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paramyosin
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE · 2023 · IF 4.1

Interactions between paramyosin and actin greatly improve their thermostability and gel properties

Shuhua Yin,Maoping Duan,Jian Zhang,Tuo Zhang,Guanghua Zhao

BACKGROUND Myofibrillar proteins, the main contributors to the quality of meat products, are the main structural protein component of muscle and have functional properties such as the formation of a 3D protein gel network and water binding. The susceptibility of meat-derived proteins to heat-induced aggregation is the functional constraint that hinders their applications in industry, and so establishing an effective but simple method to improve their thermostability of the proteins is of great importance. RESULTS In the present study, we describe an easy approach to perform high colloidal thermostability of both paramyosin and actin by mixing them at low ionic strength. The improvement in thermal stability was found to be derived from intermolecular interactions between these two different proteins through non-covalent binding with each other. Consequently, such interactions protected each of them from thermal-induced degradation compared to individual components. Notably, this binary native protein mixture rather than single paramyosin or actin component has the ability to form protein hydrogels with a shear-thinning and reversible sol–gel transformation behavior, which is markedly different from most of reported heat-induced, denatured protein hydrogels. CONCLUSION The present study not only presents a facile and effective strategy for improvement of the thermal stability and gel properties of a binary paramyosin and actin mixture, but also enhances our understanding of how mutual interactions of protein components affect their physicochemical and functional properties. © 2023 Society of Chemical Industry.

研究领域: 食品科学 · 生物化学 · 分子生物学
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CHEMICAL ENGINEERING JOURNAL · 2023 · IF 15.1

Regulatable and reversible native paramyosin hydrogels promote the wound healing of the skin in mice

Shuhua Yin,Maoping Duan,Yiran Qian,Chenyan Lv,Jiachen Zang,Guanghua Zhao,Tuo Zhang

Protein hydrogels with multifunction including tunable mechanical property, sustained drug release and excellent biocompatibility have shown considerable promise in biological applications. However, these hydrogels are usually generated using denatured or modified protein molecules, it remains challenging to construct injectable hydrogel based on native protein as building blocks. Here, a native nanofibrous protein, paramyosin (PM) was utilized as building blocks to create hydrogels under mild conditions, taking advantage of Zn 2+ -mediated metal coordination with His-Glu motifs located on the exterior surface of the protein. The bioactive substance cyanidin-3- O -galactoside was shielded from light-induced degradation by being enclosed in the native PM hydrogels. Moreover, the rheological property and biological activity of construction PM hydrogels were improved through noncovalent interactions with natural polyphenols, such as proanthocyanidins. Importantly, all of these manufactured native hydrogels endow good biocompatibility, reversible sol–gel transforming behavior, great stability, and considerably speed up the healing of wounds in mice with skin injuries. Overall, these hydrogels derived from natural protein not only demonstrates beneficial qualities that are very effective in encouraging wound healing, but also offers a straightforward and repeatable gelation approach to produce protein hydrogel employed in biomedical applications.

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