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Mechanism of heat-induced gelation for ovalbuminunder acidic conditions and the effect of peptides
Polymer Journal ( IF 2.8 ) Pub Date : 2020-07-07 , DOI: 10.1038/s41428-020-0382-1
Takashi Hiroi , Kazu Hirosawa , Yuya Okazumi , Sai Venkatesh Pingali , Mitsuhiro Shibayama

The mechanism of the heat-induced gelation of ovalbumin (OVA) under acidic conditions and the effect of amphiphilic peptide additives on gelation were investigated using dynamic light scattering (DLS) and small-angle neutron scattering (SANS). This combination of techniques provides structural details spanning a wide range of length scales, from micrometer (DLS) to nanometer (SANS). The molecular morphology and structure probed by SANS suggest that the heat-induced gelation of OVA solution forms a phase-separated structure. The addition of an amphiphilic peptide to the system drastically changed the aggregated structure by promoting the formation of OVA clusters. Furthermore, heating of the solution of OVA and the peptide resulted in effective distribution of the peptide in the matrix of the heat-induced OVA gels and endowed the gel with increased strength. This simplistic approach to increase the gel strength can be applied to any protein/peptide gel system to impart the gel system with specific physical properties required by their intended application. The mechanism of the heat-induced gelation of ovalbumin (OVA) under acidic conditions and the effect of amphiphilic peptide additives on gelation were investigated using dynamic light scattering (DLS) and small-angle neutron scattering (SANS). The molecular morphology and structure probed by DLS and SANS suggest that the heat-induced gelation of OVA solution forms a phase-separated structure. Heating of the solution of OVA and the peptide resulted in effective distribution of the peptide in the matrix of the heat-induced OVA gels and endowed the gel with increased strength.

中文翻译:

酸性条件下卵清蛋白热诱导凝胶化的机理及肽的作用

使用动态光散射 (DLS) 和小角中子散射 (SANS) 研究了酸性条件下卵清蛋白 (OVA) 的热诱导凝胶化机制和两亲性肽添加剂对凝胶化的影响。这种技术组合提供了跨越从微米 (DLS) 到纳米 (SANS) 的各种长度尺度的结构细节。SANS 探测的分子形态和结构表明 OVA 溶液的热诱导凝胶形成相分离结构。通过促进 OVA 簇的形成,向系统中添加两亲性肽极大地改变了聚集结构。此外,OVA 和肽的溶液的加热导致肽在热诱导的 OVA 凝胶的基质中的有效分布并使凝胶具有增加的强度。这种增加凝胶强度的简单方法可以应用于任何蛋白质/肽凝胶系统,以赋予凝胶系统其预期应用所需的特定物理特性。使用动态光散射 (DLS) 和小角中子散射 (SANS) 研究了酸性条件下卵清蛋白 (OVA) 的热诱导凝胶化机制和两亲性肽添加剂对凝胶化的影响。DLS 和 SANS 探测的分子形态和结构表明 OVA 溶液的热诱导凝胶形成相分离结构。
更新日期:2020-07-07
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