Characterization of Poultry Gelatins Prepared by a Biotechnological Method for Targeted Changes at the Molecular Level.

Chicken collagen is a promising raw material source for the production gelatins and hydrolysates. These can be prepared biotechnologically using proteolytic enzymes. By choosing the appropriate process conditions, such changes can be achieved at the molecular level of collagen, making it possible to prepare gelatins with targeted properties for advanced cosmetic, pharmaceutical, medical, or food applications. The present research aims to investigate model samples of chicken gelatins, focusing on: (i) antioxidant activity using 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2-azinobis-3-etylbenzotiazolin-6-sulfonic acid (ABTS); (ii) the distribution of molecular weights via gel permeation chromatography with refractometric detection (GPC-RID); (iii) functional groups and the configuration of polypeptide chains related to molecular-level properties using Fourier transform infrared spectroscopy (FTIR); (iv) the microbiological populations on sabouraud dextrose agar (SDA), plate count agar (PCA), tryptic soy agar (TSA), and violet red bile lactose (VRBL) using the matrix-assisted laser desorption ionization (MALDI) method. Antioxidant activity towards ABTS radicals was more than 80%; activity towards DPPH radicals was more than 69%. The molecular weights of all gelatin samples showed typical α-, ß-, and γ-chains. FTIR analysis confirmed that chicken gelatins all contain typical vibrational regions for collagen cleavage products, Amides A and B, and Amides I, II, and III, at characteristic wavenumbers. A microbiological analysis of the prepared samples showed no undesirable bacteria that would limit advanced applications of the prepared products. Chicken gelatins represent a promising alternative to products made from standard collagen tissues of terrestrial animals.

Antilisterial and Antimicrobial Effect of Salvia officinalis Essential Oil in Beef Sous-Vide Meat during Storage.

If food is contaminated with pathogens such as Listeria monocytogenes, improper cooking during sous-vide preparation can lead to foodborne illnesses. In this study, it was found that L. monocytogenes were inactivated with both heat and the essential oil of Salvia officinalis (sage EO) in beef tenderloin of the musculus psoas major that had undergone sous-vide processing. To determine whether the enhancement of the efficacy of heat treatment is prospective, L. monocytogenes and sage EO were mixed. Groups with L. monocytogenes alone and sage essential oil combined with L. monocytogenes and test groups without EO were established. The samples were vacuum-packed, inoculated with L. monocytogenes, and then cooked sous-vide for the predetermined duration at 50, 55, 60, or 65 °C. In both groups with sous-vide beef tenderloin, the total bacterial count, the coliforms bacterial count, and the amount of L. monocytogenes were assessed on days 0, 3, 6, 9, and 12. Over these days, the amounts of L. monocytogenes, coliform bacteria, and overall bacteria increased. The identification of bacterial strains in various days and categories was performed by MALDI-TOF mass spectrometry. The test group that was exposed to a temperature of 50 °C for 5 min had a higher overall bacterial count for each day that was assessed. Pseudomonas fragi and L. monocytogenes were the most isolated organisms from the test group and the treated group. To ensure the safety for the consumption of sous-vide beef tenderloin, it was found that the addition of natural antimicrobials could produce effective outcomes.

Preparation of Gelatin from Broiler Chicken Stomach Collagen.

With the increasing consumption of poultry meat around the world, the use of chicken stomachs as a source of collagen is being offered. The objective of this study was to extract gelatin from the stomachs of broiler chickens and to estimate their gel strength, ash content, viscosity, gelling point, melting point, clarity and digestibility. An innovative biotechnological method based on the conditioning of collagen with a microbial endoproteinase (Protamex®) and hot-water extraction was used to control the chemical and thermal denaturation process of collagen to prepare gelatin. The experiments were planned using a Taguchi design, 2 factors at 3 levels; factor A for the amount of proteolytic enzyme (0.10, 0.15 and 0.20%) and factor B for the extraction temperature (55.0, 62.5 and 70.0 °C). Data were statistically processed and analyzed at a significance level of 95%. The gelatin yield averaged 65 ± 8%; the gel strength ranged from 25 ± 1 to 439 ± 6 Bloom, the viscosity from 1.0 ± 0.4 to 3.40 ± 0.03 mPa·s, gelling point from 14.0 ± 2.0 to 22.0 ± 2.0 °C, melting point from 28.0 ± 1.0 to 37.0 ± 1.0 °C. The digestibility of gelatin was 100.0% in all samples; the ash content was very low (0.44 ± 0.02-0.81 ± 0.02%). The optimal conditions for the enzymatic treatment of collagen from chicken stomachs were achieved at a higher temperature (70.0 °C) and a lower amount of enzyme (0.10-0.15%). Conditioning chicken collagen with a microbial endoproteinase is an economically and environmentally friendly processing method, an alternative to the usual acid- or alkaline-based treatment that is used industrially. The extracted products can be used for food and pharmaceutical applications.

Collagen Hydrolysate Prepared from Chicken By-Product as a Functional Polymer in Cosmetic Formulation.

Chicken stomachs can be processed into collagen hydrolysate usable in cosmetic products. The aim of the study was to verify the effects of a carbopol gel formulation enriched with 1.0% (w/w) chicken hydrolysate on the properties of the skin in the periorbital area after regular application twice a day for eight weeks in volunteers ageed 50 ± 9 years. Skin hydration, transepidermal water loss (TEWL), skin elasticity and skin relief were evaluated. Overall, skin hydration increased by 11.82% and 9.45%, TEWL decreased by 25.70% and 17.80% (always reported for the right and left area). Generally, there was an increase in skin elasticity, a decrease in skin roughness, as the resonance times decreased by 85%. The average reduction of wrinkles was 35.40% on the right and 41.20% on the left. For all results, it can be seen that the longer the cosmetic gel formulation is applied, the better the results. Due to the positive effect on the quality and functionality of the skin, it is possible to apply the cosmetic gel formulation in the periorbital area. The advantage of the product with chicken collagen hydrolysate is also the biocompatibility with the skin and the biodegradability of the formulation.