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首页> 外文期刊>Biotechnology Progress >Structure and binding ability of self-assembled alpha-lactalbumin protein nanotubular gels
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Structure and binding ability of self-assembled alpha-lactalbumin protein nanotubular gels

机译：自组装α-乳白蛋白蛋白纳米凝胶的结构和结合能力

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摘要

Partial hydrolysis of whey-based alpha-lactalbumin (alpha-La) with Bacillus licheniformis protease (BLP) induces the formation of nanotubular structures in the presence of calcium ions by a self-assembly process. alpha-La nanotubes (alpha-LaNTs) exist in the form of regular hollow strands with well-defined average dimensions. The growth of nanotubes induces the formation of stiff transparent protein gels due to the well-arranged networks that the strands can form; these gels can be used for entrapment, transportation, and target delivery of bioactive agents in the industry. High purity of alpha-La (free of other whey protein fractions) is desirable for nanotube formation; however, pure proteins are very expensive and not practically obtained for industrial applications. Thus, the purpose of this research was to construct alpha-LaNTs from an alpha-La preparation with lower purity and to study the gelation phenomena triggered by the self-assembled nanotubes. Some structural features of nanotube gels and their active agent-binding abilities were also investigated. A lower amount of alpha-LaNTs was observed when low purity alpha-La was used for nanotube formation. Nanotube growth induced gel formation and higher gel stiffness was obtained when compared to alpha-La hydrolysates. alpha-La was denatured after hydrolysis and self-assembly, and remarkable changes were observed in the alpha-helix and beta-sheet domains of alpha-La structure. Increased intensity in Amide I and II regions indicated potential locations for binding of active agents to alpha-LaNTs. Whey-based alpha-La without much purification can be used to produce nanotubular gels and these gels can be considered carrying matrices for active agents in various industrial applications.
机译：用芽孢杆菌的乳清基α-乳白蛋白酶（BLP）部分水解芽孢杆菌蛋白酶（BLP）诱导通过自组装方法在钙离子存在下形成纳米管结构。 Alpha-La Nanotubes（alpha-lant）以常规空心股线的形式存在，具有明确的平均尺寸。纳米管的生长引起的透明蛋白凝胶的形成由于股线可以形成的良好的网络;这些凝胶可用于行业中的生物活性剂的夹带，运输和靶向递送。纳米管形成期望高纯度α-La（不含其他乳清蛋白级分）;然而，纯蛋白质非常昂贵，而且实际上没有用于工业应用。因此，该研究的目的是用较低纯度的α-La制剂构建α-百倍，并研究由自组装纳米管触发的凝胶化现象。还研究了纳米管凝胶的一些结构特征及其活性剂结合能力。当低纯度α-1a用于纳米管形成时，观察到较少量的α-百乙含量。与α-LA水解液相比，获得纳米管生长诱导的凝胶形成和更高的凝胶刚度。在水解和自组装后变性α-LA，在α-螺旋和α-LA结构的α-螺旋和β-板状结构域中观察到显着变化。酰胺I和II区域的强度增加，指示潜在的活性剂与α-含量结合的位置。基于乳清的α-LA没有太多纯化可用于产生纳米凝胶，并且可以认为这些凝胶可以被认为是各种工业应用中的活性剂的载体矩阵。

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