Natural and synthetic protein filaments in foodstuffs: Similarity and difference.

Over the past few decades, 1D self-assembly of proteins into various filaments has received considerable attention. Protein filaments ubiquitously exist in nature, which not only govern the cellar metabolism in vivo but also tune the physiochemical properties of foodstuffs in vitro. Myofibrillar proteins and collagens are natural filaments abundantly occurring in muscles, with a precise associating and dissociating mechanism. Sharing similar morphologies, a great number of globular proteins, sourced from versatile foodstuffs, can likewise be converted into filaments upon different treatments, albeit their structure remains enigmatic. This review summarized both natural and synthetic protein filaments by characterizing their distinct structures, assembly behaviors, methodologies, and promising applications. Finally, current challenges and future strategies in this research field are discussed. The goal of this review is to highlight the essence of different protein filaments constructed by natural and denatured building blocks, which may support valuable insights into food science and broader applications. [Display omitted] • Protein filaments are ubiquitously existed in foodstuffs. • Myofibrillar proteins and collagens have specific assembly mechanism. • Natural and synthesized protein filaments have been compared. • A few factors affect the process of protein fibrilization. [ABSTRACT FROM AUTHOR]