Search

Unlike spider silk, spinning silkworm silk has the added intricacy of being both fibre and micron-thick glue-like coating. Whilst the natural flow properties of the fibre feedstock fibroin are now becoming more established, our understanding of the coating sericin is extremely limited and thus presents both a gap in our knowledge and a hindrance to successful exploitation of these materials. In this study we characterise sericin feedstock from the silkworm Bombyx mori in its native state and by employing both biochemical, rheological and spectroscopic tools, define a natural gold standard. Our results demonstrate that native sericin behaves as a viscoelastic shear thinning fluid, but that it does so at a considerably lower viscosity than its partner fibroin, and that its upper critical shear rate (onset of gelation) lies above that of fibroin. Together these findings provide the first evidence that in addition to acting as a binder in the construction of the cocoon, sericin is capable of lubricating the flow of fibroin within the silk gland, which has implications for future processing, modelling and biomimetic use of these materials. Statement of Significance This study addresses one of the major gaps in our knowledge regarding natural silk spinning by providing rigorous rheological characterisation of the other major protein involved – sericin. This allows progress in silk flow modelling, biomimetic system design, and in assessing the quality of bioinspired and waste sericin materials by providing a better understanding of the native, undegraded system. [ABSTRACT FROM AUTHOR]

Natural silk spinning offers several advantages over the synthetic fiber spinning, although the underlying mechanisms of this process are yet to be fully elucidated. Silkworm silks, specifically B. mori, comprise two main proteins: fibroin, which forms the fiber, and sericin, a coextruded coating that acts as a matrix in the resulting nonwoven composite cocoon. To date, most studies have focused on fibroin's self-assembly and gelation, with the influence of sericin during spinning receiving little to no attention. This study investigates sericin's effects on the self-assembly of fibroin via their natural phase-separation. Through changes in sample opacity, FTIR, and XRD, we report that increasing sericin concentration retards the time to gelation and β-sheet formation of fibroin, causing it to adopt a Silk I conformation. Such findings have important implications for both the natural silk spinning process and any future industrial applications, suggesting that sericin may be able to induce long-range conformational and stability control in silk fibroin, while being in a separate phase, a factor that would facilitate long-term storage or silk feedstocks. [ABSTRACT FROM AUTHOR]

Understanding the interactions between fibroin and sericin is crucial in solving the mechanism of silk spinning. In this study, various commercially available dyes were used to monitor the interface between fibroin and sericin during the gelation of fibroin. The phase separation between fibroin and sericin could be observed by the addition of azo dyes over a certain molecular weight. Furthermore, the addition of the dyes to the sericin layer showed vivid phase separation over addition to the fibroin layer. [ABSTRACT FROM AUTHOR]

Abstract: In this study, silk sericin nanofibers from sericin hope-silkworm, whose cocoons consist almost exclusively of sericin were successfully prepared by electrospinning method. Scanning electron microscopy (SEM) was used to observe the morphology of the fibers. The effect of spinning conditions, including the concentration of sericin cocoon solution, acceleration voltage, spinning distance and flow rate on the fiber morphologies and the size distribution of sericin nanofibers were examined. The structure and physical properties were also observed by Fourier transform infrared (FT-IR), differential scanning calorimetry (DSC) and thermogravimetric analysis (TG). The optimum conditions for producing finely thinner fibrous sericin nanofibers without beads were the concentration of sericin solution above 6–8wt%, acceleration voltage ranging from 25 to 32kV, spinning distance above 9cm, and flow rate above 0.06cmmin−1. The mean diameter of as spun sericin fibers varied from 114 to 430nm at the different spinning conditions. In the as-spun fibers, silk sericin was present in a random coil conformation, while after methanol treatment, the molecular structure of silk sericin was transformed into a β-sheet containing structure. Sericin hope nanofiber demonstrated thermal degradation at lower temperature than the sericin hope cocoon, which probably due to the randomly coiled rich structure of the sericin hope nanofiber. [Copyright &y& Elsevier]

Abstract: Although silk sericin (SS) occupies 25% of silk protein, its importance has often been overlooked in the natural silk spinning process and in the formation of the crystalline structure of silk fibroin (SF). In this study, we elucidated the role of SS in the crystallization process of SF under shear using SF/SS blend solutions. In order to apply shear stress to the blend solution, a rotating glass rod was inserted into a glass tube filled with the solution and the shear rate was determined to be in the range of 598–724s−1. After shearing, SF aggregates were formed and the amount of the aggregates increased with shearing time. Additionally, it was observed that the aggregate formation and β-sheet transition of SF were enhanced when a proper amount of SS was in the blend solution. Consequently, the SS considerably contributes to the structural transition of SF under shear. The SS can improve the shear-induced β-sheet transition and crystallization of SF. [Copyright &y& Elsevier]