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TEXTURE AND MICROSTRUCTURE OF HEAT-FORMED EGG WHITE, EGG YOLK, AND WHOLE EGG GELS (WATER-BINDING).

机译:热成型蛋白,蛋黄和全蛋凝胶的质地和微观结构(水结合)。

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摘要

The texture and microstructure of egg white, egg yolk, and whole egg gels were investigated by gel compression and scanning electron microscopy. Samples were treated by varying pH from 5 to 9, protein content from 9 to 13%, NaCl concentration from 0 to 1.00 M, temperature from 75 to 90(DEGREES)C, and heating time from 10 to 50 minutes. Gel strength generally increased with increasing pH, protein, temperature, and time of heating for all gels. Salt reduced the firmness of egg white gels, increased the firmness of egg yolk gels substantially, and caused slight increases in whole egg gel hardness. Gels from blends of white and yolk were 20 to 140% firmer than corresponding egg white or egg yolk gels due to product interaction.Freezing of gels caused structural artifacts due to ice crystal formation. Damage was most severe in egg white gels, slightly less severe in whole egg gels, and only slight in egg yolk gels. Gels were acceptably prepared for scanning electron microscopy by fixation in glutaraldehyde, post-fixation in O(,S)O(,4), hardening in uranyl acetate, dehydration in ethanol, and critical point drying.Egg white gel structure was affected by pH, heating time and temperature, salt, and yolk. Gels at pH 9 were uniform with small pores. Severe aggregation occurred at pH 5 and 6. Aggregation was enhanced by salt and reduced by 10% or more yolk in egg white. As time and temperature of heating were increased, egg white gels were more completely crosslinked. The microstructure of hard-cooked egg yolk was grainy and crumbly, while that of stirred egg yolk gels was smooth and continuous. Whole egg gels had a uniform structure which was only slightly affected by changing pH or adding salt.Water-binding ability was determined by expressing serum from frozen-thawed gels. Serum proteins were separated and identified by polyacrylamide gel electrophoresis. As gel hardness increased the amount of serum generally decreased. The best water-binding ability occurred for gels at pH 9, 13% protein, 80 to 85(DEGREES)C, and 30 minutes of heating. Salt caused slight reductions in serum of egg white and egg yolk gels, but it more effectively lowered serum in whole egg gels. Egg white, egg yolk and whole egg gels averaged 58, 7, and 27% expressed serum, respectively.
机译:通过凝胶压缩和扫描电子显微镜研究蛋清,蛋黄和全蛋凝胶的质地和微结构。通过改变pH值从5到9,蛋白质含量从9到13%,NaCl浓度从0到1.00 M,温度从75到90(摄氏度)和加热时间从10到50分钟进行处理。对于所有凝胶,凝胶强度通常随pH,蛋白质,温度和加热时间的增加而增加。盐会降低蛋清凝胶的硬度,显着增加蛋黄凝胶的硬度,并导致整个蛋凝胶硬度略有增加。由于产品之间的相互作用,白色和蛋黄混合物的凝胶比相应的蛋清或蛋黄凝胶坚固20%至140%。凝胶的冻结由于形成冰晶而导致结构伪影。损害在蛋清凝胶中最为严重,在全蛋凝胶中危害较小,而在蛋黄凝胶中仅轻微。制备可接受的凝胶以用于扫描电子显微镜检查,方法是将戊二醛固定在O(,S)O(,4)中,后固定在乙酸铀酰中硬化,在乙醇中脱水以及临界点干燥。鸡蛋白凝胶结构受pH值的影响,加热时间和温度,盐和蛋黄。 pH为9的凝胶是均匀的,有小孔。在pH 5和6时发生严重的聚集。在蛋清中,聚集会因盐而增加,卵黄减少10%或更多。随着加热时间和温度的增加,蛋清凝胶更完全交联。煮熟的蛋黄的微观结构呈颗粒状和脆性,而搅拌的蛋黄凝胶的微观结构则光滑且连续。全蛋凝胶具有均匀的结构,仅受pH值变化或添加盐的影响很小。通过从冻融的凝胶中表达血清来确定水结合能力。分离血清蛋白并通过聚丙烯酰胺凝胶电泳鉴定。随着凝胶硬度的增加,血清的量通常会减少。凝胶的最佳水结合能力出现在pH 9,蛋白质13%,80至85(DEGREES)C和加热30分钟的情况下。盐会使蛋清和蛋黄凝胶的血清稍微减少,但可以更有效地降低全蛋凝胶的血清。蛋清,蛋黄和全蛋凝胶分别平均表达了58%,7%和27%的血清。

著录项

  • 作者

    WOODWARD, SCOTT ALAN.;

  • 作者单位

    University of Missouri - Columbia.;

  • 授予单位 University of Missouri - Columbia.;
  • 学科 Agriculture Food Science and Technology.
  • 学位 Ph.D.
  • 年度 1984
  • 页码 228 p.
  • 总页数 228
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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