Enriched characteristics of poultry collagen over other sources of collagen and its extraction methods: A review.

Collagen is the most abundant protein in animals and is extensively studied for its structural and thermal stability, biocompatibility, and healing properties which enables them to be widely applied in various fields. Collagen extracted from poultry sources have shown improved structural stability and reduced risk of triggering allergic responses and transmitting animal diseases onto humans. Furthermore, poultry collagen is widely accepted by consumers of diverse beliefs in comparison to collagen extracted from bovine and porcine sources. The review aims to compare different sources of collagen, focusing on the various beneficial characteristics of poultry collagen over the other sources. Moreover, the review explains various pre-treatment and extraction methods of poultry collagen and its versatile applications in different industrial sectors.

Physicochemical and thermal properties of pepsin- and acid-soluble collagen isolated from the body wall of sea cucumbers (Stichopus hermanni).

The main objective of this work was to characterize the acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the body wall of the sea cucumber scientifically called, Stichopus hermanni. For the extraction of ASC and PSC, the pre-treated sea cucumber body walls were subjected to 0.5 M acetic acid and 5 g L-1 pepsin, respectively. The yield of ASC (7.30% ± 0.30%) was found to be lower than the PSC (23.66% ± 0.15%), despite both ASC and PSC having similar chemical compositions except for the quantity of protein. The collagens produced from ASC and PSC show maximum peaks on ultraviolet-visible spectroscopic profiles at wavelengths of 230 and 235 nm, respectively, with no significant difference in the maximum temperature (Tmax ) of the extracted ASC and PSC. The ASC's coloration was whiter than that of the PSC. As a result, the collagen obtained from the body wall of the sea cucumber showed promise for usage as a substitute for collagen derived from marine sources. PRACTICAL APPLICATION: The two most popular methods of collagen extraction were acid hydrolysis and enzymatic hydrolysis. To determine whether the extracted collagen is a suitable substitute for animal collagen in different industries, it is required to characterize its physicochemical qualities. This study discovered a new application for marine collagen in the food industry: The sea cucumber has collagen with a greater yield in pepsin extraction with good physicochemical qualities.

Marine collagen: Unveiling the blue resource-extraction techniques and multifaceted applications.

Marine organisms such as fish and shellfish are composed of compounds with properties and characteristics that have been proven useful in a variety of sectors such as cosmetics, healthcare (wound healing), food industries, and tissue engineering. Collagen extraction from fish waste as a "blue resource" has attracted research attention over the past decade. Around 75 % of fish waste contains a high concentration of collagen. This has driven research in the conversion of these low-cost by-products into valuable products. Collagen extracted by acidic or/and enzymatic methods is gaining a lot of attention today due to its low cost and high yield. Fermentation and enzymatic hydrolysis stand out as one of the most environmentally sustainable and ecologically friendly methods for collagen extraction. Because of its great biocompatibility, excellent bioactivity, and low antigenicity, marine collagen is receiving more attention. Furthermore, collagen-derived peptides may exhibit interesting antioxidant activity, potent antihypertensive activity, and antimicrobial activity against different strains of bacteria. This review focuses on the advancements in extraction and detection methods of marine collagen, both from a technological and legislative standpoint, in addition to exploring its diverse range of application domains.

Extraction of collagenolytic proteases from Aspergillus heteromorphus URM 0269 in an aqueous two-phase system for application in collagen hydrolysis.

Collagenolytic proteases produced by Aspergillus heteromorphus URM0269 were extracted using a PEG/sulfate aqueous two-phase system (ATPS). A 23 factorial design was performed to analyze the independent variables: PEG molar mass (MPEG), PEG concentration (CPEG), and sulfate concentration (Csulf). The extracted proteases were also evaluated for their optimum pH and stability at different pH levels (4.0 - 11.0) after 20 h of incubation. Collagen was extracted from mutton snapper (Lutjanus analis) skin using acetic acid (0.5 mol L-1). The enzyme was preferentially partitioned to the PEG-rich phase (K > 1), whose highest purification factor and recovery (PF = 6.256 and Y = 404.432%) were obtained under specific conditions: MPEG 8000 g.mol-1, CPEG 30%, Csulf 10%. The ATPS extraction provided an enzymatic activity range of pH 7.0 - 11.0, exhibiting greater stability compared to the crude extract. Approximately 80% of protease activity was maintained after 20 hours of incubation at all analyzed pH levels, except pH 11.0. Collagen extraction from L. analis skin yielded 8.056%, and both crude extract samples and ATPS-derived samples successfully hydrolyzed the extracted collagen, reaching peak hydrolysis after 36 hours of treatment. These findings demonstrate the feasibility of extracting highly purified and active proteases capable of hydrolyzing L. analis collagen.

Exploring dog antler chews as a novel source of collagen supplementation: extraction and characterization of collagen from red deer antlers.

Collagen is the body's most abundant protein and is primarily found in the skin, bones, tendons, and ligaments of animals and fish. As the interest in collagen supplementation grows, new sources of this protein are continually being introduced. We have confirmed that red deer antlers are a source of type I collagen. We investigated the effects of chemical treatment, temperature, and time on the extractability of collagen from red deer antlers. The optimal conditions for obtaining the highest collagen yield were determined to be: 1) removing noncollagenous proteins at 25°C for 12 h in an alkaline solution, 2) defatting at 25°C using a 1:10 grounded antler:butyl alcohol ratio, and 3) acidic extraction lasting 36 h using a 1:10 antler:acetic acid ratio. Under these conditions, we obtained a collagen yield of 22.04%. The molecular characterization of red deer antler collagen revealed typical features of type I collagens, including the presence of three α-chains, high glycine content, and high levels of proline and hydroxyproline, as well as helical arrangements. This report suggests that red deer antlers have significant potential as a source of collagen supplements.

Collagen Derived from Fish Industry Waste: Progresses and Challenges.

Fish collagen garnered significant academic and commercial focus in the last decades featuring prospective applications in a variety of health-related industries, including food, medicine, pharmaceutics, and cosmetics. Due to its distinct advantages over mammalian-based collagen, including the reduced zoonosis transmission risk, the absence of cultural-religious limitations, the cost-effectiveness of manufacturing process, and its superior bioavailability, the use of collagen derived from fish wastes (i.e., skin, scales) quickly expanded. Moreover, by-products are low cost and the need to minimize fish industry waste's environmental impact paved the way for the use of discards in the development of collagen-based products with remarkable added value. This review summarizes the recent advances in the valorization of fish industry wastes for the extraction of collagen used in several applications. Issues related to processing and characterization of collagen were presented. Moreover, an overview of the most relevant applications in food industry, nutraceutical, cosmetics, tissue engineering, and food packaging of the last three years was introduced. Lastly, the fish-collagen market and the open technological challenges to a reliable recovery and exploitation of this biopolymer were discussed.

Age-Related Properties of Aquaponics-Derived Tilapia Skin (Oreochromis niloticus): A Structural and Compositional Study.

In the last two decades, fisheries and fish industries by-products have started to be recovered for the extraction of type I collagen because of issues related to the extraction of traditional mammalian tissues. In this work, special attention has been paid to by-products from fish bred in aquaponic plants. The valorization of aquaponic fish wastes as sources of biopolymers would make the derived materials eco-friendlier and attractive in terms of profitability and cost effectiveness. Among fish species, Nile Tilapia is the second-most farmed species in the world and its skin is commonly chosen as a collagen extraction source. However, to the best of our knowledge, no studies have been carried out to investigate, in depth, the age-related differences in fish skin with the final aim of selecting the most advantageous fish size for collagen extraction. In this work, the impact of age on the structural and compositional properties of Tilapia skin was evaluated with the aim of selecting the condition that best lends itself to the extraction of type I collagen for biomedical applications, based on the known fact that the properties of the original tissue have a significant impact on those of the final product. Performed analysis showed statistically significant age-related differences. In particular, an increase in skin thickness (+110 µm) and of wavy-like collagen fiber bundle diameter (+3 µm) besides their organization variation was observed with age. Additionally, a preferred collagen molecule orientation along two specific directions was revealed, with a higher fiber orientation degree according to age. Thermal analysis registered a shift of the endothermic peak (+1.7 °C) and an increase in the enthalpy (+3.3 J/g), while mechanical properties were found to be anisotropic, with an age-dependent brittle behavior. Water (+13%) and ash (+0.6%) contents were found to be directly proportional with age, as opposed to protein (-8%) and lipid (-10%) contents. The amino acid composition revealed a decrease in the valine, leucine, isoleucine, and threonine content and an increase in proline and hydroxyproline. Lastly, fatty acids C14:0, C15:0, C16:1, C18:2n6c, C18:3n6, C18:0, C20:3n3, and C23:0 were revealed to be upregulated, while C18:1n9c was downregulated with age.

Extraction and characterization of collagen from the skin of Amazonian freshwater fish pirarucu

The need to fully exploit fishing resources due to increasing production and consequent waste generation requires research to promote the sustainability of the fishing industry. Fish waste from the industry is responsible for relevant environmental contamination. However, these raw materials contain high amounts of collagen and other biomolecules, being attractive due to their industrial and biotechnological applicability. Thus, to reduce the waste from pirarucu (Arapaima gigas) processing, this study aimed to obtain collagen from pirarucu skin tissue. The extraction process used 0.05 M sodium hydroxide, 10% butyl alcohol, and 0.5 M acetic acid, with extraction temperature of 20°C. The obtained yield was 27.8%, and through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), it was determined that the collagen obtained was type I. This study showed that collagen solubility was highest at pH 3 and the lowest solubility was at concentrations of 3% sodium chloride. The denaturation temperature of collagen was 38.1°C, and its intact molecular structure was observed using the Fourier transform infrared spectrophotometry technique with an absorption radius of 1. The results showed that it was possible to obtain collagen from pirarucu skin at 20°C, which has the typical characteristics of commercial type I collagen. In conclusion, the procedures used may be considered to be an interesting alternative for collagen extraction, a new product obtained from the processing of fish waste.

Collagen Obtained from Leather Production Waste Provides Suitable Gels for Biomedical Applications.

Collagen and its derivates are typically obtained by extracting them from fresh animal tissues. Lately, however, there has been an increased interest in obtaining collagen from other sources, such as waste material, because of the growing trend to replace synthetic materials with sustainable, natural counterparts in various industries, as well as to ensure a rational waste revalorization. In this paper, collagen was obtained from non-tanned waste of leather production, taken at different stages of the production process: limed pelt, delimed pelt, and fleshings. A stepwise extraction through acid hydrolysis in 0.5 M acetic acid and subsequent precipitation with NaCl lead to collagen-containing protein extracts. The highest collagen yield was achieved in extracts based on delimed pelt (2.3% m/m after a first extraction round, and an additional 1.4% m/m after the second round). Hyp/Hyl molar ratios of 10.91 in these extracts suggest the presence of type I collagen. Moreover, gels based on these collagen extracts promote adhesion and spreading of HEK293 cells, with cells grown on collagen from delimed pelt showing a larger nuclear and cell expansion than cells grown on traditional bovine tendon atelocollagen. This suggests that these collagen gels are promising natural biomedical carriers and could be used in a wide range of medical and cosmetic applications.

Chemical and Antioxidant Characteristics of Skin-Derived Collagen Obtained by Acid-Enzymatic Hydrolysis of Bigeye Tuna (Thunnus obesus).

The utilization of bigeye tuna skin as a source of collagen has been increasing the value of these skins. In this study, the quality of the skin was studied first. The skin after 14 h freeze-drying showed a high protein level (65.42% ± 0.06%, db), no histamine and a lack of heavy metals. The collagens were extracted through acid and acid-enzymatic methods. The enzymes used were bromelain, papain, pepsin, and trypsin. The two highest-yield collagens were pepsin-soluble collagen (PSC) and bromelain-soluble collagen (BSC). Both were type I collagen, based on SDS-PAGE and FTIR analysis. They dissolved very well in dimethyl sulfoxide and distilled water. The pH ranges were 4.60-4.70 and 4.30-4.40 for PSC and BSC, respectively. PSC and BSC were free from As, Cd, Co, Cr, Cu, and Pb. They showed antioxidant activities, as determined by the DPPH method and the reducing power method. In conclusion, bigeye tuna skin shows good potential as an alternative source of mammalian collagen. Although further work is still required, PSC and BSC showed the potential to be further used as antioxidant compounds in food applications. Other biological tests of these collagens might also lead to other health applications.

Characterization of an intracellular aspartic protease (PsAPA) from Penicillium sp. XT7 and its application in collagen extraction.

An intracellular aspartic protease, PsAPA, was identified from Penicillium sp. XT7. This protease was belonged to penicillopepsin and was expressed in Pichia pastoris GS115. The recombinant PsAPA had a specific activity of 4289.7 ± 261.7 U/mg. The pH and temperature maxima of the enzyme were 3.0 and 30 °C, respectively. The PsAPA was stable in the pH range from 3.0 to 6.0 and was completely inactivated after incubation at 50 °C for 15 min. Presence of Mn2+ and Cu2+ increased the proteolytic activity and ß-mercaptoethanol and SDS showed inhibitory effects, whereas 0.05 M pepstatin A strongly inhibited it. PsAPA could effectively hydrolyze animal proteins, including myoglobin, and hemoglobin but not collagens. PsAPA increased the yield of collagen extraction compared to the acid extraction method. The above properties show that the novel low-temperature acidic protease, PsAPA, is comparable to commercial proteases (porcine pepsin) and has great potential for collagen extraction.

Fish Collagen: Extraction, Characterization, and Applications for Biomaterials Engineering.

The utilization of marine-based collagen is growing fast due to its unique properties in comparison with mammalian-based collagen such as no risk of transmitting diseases, a lack of religious constraints, a cost-effective process, low molecular weight, biocompatibility, and its easy absorption by the human body. This article presents an overview of the recent studies from 2014 to 2020 conducted on collagen extraction from marine-based materials, in particular fish by-products. The fish collagen structure, extraction methods, characterization, and biomedical applications are presented. More specifically, acetic acid and deep eutectic solvent (DES) extraction methods for marine collagen isolation are described and compared. In addition, the effect of the extraction parameters (temperature, acid concentration, extraction time, solid-to-liquid ratio) on the yield of collagen is investigated. Moreover, biomaterials engineering and therapeutic applications of marine collagen have been summarized.

Characterization and potential strategies for the valorisation of the Southwest Atlantic butterfish (Stromateus brasiliensis).

The waste of fish resources constitutes a serious environmental problem that must be avoided. The valorisation of by-catch species and decreasing the discard rate constitute a more efficient and sustainable use of these marine biomasses. In this work, we characterize and propose different potential uses for Stromateus brasiliensis, another frequently discarded (≥ 90%) and poorly studied by-catch species captured in the South Atlantic Ocean (FAO 41) by trawler fishing fleets. Furthermore, in the case of this species, freezing and frozen storage of the whole fish is the only strategy currently employed for its exploitation. The results revealed that muscle from S. brasiliensis presented a high content of polyunsaturated fatty acids (20.34%) and that the concentrations of both total diacyl glyceryl ethers (2.41%) and heavy metals (Hg 0.038, Pb 0.006 and Cd 0.018 mg/kg) were below the established limits for safe human consumption. Likewise, the protein hydrolysates proved to be a good source of amino acids for human consumption or animal feeding. Minced muscle blocks could be made by a mechanical separation process of the flesh, and the composition of minced muscle did not differ much from that of the whole fish. Furthermore, this process allows the incorporation of cryoprotectants and antioxidants to extend the frozen shelf life of this fatty fish. An extraction process from mechanically mixed skin and bones yielded a good source of collagen that should not be neglected.