食品科学 ›› 0, Vol. ›› Issue (): 0-0.

• 食品化学 •    下一篇

L-组氨酸修饰乳清蛋白结构及其热诱导凝胶特性

王耀松1,马天怡1,胡荣蓉2,张唯唯1,应瑞峰1,黄梅桂1,唐长波2   

  1. 1. 南京林业大学
    2. 南京农业大学
  • 收稿日期:2020-01-28 修回日期:2021-01-15 出版日期:2021-03-25 发布日期:2021-03-22
  • 通讯作者: 唐长波 E-mail:tangcb@njau.edu.cn
  • 基金资助:
    国家自然科学基金青年基金项目;国家自然科学基金青年基金项目;江苏省优势学科建设项目青年创新基金

L-Histidine Modifies the Structure thereof and Heat-induced Gel Properties of Whey Protein

2, 2, 2,Mei-gui Huang   

  • Received:2020-01-28 Revised:2021-01-15 Online:2021-03-25 Published:2021-03-22

摘要: 采用L-组氨酸(L-Histidine,L-His)作为蛋白凝胶功能性的增强剂,将其加入乳清分离蛋白溶液中制备热诱导凝胶,研究L-His对乳清蛋白结构及其凝胶特性的影响。结果表明:在乳清蛋白等电点(pI 5.2)时蛋白形成尺度约1 700 nm、具有极小比表面积且几乎不带电的蛋白聚集体,远离蛋白等电点时则所形成的聚集体大小约为400 nm;L-His抑制蛋白聚集体的形成而降低其粒径大小、显著提高聚集体比表面积,促进蛋白分子结构展开并提高其带电量。在经历热诱导后,乳清蛋白除在其等电点时形成持水性差的白色凝胶,而在其他pH值时则形成持水性高的黄色凝胶且越远离等电点,胶体黄度值越大;L-His的加入对凝胶颜色变化无显著影响,但能够显著提高凝胶的持水性(P<0.05);有效提高凝胶的质地特性,特别是在pH 7.59和pH 9.74时显著提高乳清蛋白凝胶的弹性及咀嚼性(P<0.05)。这些质构变化可能主要归结于L-His改变了凝胶内的氢键、二硫键和疏水作用力的重排。总之,L-His修饰乳清蛋白结构而改变其凝胶性能且同时受到pH值的影响。

关键词: 乳清蛋白, pH, L-组氨酸, 结构, 凝胶性能

Abstract: L-Histidine (L-his) used as a functional enhancer of protein gels, was added to whey protein isolate in aqueous solutions to prepare heat-induced gels. The effect of L-his on the structure thereof and gel properties of whey protein were investigated. The results show that the protein aggregates with a size of ~1700 nm and a smaller specific surface area were formed at the isoelectric point (pI 5.2) of whey protein. However, the aggregate size was ~400 nm when pH was diverted from the pI. L-His inhibits whey protein aggregating, suppresses aggregate size but dramatically increases its specific surface area, and also promotes the unfolding of whey protein single molecules when the pH of samples beyond pI. Whey protein formed a heat-induced white gel at the pI with a low water holding capacity (WHC), whereas the gels formed at other pHs were yellow and the tendency towards yellowness was increased as pH far away from the pI, and the WHC was also significantly improved (P<0.05). L-His effectively enhanced the textural properties of gels. Typically, the elasticity and chewiness of the gel that formed at pH 7.59 and pH 9.74 were significantly improved (P<0.05). These changes of gel functional properties could be mainly ascribed to L-His impelling the rearrangement of hydrogen bonds, disulfide bridges and hydrophobic interactions involved the gel matrix. Overall, L-His changes the structure of whey protein and improves the gel properties but also was affected by pH.

Key words: whey proteins, pH, L-histidine, structure, gel properties

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