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 TG_GS improved them significantly.

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.

The food packaging materials from natural polymers including polysaccharides offer an ecologically important alternative to commonly used synthetic, non-biodegradable counterparts. The purpose of this work was to modify of bacterial cellulose (BC) leading to the improvement of its functional properties in terms of use as a food packaging material. Effects of disintegration of BC and addition of montmorillonite (MMT) on its water barrier, mechanical and thermal properties were investigated. Disintegration of BC increased its water vapour permeability (WVP) and thermal stability, but decreased its tensile strength (σ). These changes were closely related to the rearrangement of hydrogen-bond network in the BC structure, resulting in a partial conversion from the I_α to I_β allomorph. The addition of 2% of MMT did not affect WVP and σ of the disintegrated BC (bBC), while the plasticization of the modified bBC generally decreased WVP, and did not increase σ. The improvement in water barrier properties of bBC modified by adding 2% of MMT in the presence of glycerol was caused by the formation of hydrogen bonds between the components of the composite. The results presented show the potential usefulness of BC modified by disintegration and adding 2% of MMT and 10–15% of glycerol as a food packaging material.

Prolyl oligopeptidase (POP) is a conserved serine protease belonging to proline-specific peptidases. It has both enzymatic and non-enzymatic activity and is involved in numerous biological processes in the human body, playing a role in e.g., cellular growth and differentiation, inflammation, as well as the development of some neurodegenerative and neuropsychiatric disorders. This article describes the physiological and pathological aspects of POP activity and the state-of-art of its peptidic inhibitors originating from food proteins, with a particular focus on their potential as cognition-enhancing agents. Although some milk, meat, fish, and plant protein-derived peptides have the potential to be applied as natural, procognitive nutraceuticals, their effectiveness requires further evaluation, especially in clinical trials. We demonstrated that the important features of the most promising POP-inhibiting peptides are very short sequence, high content of hydrophobic amino acids, and usually the presence of proline residue.

This study compared the effectiveness of urea-containing and urea-free L-cysteine solutions in extracting high-quality feather keratin and evaluated commercial proteases for producing keratin-derived bioactive peptides. The urea-assisted extraction was crucial for achieving high structural integrity and yield of soluble keratin. The keratin isolate exhibited oil-holding capacity of 9.37 g/g, foaming capacity of up to 127 %, and emulsifying capacity of up to 49 %. Its proteolysis with trypsin, chymotrypsin, pepsin and subtilisin resulted in peptides with average molecular weight between 2.10 and 5.96 kDa and degree of hydrolysis from 6 to 36 %. The subtilisin hydrolysate had the highest degree of hydrolysis, 63 % of peptides <1 kDa, and excellent solubility across a wide pH range, but negligible water and oil-binding, foaming, and emulsifying properties. This study highlights the need to optimize each step in keratin extraction and hydrolysis processes to produce high-quality bioactive keratin preparations for diverse applications, including food and pharmaceutical.