肌原纤维蛋白;大豆分离蛋白;膨胀;流变学性质;显微结构;

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