Structural analysis of proteinaceous components in Byssal threads of the mussel Mytilus galloprovincialis.
The mussel byssus is a unique holdfast structure employed by marine mussels to colonize diverse substrates. The byssus consists of extracellular threads with mainly proteinaceous components. Individual threads reveal high tensile strength at their distal end and high elasticity in their proximal portion. Our studies show that proteins of the distal part are oriented along the thread axis and are well-ordered with a high beta-structural content. In contrast, proteins of the proximal part are less ordered and are not as well-oriented with primarily alpha-helical structure. The detected differences in the structural features of the proteins along a byssus thread are likely an important basis for its gradual mechanical properties.
Collagen extraction from mussel byssus: a new marine collagen source with physicochemical properties of industrial interest
Mussel byssus is a by-product of mussel production and is a potential source of collagen. The goal of this study was to extract collagen from the byssus of Chilean mussel using an enzymatic method and characterize it. A pepsin-aided extraction method was employed where first an enzymatic hydrolysis at two pepsin/substrate ratios (1:50 or 4:50) and times (4 or 24 h) was done. Extraction was conducted at 80 °C for 24 h, in a 0.5 N acetic acid solution. All samples were analyzed for collagen content, amino acid profile, turbidity, viscosity, solubility, denaturation temperature and surface tension. Hydrolysis time had significant effect on collagen content, hydroxyproline content and extraction yield. Hydrolysis with a pepsin/byssus ratio of 4:50 for 24 h gave the better extraction performance with values of 69 mg/g protein, 1.8 mg/g protein and 30%, for collagen content, hydroxyproline content and extraction yield, respectively. No differences were found for the viscosity and surface tension of collagen dispersions, suggesting that the enzymatic hydrolysis did not affect the integrity of the collagen molecule. Denaturation temperature of freeze-dried byssus collagen presented a high value (83–91 °C), making this kind of collagen a very interesting material for encapsulation of bioactive molecules and for biomedical applications.
Measuring Sheet Resistances of Dielectrics Using Co‐Planar Hydrogel Electrochemical Cells with Practical Applications to Characterize the Protective Quality of Paints on Sculptures
Electrical properties of thin dielectric films at the solid-liquid phase boundary are an important performance characteristic of many devices, coatings and sensors. In this paper, co-polymeric hydrogels of polyacrylic acid co-sulfonic acid, swollen with a salt solution to act as the solid electrolyte, were used to assess interfaces using electrochemical impedance spectroscopy (EIS) in a co-planar geometry. Silane-modified glasses were characterized by the co-planar hydrogel EIS cell and found to be distinguishable based on their surface monolayer chemistry. EIS measurements were also made on primed and painted metal substrates, using both test panels and an outdoor sculpture, Tony Smith's Stinger. The panels were then exposed to accelerated and outdoor weathering and showed degradation on the surface paint layers, which was observable electrochemically using EIS and confirmed visually by SEM. Electrochemical spectral features were compared between data from a standard paint-test cell versus this co-planar hydrogel cell; both cell types were able to measure coating capacitance, providing useful information about the condition of the bulk coating. Yet, sheet resistance (Rs) was a spectral feature seen only by the co-planar hydrogel cell. Thus, it can be concluded that the use of such co-planar hydrogel cells can provide an earlier warning sign to coating degradation and such cells provide a new type of spectral information that is not assessable by the standard geometry.