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Properties of beta-casein and edible beta-casein films.

机译:β-酪蛋白和可食用β-酪蛋白薄膜的性质。

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摘要

Physicochemical properties of β-casein interactions with water were characterized. Moisture sorption isotherms at +4°C and +22.5°C were obtained for β-casein after isolation and after 9 months of storage at –29°C and +22.5°C. Glass transition state diagrams (Tg vs. moisture) were determined for β-casein after storage. Results showed that the effects of storage temperature on moisture sorption isotherms were varied; however, at any aw differences in moisture content between samples were small. The glass transition temperatures for β-casein were above room temperature, even at aw = 0.76. Onset of stickiness occurred above aw = 0.76.; Effects of storage conditions on the secondary structure of β-casein in powders, films, and solutions were determined. Fourier transform infrared spectroscopy absorbance spectra were obtained for β-casein samples after the protein had been stored for 16 months at –29°C or +22.5°C. Correlation coefficients of second derivative absorbance spectrum in the amide I region (1720–1600 cm-1) were used to compare secondary structures of β-casein. Secondary structure did not change as a function of storage temperature but was affected by the physical state of the protein (i.e. structure of β-casein in solution was different than that of β-casein films and powders).; A method was developed to produce viable edible β-casein films on a laboratory scale. Edible films were made using glycerol and β-casein that had been stored for 16 months at –29°C and +22.5°C. Water vapor permeability at +22.5°C was determined for two relative humidity gradients (53–11% and 53–75% RH). Stress-strain curves for mechanical property evaluation were obtained by the extension-film dynamic mechanical analysis method. Protein storage temperature did not significantly affect water vapor permeability or elongation properties; however, films made from β-casein stored at –29°C had higher ultimate tensile strength, modulus of elasticity, and yield strength than films made from +22.5°C stored β-casein.; Overall this research contributed to the understanding of the stability of physicochemical and structural properties of β-casein with respect to storage temperature and provided quantitative water vapor permeability and mechanical data for β-casein edible films.
机译:表征了β-酪蛋白与水相互作用的理化性质。分离后以及在–29°C和+ 22.5°C储存9个月后,β-酪蛋白在+ 4°C和+ 22.5°C的水分吸附等温线。储存后测定β-酪蛋白的玻璃化转变状态图(T g 与水分的关系)。结果表明,贮藏温度对水分吸附等温线的影响各不相同。然而,在任何一个水分之间,样品之间的水分含量差异都很小。 β-酪蛋白的玻璃化转变温度即使在 w = 0.76时也高于室温。粘性开始发生在a w 大于0.76时。确定了储存条件对粉末,薄膜和溶液中β-酪蛋白二级结构的影响。蛋白质在–29°C或+ 22.5°C下储存16个月后,获得了β-酪蛋白样品的傅里叶变换红外光谱吸收光谱。使用酰胺I区(1720–1600 cm -1 )中二阶导数吸收光谱的相关系数来比较β-酪蛋白的二级结构。二级结构不随贮存温度而变化,而是受蛋白质物理状态的影响(即溶液中β-酪蛋白的结构不同于β-酪蛋白薄膜和粉末的结构)。开发了一种在实验室规模上生产可行的可食用β-酪蛋白薄膜的方法。使用甘油和β-酪蛋白制作了可食用的薄膜,它们在–29°C和+ 22.5°C的温度下保存了16个月。在两个相对湿度梯度(53-11%和53-75%RH)下确定了+ 22.5°C的水蒸气渗透率。通过延伸膜动态力学分析方法获得了用于力学性能评估的应力-应变曲线。蛋白质的储存温度对水蒸气的渗透性或伸长率没有明显的影响。但是,由β-酪蛋白在–29°C下储存的薄膜具有比在+ 22.5°C下由β-酪蛋白储存的薄膜更高的极限拉伸强度,弹性模量和屈服强度。总体而言,这项研究有助于了解β-酪蛋白相对于储存温度的理化和结构性质的稳定性,并为β-酪蛋白可食用膜提供了定量的水蒸气透过率和力学数据。

著录项

  • 作者

    Mauer, Lisa Jurgonski.;

  • 作者单位

    University of Minnesota.;

  • 授予单位 University of Minnesota.;
  • 学科 Agriculture Food Science and Technology.
  • 学位 Ph.D.
  • 年度 1999
  • 页码 94 p.
  • 总页数 94
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 农产品收获、加工及贮藏;
  • 关键词

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