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Aqueous fiber spinning from a renewable protein waste material

机译：来自可再生蛋白质废料的含水纤维

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Crystallin proteins from animal eye lenses represent a renewable, environmentally responsible biopolymer source for bio-derived fibers. The crystallin protein family is a diverse and highly conserved set of proteins that form the macromolecular structure of the lenses of many vertebrates. Despite variability in lens anatomy across organisms, these proteins are consistently organized in a supramolecular structure that is optically clear, preserving the ability of the lens to refract light. Due to their natural functions, these proteins possess a range of interesting features which make them attractive for the production of new biomaterials such as self-assembly and the formation of stable, well ordered structures. These structures include soluble protein, nanofibrils, and amorphous aggregates, each derived from native conformations. Here, we describe the aqueous processing and spinning of crystallin proteins generated from a waste material, namely fish eye lens, into durable fibers. Crystallin protein was isolated from North Atlantic Haddock (Melanogrammus aeglefinus) eye lenses through a simple homogenization technique. Intact lenses were extracted and gently stirred at room temperature in an aqueous homogenization buffer designed to minimize protein aggregation and stabilize intermediate assembly states. After 24 hrs, the fish lens homogenate (FLH) is clarified by centrifugation and collected as an opaque suspension in which crystallin protein is present in both amorphous and structured forms. The FLH is comprised of a series of related structural proteins, which are used for subsequent investigations without further purification.
机译：来自动物眼镜的晶体素蛋白代表了生物衍生纤维的可再生环境负责的生物聚合物来源。结晶蛋白家族是一种多样化且高度保守的蛋白质，形成许多脊椎动物镜片的大分子结构。尽管椎间晶状体解剖结构具有可变性，但这些蛋白质在光学透明的超分子结构中始终如一地组织，保持晶状体折射光的能力。由于它们的自然功能，这些蛋白质具有一系列有趣的特征，使它们使它们具有诸如自组装等新生物材料的生产具有吸引力和稳定，有序的结构的形成。这些结构包括可溶性蛋白质，纳米纤维和无定形聚集体，各自衍生自定形构象。在这里，我们描述了从废料，即鱼眼镜镜片中产生的晶体蛋白质的水性加工和纺丝成耐用的纤维。通过简单的均化技术从北大西洋海豚（Melanographmus Aeglefinus）眼镜中分离出晶蛋白。萃取完整的透镜并在室温下在室温下在均质化缓冲液中轻轻搅拌，设计成最大限度地减少蛋白质聚集并稳定中间组装状态。在24小时后，通过离心澄清鱼透镜匀浆（FLH），并作为不透明悬浮液收集，其中结晶蛋白在无定形和结构形式中存在。 FLH由一系列相关的结构蛋白组成，其用于随后的研究而无需进一步纯化。

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