食品与发酵工业 >

2019 , Vol. 45 >Issue 9: 89 - 95

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.018733

研究报告

豌豆蛋白对牛肉盐溶蛋白共混凝胶特性的影响

  • 计红芳 ,
  • 李莎莎 ,
  • 张令文 ,
  • 王雪菲 ,
  • 陈复生 ,
  • 马汉军
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  • 1(河南科技学院 食品学院,河南 新乡,453003)
    2(河南工业大学,食品科学与工程博士后流动站,河南 郑州,450001)
博士,副教授

收稿日期: 2018-09-10

  网络出版日期: 2019-06-06

基金资助

河南省重大科技专项项目(161100110600);河南省博士后基金(2017);河南科技学院博士后基金(2017)

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Effects of pea protein on co-gel properties of salt-soluble proteins in beef

  • JI Hongfang ,
  • LI Shasha ,
  • ZHANG Lingwen ,
  • WANG Xuefei ,
  • CHEN Fusheng ,
  • MA Hanjun
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  • 1(School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003,China)
    2(Food Science and Engineering Post-doctoral Research Station, Henan University of Technology, Zhengzhou 450001,China)

Received date: 2018-09-10

  Online published: 2019-06-06

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摘要

为改善牛肉盐溶蛋白凝胶特性,提高豌豆蛋白附加值,研究了豌豆蛋白对牛肉盐溶蛋白共混凝胶色泽、保水性、蒸煮得率、质构、动态流变、微观结构、水分迁移等特性的影响。结果表明:随豌豆蛋白添加量增加,凝胶L*值先升高后下降,a*值下降,b*值上升;豌豆蛋白的添加显著提高了不易流动水T21的相对百分含量,降低了自由水T22的相对百分含量,使T21、T22向快弛豫时间方向移动,保水性与蒸煮得率进一步提升,在添加质量浓度为0.12 g/mL时,分别为88.85%、89.49%;硬度、咀嚼性持续上升;弹性与恢复性先升高后下降,添加质量浓度为0.12 g/mL时最大,分别为0.969、0.432;豌豆蛋白能提高肌球蛋白头部变性温度,由53 ℃增加到58 ℃,G′初始值和终值均随豌豆蛋白添加量增加而升高;添加量为0.12 g/mL时,凝胶网络结构最好,细致均匀、高度有序。

关键词： 豌豆蛋白; 牛肉盐溶蛋白; 凝胶特性; 低场核磁共振

本文引用格式

计红芳 , 李莎莎 , 张令文 , 王雪菲 , 陈复生 , 马汉军 . 豌豆蛋白对牛肉盐溶蛋白共混凝胶特性的影响[J]. 食品与发酵工业, 2019 , 45(9) : 89 -95 . DOI: 10.13995/j.cnki.11-1802/ts.018733

Abstract

In order to improve the gel properties of beef salt-soluble proteins and increase the extra value of pea protein (PP), effects of PP on color, water holding capacity, cooking yield, texture, dynamic rheology, microstructure, and water migration of beef salt-soluble protein gel were investigated. The results indicated that with increasing PP, the L* of the gel increased first and then decreased, a* decreased while b* increased. PP significantly enhanced the relative content of T21 while the relative content of T22 decreased, which made T21 and T22 move to the direction of fast relaxation time. Additionally, 0.12 g/mL PP improved both water holding capacity and cooking yield to 88.85% and 89.49%, respectively. Moreover, the hardness and chewiness of the gel increased, while its springiness and resilience increased first and then decreased, and 0.12 g/mL PP increased its springiness and resilience values to the highest (0.969 and 0.432, respectively). Furthermore, PP enhanced the denaturation temperature of myosin head from 53 to 58 ℃. Besides, the initial and final values of G′ increased with increasing content of PP. With 0.12 g/mL PP, the gel had the best uniform and highly ordered network structure.

Key words： pea protein; beef salt-soluble protein; gel properties; low field nuclear magnetic resonance (LF-NMR)

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