This article compares the properties of bacterial cellulose/fish collagen composites (BC/Col) after enzymatic and chemical cross-linking. In our methodology, two transglutaminases are used for enzymatic cross-linking—one recommended for the meat and the other proposed for the fish industry—and pre-oxidated BC (oxBC) is used for chemical cross-linking. The structure of the obtained composites is characterized by scanning electron microscopy, thermogravimetric analysis, X-ray diffraction, and Fourier transform infrared spectroscopy, and their functional properties by mechanical and water barrier tests. While polymer chains in uncross-linked BC/Col are intertwined by H-bonds, new covalent bonds in enzymatically cross-linked ones are formed—resulting in increased thermal stability and crystallinity of the material. The C2–C3 bonds cleavage in D-glucose units, due to BC oxidation, cause secondary alcohol groups to vanish in favor of the carbonyl groups’ formation, thus reducing the number of H-bonded OHs. Thermal stability and crystallinity of oxBC/Col remain lower than those of BC/Col. The BC/Col formation did not affect tensile strength and water vapor permeability of BC, but enzymatic cross-linking with TGGS improved them significantly.
Feathers, burdensome waste from the poultry industry, can be a cheap source of keratin, a protein with excellent physicochemical, biological, and mechanical properties. Acid and alkaline hydrolyses are usually adopted for isolation of keratin from its natural resources. This study aimed at assessing the statistically significant effect of input variables in the alkaline hydrolysis of keratin from chicken feathers on the process yield and on the molecular weight of peptides obtained. The effect of the volume ratio of 1M NaOH to the feathers’ mass, the hydrolysis time, and the shaking speed of the reaction mixture on the process yield were analyzed. The use of statistical analysis at the design step of experiment allowed reducing the trial number from 27 to 9. Among the input variables analyzed, only the volume ratio of 1M NaOH to the feathers’ mass had a significant effect on the process yield, while none of them significantly affected the molecular weight of the peptides obtained. All hydrolysates were dominated by two peptides’ fractions, with molecular weights of ca. 130 and 250 kDa, and mixture of many peptides of weight close to 10 kDa and smaller. Alkaline hydrolysis of feather keratin yielded protein hydrolysates soluble over a wide pH range.
Plant oils contain a high content of unsaturated fatty acids. Studies of food products have revealed a considerable disproportion in the ratio of ω6 to ω3. This article presents information on the healthful qualities of eight new oil blends that contain a beneficial proportion of ω6 to ω3 fatty acids (5:1), as well as their degradation during heating at 170 and 200 °C. The fatty acid profile was analyzed by gas chromatography (GC), content of polar compounds and polymers of triacylglycerols by liquid chromatography (LC), water content was measured by the Karl Fischer method, and oxidative stability was measured by differential scanning calorimetry (DSC) and low-field nuclear magnetic resonance (LF NMR) methods. The results showed that during heating, the polar fraction content increased in samples heated at both analyzed temperatures compared to unheated oils. This was mainly due to the polymerization of triacylglycerols forming dimers. In some samples that were heated, particularly those heated to 200 °C, trimers were detected, however, even with the changes that were observed, the polar fraction content of the blends did not go beyond the limit. Despite the high content of unsaturated fatty acids, the analyzed blends of oils are characterized by high oxidative stability, confirmed by thermoanalytical and nuclear magnetic resonance methods. The high nutritional value as well as the oxidative stability of the developed oil blends allow them to be used in the production of food, in particular products that ensure an adequate supply of ω3 fatty acids.
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