Thermal stability and molecular microstructure of heat-induced cereal grains, revealed with Raman molecular microspectroscopy and differential scanning calorimetry.

The objectives of the present study were to use Raman molecular microspectroscopy and differential scanning calorimetry (DSC) to reveal molecular thermal stability and thermal degradation behavior of heat-induced cereal grains and reveal the molecular chemistry of the protein structures of cereal grain tissues affected by heat processing and to quantify the protein secondary structures using multicomponent peak modeling Gaussian and Lorentzian methods. Hierarchical cluster analysis (CLA) and principal components analysis (PCA) were also conducted to identify molecular differences in the Raman spectra. Three cereal grain seeds, wheat, triticale, and corn, were used as the model for feed protein in the experiment. The specimens were autoclaved (moist heating) and dry-heated (roasted) at 121 °C for 80 min, respectively. Raman spectroscopy results revealed that there are marked differences in the secondary structures of the proteins subjected to various heating treatments of different cereals. The sensitivity of cereals to moist heating was much higher than the sensitivity to dry heating. The multivariate analyses (CLA and PCA) showed that heat treatment was significantly isolated between the different Raman raw spectra. The DSC study revealed that the thermal degradation behavior of cereals was significantly changed after moist- and dry-heat treatments. The position of the major endothermic peak of dry-heated cereals shifted toward a higher temperature, from 131.7 to 134.0 °C, suggesting the high thermal stability of dry-heated cereals. In contrast, the endothermic peak position was slightly decreased to 132.1 °C in the case of moist autoclaved heating. The digestive behavior and nutritive value of rumen-undegradable protein in animals may be related to the changes of the protein secondary molecular structure and thermal stability of the cereal grain materials, which is attributed by Raman microspectroscopy and DSC endotherm profiles.

Fabrication of silk sericin nanofibers from a silk sericin-hope cocoon with electrospinning method.

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 6-8 wt%, acceleration voltage ranging from 25 to 32 kV, spinning distance above 9 cm, and flow rate above 0.06 cm min(-1). The mean diameter of as spun sericin fibers varied from 114 to 430 nm 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 ß-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.

Physical properties and structure of aquatic silk fiber from Stenopsyche marmorata.

To study the properties and structure of aquatic silk, nest-spinning hydropsychid caddisfly (Stenopsyche marmorata) larva were collected from a Japanese river and the silk glands were removed from the larva by dissecting and dried on the glass plate at room temperature. The silk fibers were obtained by removing fibrous materials, which the aquatic insects spun at the bottom of glass container and the microstructure and physical properties of aquatic silk protein fibres and their solid silk protein gland were evaluated. Silk fiber produced by the caddisfly larvae is composed of two filament embedded in a layer of glue. The results of Fourier transform infrared spectroscopy and X-ray diffraction measurements suggested the existence of binary structure containing random coil conformation and additional minor beta-molecular structure. Differential scanning calorimetry results are characterized by two broad endothermic transitions, at 230 degrees C and 320 degrees C, which corresponds to the decomposition of silk glue and silk fiber from caddis fly, respectively. The storage modulus (E') remained almost unchanged and nearly constant at above 60 degrees C until about 214 degrees C, where it began to show a sharp drop. A prominent relaxation peak appeared in the imaginary part of the modulus (loss peak at 230 degrees C), in response to the strong motional transitions exhibited by the silk fiber at this temperature. There was significant difference of tensile strength of single solid silk protein gland in dry and wet state. The results obtained are quite promising as a basis for possible future biotechnological and adhesive applications of aquatic silk.

Structural characteristics and properties of Bombyx mori silk fiber obtained by different artificial forcibly silking speeds.

To study the spinning condition of natural biopolymer silk, the silk fibers were directly acquired from Bombyx mori silkworm, N140 x C140 by a simple artificial forcibly silking method at the speed of 60, 120, 180 and 240 cm min(-1), respectively and its microstructure and physical properties were evaluated. The fine silk fibers (about 8 microm) were obtained at faster spinning speed, 240 cm min(-1). The tensile properties of silk fibers were remarkably increased with raising the forcibly spinning speeds. The beta-sheet structure contents of silk fibers obtained at higher speed were considerably increased. The fibers obtained by different spinning speeds exhibited a fairly similar X-ray crystallinity, while the degree of molecular orientation increased with decreasing the fiber diameter. The fine silk fibers obtained at higher speed (240 cm min(-1)) exhibited a slightly higher thermal stability, as shown by the upward shift of differential scanning calorimetry (DSC) decomposition temperature.