Prokopová, A.; Mokrejš, P.; Gál, R.; Pavlačková, J.; Hurajová, A. Characterization of Poultry Gelatins Prepared by a Biotechnological Method for Targeted Changes at the Molecular Level. Int. J. Mol. Sci.2024, 25, 916.
Prokopová, A.; Mokrejš, P.; Gál, R.; Pavlačková, J.; Hurajová, A. Characterization of Poultry Gelatins Prepared by a Biotechnological Method for Targeted Changes at the Molecular Level. Int. J. Mol. Sci. 2024, 25, 916.
Prokopová, A.; Mokrejš, P.; Gál, R.; Pavlačková, J.; Hurajová, A. Characterization of Poultry Gelatins Prepared by a Biotechnological Method for Targeted Changes at the Molecular Level. Int. J. Mol. Sci.2024, 25, 916.
Prokopová, A.; Mokrejš, P.; Gál, R.; Pavlačková, J.; Hurajová, A. Characterization of Poultry Gelatins Prepared by a Biotechnological Method for Targeted Changes at the Molecular Level. Int. J. Mol. Sci. 2024, 25, 916.
Abstract
Chicken collagen is a promising raw material source to produce gelatins and hydrolysates. Gelatins and hydrolysates can be prepared biotechnologically using proteolytic enzymes produced by submerged fermentation of genetically modified microorganisms. By choosing the appropriate process conditions, such changes can be achieved at the molecular level of collagen, making it possible to prepare products with targeted properties for advanced cosmetic, pharmaceutical, medical or food applications. The research aims to investigate: i) antioxidant activity (DPPH and ABTS) in model samples of chicken collagen products (gelatin and hydrolysates); ii) distribution of molecular weights by the GPC-RID analysis method; iii) functional groups and configuration of polypeptide chains related to molecular level properties using FTIR; iv) the microbiological properties on SDA, PCA, TSA and VRBL microbial populations using MALDI method. Antioxidant activity towards ABTS radicals of more than 80% was found for all samples. The molecular weights of all gelatin samples showed typical α- and β-chains. FTIR analysis confirmed that the samples showed all typical vibrational regions for collagen cleavage products, Amide A and B, Amide I, II, and III at characteristic values. Microbiological analysis of the prepared samples showed no undesirable bacteria that would limit advanced applications of the prepared products. Gelatins and hydrolysates from chicken stomachs represent a promising alternative to products made from standard collagen tissues of terrestrial animals.
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