Alternative Source Of Collagen Research Articles

Effect of different acids during collagen extraction the bone and fins from purple-spotted bigeye (Priacanthus tayenus Richardson, 1846) and their physicochemical properties

This study was carried out to determine the effectiveness of different acids (acetic, lactic and citric)-on the extraction of collagen from the bone and fins of purple-spotted bigeye (Priacanthus tayenus Richardson, 1846) particularly on the yield and physicochemical properties. The physicochemical properties were characterized by electrophoretic pattern, X-ray diffraction, FT-IR, colour and pH. The citric acid-extracted collagen (CAC) has a higher percentage of yield (1.93±0.57), followed by lactic acid-extracted collagen (LAC) (1.43±0.42) and acetic acid-extracted collagen (AAC) (0.83±0.18) although those collagens did not differ significantly (p>0.05), and those acid solubilized collagens (ASC) contained about 96.82 - 96.89 mg/g of hydroxyproline. The ASCs obtained showed similar electrophoretic patterns due to the presence of identical α chains (α1 and α2) and classified as type I collagen. UV absorption spectrum in all ASCs was approximately around 231.0 - 231.5 nm. For diffraction angle analysis, first diffraction was detected at 7.23 - 7.41° and second diffraction was at 19.41 - 20.29° in all ASCs. Major absorption peaks of FT-IR spectrum, viz. amide A, amide B and amide I-III were present in the collagens with different wavenumbers. The results indicated that the physicochemical properties of ASCs extracted in the present study were comparable with collagens reported from other fish species. The findings suggested that ASCs from purple-spotted bigeye bones and fins could serve as alternative source of collagen in functional food, pharmaceutics and tissue engineering production, particularly found in acetic acidextracted collagen because of its properties.

The Characterization and Cytotoxic Evaluation of Chondrosia reniformis Collagen Isolated from Different Body Parts (Ectosome and Choanosome) Envisaging the Development of Biomaterials.

Chondrosia reniformis is a collagen-rich marine sponge that is considered a sustainable and viable option for producing an alternative to mammalian-origin collagens. However, there is a lack of knowledge regarding the properties of collagen isolated from different sponge parts, namely the outer region, or cortex, (ectosome) and the inner region (choanosome), and how it affects the development of biomaterials. In this study, a brief histological analysis focusing on C. reniformis collagen spatial distribution and a comprehensive comparative analysis between collagen isolated from ectosome and choanosome are presented. The isolated collagen characterization was based on isolation yield, Fourier-transformed infrared spectroscopy (FTIR), circular dichroism (CD), SDS-PAGE, dot blot, and amino acid composition, as well as their cytocompatibility envisaging the development of future biomedical applications. An isolation yield of approximately 20% was similar for both sponge parts, as well as the FTIR, CD, and SDS-PAGE profiles, which demonstrated that both isolated collagens presented a high purity degree and preserved their triple helix and fibrillar conformation. Ectosome collagen had a higher OHpro content and possessed collagen type I and IV, while the choanosome was predominately constituted by collagen type IV. In vitro cytotoxicity assays using the L929 fibroblast cell line displayed a significant cytotoxic effect of choanosome collagen at 2 mg/mL, while ectosome collagen enhanced cell metabolism and proliferation, thus indicating the latter as being more suitable for the development of biomaterials. This research represents a unique comparative study of C. reniformis body parts, serving as a support for further establishing this marine sponge as a promising alternative collagen source for the future development of biomedical applications.

Assessment of Tilapia Skin Collagen for Biomedical Research Applications in Comparison with Mammalian Collagen.

Collagen is an important material for biomedical research, but using mammalian tissue-derived collagen carries the risk of zoonotic disease transmission. Marine organisms, such as farmed tilapia, have emerged as a safe alternative source of collagen for biomedical research. However, the tilapia collagen products for biomedical research are rare, and their biological functions remain largely unexamined. In this study, we characterized a commercial tilapia skin collagen using SDS-PAGE and fibril formation assays and evaluated its effects on skin fibroblast adhesion, proliferation, and migration, comparing it with commercial collagen from rat tails, porcine skin, and bovine skin. The results showed that tilapia skin collagen is a type I collagen, similar to rat tail collagen, and has a faster fibril formation rate and better-promoting effects on cell migration than porcine and bovine skin collagen. We also confirmed its application in a 3D culture for kidney cells' spherical cyst formation, fibroblast-induced gel contraction, and tumor spheroid interfacial invasion. Furthermore, we demonstrated that the freeze-dried tilapia skin collagen scaffold improved wound closure in a mouse excisional wound model, similar to commercial porcine or bovine collagen wound dressings. In conclusion, tilapia skin collagen is an ideal biomaterial for biomedical research.

Amine-reactive crosslinking enhances type 0 collagen hydrogel properties for regenerative medicine.

Collagen is extensively utilised in regenerative medicine due to its highly desirable properties. However, collagen is typically derived from mammalian sources, which poses several limitations, including high cost, potential risk of immunogenicity and transmission of infectious diseases, and ethical and religious constraints. Jellyfish-sourced type 0 collagen represents a safer and more environmentally sustainable alternative collagen source. Thus, we investigated the potential of jellyfish collagen-based hydrogels, obtained from Rhizostoma pulmo (R. pulmo) jellyfish, to be utilised in regenerative medicine. A variety of R. pulmo collagen hydrogels (RpCol hydrogels) were formed by adding a range of chemical crosslinking agents and their physicochemical and biological properties were characterised to assess their suitability for regenerative medicine applications. The characteristic chemical composition of RpCol was confirmed by Fourier-transform infrared spectroscopy (FTIR), and the degradation kinetics, morphological, and rheological properties of RpCol hydrogels were shown to be adaptable through the addition of specific chemical crosslinking agents. The endotoxin levels of RpCol were below the Food and Drug Administration (FDA) limit for medical devices, thus allowing the potential use of RpCol in vivo. 8-arm polyethylene glycol succinimidyl carboxyl methyl ester (PEG-SCM)-crosslinked RpCol hydrogels preserved the viability and induced a significant increase in the metabolic activity of immortalised human mesenchymal stem/stromal cells (TERT-hMSCs), therefore demonstrating their potential to be utilised in a wide range of regenerative medicine applications.

Türkiye Kıyılarında Dağılım Gösteren İstilacı Denizkestanesinden (Diadema setosum L., 1778) Kolajen Ekstraksiyonu ve Karakterizasyonu

In the present study, collagen was obtained from tissues of the invasive sea urchin (Diadema setosum) rapidly spread in the Mediterranean Sea. As a result, the yield of collagen isolated from sea urchin was determined to be 23.78±1.33% (dry weight). As a result of SDS-Page analysis, it was determined that it contains (α1)2α2, (Molecular Weight (MA) 124, 114 kDa) and ß chains (MA 245 kDa) similar to calfskin collagen. In the amino acid analysis of collagen, it was determined that the imino acid (proline+hydroxyproline) content was 196.1 residues/1000 residues. The functional bands of amide A (3301 cm-1), B (2924 cm-1), I (1643 cm-1), II (1550 cm-1), and III (1242 cm-1) functional bands were visualized in the FTIR spectrum. These results were like other collagen sources. Invasive sea urchin was used as a source of collagen for the first time in the present study. An alternative source of collagen to mammalian collagen, which is used commercially in many industries such as biomedicine, food and cosmetics, was isolated for the first time from D. setosum. It was proposed that marine collagen can be used as an alternative source of collagen and a functional component in areas including food, cosmetics, and pharmaceutical industries.

Effectiveness of Collagen Extracted From the Skin of Nile Tilapia Fish (Oreochromis niloticus) to Accelerate Wound Healing in vivo: A Narrative Review

Developing wound dressings with good properties to accelerate wound healing has always been challenging. Mammal collagen is well known as the desired choice among naturally produced dressings despite experiencing major drawbacks. Therefore, researchers have explored the by products of Oreochromis niloticus fish or red Nile tilapia, such as the scales and skin as alternative source of collagen. This narrative review analyzes the effectiveness of collagen extracted from Oreochromis niloticus skin and its beneficial properties to accelerate wound healing in vivo. Recent studies were compiled to provide a compact review on the effectiveness of the collagen in hastening wound healing process. Faster wound closure with upregulation of multiple growth factors, and high hydroxyproline content are some of the findings. The collagen extract could also promote the formation of epidermal layers, fibroblasts proliferation, and dermal reconstitution. Thus, Oreochromis niloticus skin collagen extract has the potential to be developed as an effective wound dressing.

Recombinant collagen-like protein: ethical policy and consumers’ likelihood to consume

Purpose This study aims to investigate the tendency that Malaysian consumers will choose the recombinant collagen-like protein (RCLP) from bacteria as an alternative source of collagen in their consumption and the determinants of the consumer acceptance. Design/methodology/approach Quantitative approach is adopted in the study. Descriptive analysis and logistic regression are used to analyze primary data collected from a survey. Findings The likelihood of consumers choosing RCLP as an alternative source of collagen is higher among elderly and females. The choice is significantly influenced by the idea that the collagen should support maqasid al-syariah, approved by national Islamic body, should clear on the ingredients used and could boost local economic activities in the future. Research limitations/implications An ethical halal policy should be outlined as the guiding principles to the potential producers of RCLP. Originality/value An alternative source of collagen using bacteria as proposed is not yet being introduced in Malaysian industry, and the analysis on probability that consumers will accept this new sourced collagen product is using primary data from survey.

Effect of Ultrasonic Amplitude on the Yield and Properties of Barramundi (Lates calcarifer) Skin Collagen

Barramundi skin, a by-product of the fish processing industry, has shown potential as an alternative collagen source. However, the commonly used acid extraction method to produce collagen rendered a low yield requires a lengthy time and is not environmentally friendly. As a result, the adoption of greener technology, such as ultrasound, to improve the conventional extraction process is emerging. This study aimed to investigate the effect of different ultrasonication amplitudes on collagen recovery from barramundi skin. The resulting collagens were evaluated for their protein, hydroxyproline and moisture content, colour, molecular weight distribution, and FTIR spectra. Ultrasound-assisted extraction (UAE) was performed at 40 (UAE40), 60 (UAE60) and 80 (UAE80) % amplitude for 20 min. For comparison, acetic acid extraction was also carried out to produce acid-soluble collagen (ASC). UAE increased the yield (p<0.05) of collagen from barramundi skin, with UAE80 exhibiting a 7-fold increment compared to ASC. Increasing the ultrasonic amplitude increased the yield considerably but decreased the hydroxyproline content, indicating a reduction in collagen quality. Furthermore, the protein content and SDS-PAGE profile of the extracted collagens revealed that UAE promoted protein degradation. FTIR spectra indicated that despite slightly varying wavenumbers, no detrimental effect on the triple helical structure was seen following UAE with the presence of amides A, B, I, II, and III. Also, the α1, α2 and ß-chains were found in all samples, although the band intensity reduced as the amplitude increased. In conclusion, given the right conditions, UAE could improve the extraction yield without influencing the collagen structure.

Potential of Atlantic Codfish (Gadus morhua) Skin Collagen for Skincare Biomaterials.

Collagen is the major structural protein in extracellular matrix present in connective tissues, including skin, being considered a promising material for skin regeneration. Marine organisms have been attracting interest amongst the industry as an alternative collagen source. In the present work, Atlantic codfish skin collagen was analyzed, to evaluate its potential for skincare. The collagen was extracted from two different skin batches (food industry by-product) using acetic acid (ASColl), confirming the method reproducibility since no significant yield differences were observed. The extracts characterization confirmed a profile compatible with type I collagen, without significant differences between batches or with bovine skin collagen (a reference material in biomedicine). Thermal analyses suggested ASColl's native structure loss at 25 °C, and an inferior thermal stability to bovine skin collagen. No cytotoxicity was found for ASColl up to 10 mg/mL in keratinocytes (HaCaT cells). ASColl was used to develop membranes, which revealed smooth surfaces without significative morphological or biodegradability differences between batches. Their water absorption capacity and water contact angle indicated a hydrophilic feature. The metabolic activity and proliferation of HaCaT were improved by the membranes. Hence, ASColl membranes exhibited attractive characteristics to be applied in the biomedical and cosmeceutical field envisaging skincare.

Assessing Malaysian Firms’ Intention to Use Recombinant Collagen-Like Protein in Collagen Products

The study aims to assess the prospect of using recombinant collagen-like protein (RCLP) from producers’ point of view. Using cross-sectional data from a survey, the study attempts to validate the proposed hypothesis within Technology Acceptance Model (TAM) by using the Partial Least Square (PLS) path modeling approach (a variance-based SEM technique). Results show a direct positive and significant relations between ‘perceive ease of use’ and ‘attitude toward’, ‘perceived ease of use’ and ‘perceived usefulness’, ‘attitude toward’ and ‘behavioural intention’, and ‘perceived usefulness’ and ‘behavioural intention’ of producing collagen products sourced from recombinant collagen-like protein among firms. The results imply the high potential end collagen products to be marketed using this alternative source of collagen which is environmentally friendly and promotes sustainable development.

Evaluation of cattle skin collagen for producing co-extrusion sausage casing

Co-extrusion is a fully automated sausage production process that employs a continuous stream of collagen dispersion to encase the extruded meat mass to form an endless sausage rope, that is later crimped into links of selected sizes. Fibrous and soluble type I collagen dispersions obtained from bovine skins of animals aged 18–36 months is used as the raw material for these dispersions.In this study, the chemical and physical properties of cattle skin collagen preparations from four sources [American Calf (AC), Dutch Heavy Veal (DHV), Danish Ox and/or Heifer (DOH), and Heavy German Cow (HGC)] were investigated for their potential application as collagen source for co-extrusion.All dispersions exhibited shear-thinning behavior, following a power-law model with k* values for HGC, DHV, AC, and DOH dispersions of 59, 68, 95 and 114 Pa sn*, respectively. Rheological measurements showed for all dispersions a decrease in elasticity and loss modulus at 35–40 °C. SDS-PAGE indicated the presence of α1(I)- and α2(I)-chains of type I collagen for all dispersions. The mechanical strength of the films was 1.6, 1.6, 1.3 and 1.2 MPa for films prepared from AC, DOH, DHV and HGC dispersions, respectively. After crosslinking a 27% reduction of free amine groups was found for HGC and DOH, followed by 26 and 19% for AC and DHV, respectively.Based on the properties of the dispersions and the films in relation to the co-extrusion process AC, DHV and DOH are potentially suitable as an alternative collagen source.

The Effectiveness of Oral Fish Collagen Supplementation on Skin Aging: A Systematic Review and Meta-analysis of Skin Hydration, Skin Elasticity, and Skin Wrinkles

Introduction: Skin aging is a complex biological process with cumulative structural and physiological changes, progressive changes in each layer of the skin, and changes in the appearance of the skin. Human skin undergoes 2 types of skin aging, that are intrinsic and extrinsic skin aging. Skin aging is characterized by a decrease in skin hydration and elasticity, as well as an increase in skin wrinkles. Anti-aging strategies are still being developed. A new anti-aging therapy modality that has been widely used is nutraceutical supplementation, such as fish collagen. Fish collagen is a new alternative source of collagen with a high degree of homology to human collagen structure and high bioavailability. The aim of this study was to assess the efficacy of oral fish collagen supplementation on skin aging. Methods: This study was an analytic observational study, with systematic review and meta-analysis. Data searching was conducted online at Pubmed-MEDLINE, EBSCO (CINAHL), Scopus, SpringerLink, ProQuest, Cochrane Library, ClinicalTrials.gov, Cambridge Core, and Google Scholar, as well as hand searching from libraries in Indonesia. Twelve studies were included in the qualitative analysis (systematic review) (n=753 subjects) and 6 of them were included in the quantitative analysis (meta-analysis) (n=426 subjects). Results: The results of the meta-analysis showed that the increase in skin hydration in the group given oral fish collagen supplementation was greater significantly than in the placebo group, with standardized mean difference (SMD) (95% CI)=0.56 (0.32 to 0.81), Z=4.47 (p<0.00001), I2=24%. The increase in skin elasticity in the group given oral fish collagen supplementation was greater significantly than in the placebo group, with SMD (95% CI)=0.33 (0.17 to 0.49), Z=4.05 (p<0 ,0001), I2=21%. The reduction in skin wrinkles in the group given oral fish collagen supplementation was greater significantly than in the placebo group, with SMD (95% CI)=-0.47 (-0.74 to -0.19), Z=3.34 ( p=0.0008), I2=49%. Adverse events were not found in the included studies. Conclusion: Oral fish collagen supplementation is effective against skin aging, mainly in increasing skin hydration and skin elasticity, and reducing skin wrinkles.

Hair-Growth-Promoting Effects of the Fish Collagen Peptide in Human Dermal Papilla Cells and C57BL/6 Mice Modulating Wnt/β-Catenin and BMP Signaling Pathways.

Fish-derived collagen has recently emerged as an alternative collagen source with bioactive properties, including the enhancement of hair and skin health. It is also cost-effective and has high bioavailability, in addition to having fewer side-effects compared to collagen from porcine skin or bovine skin. Collagen peptides (CPs) extracted from the scales of Mozambique tilapia (Oreochromis mossambicus) reportedly promote hair and skin health. This study sought to evaluate the effects of CPs on hair growth using in vitro and in vivo models. CP significantly enhanced hair regrowth and the proliferation of human dermal papilla cells (hDPCs) in vitro. CP was orally administered to C57BL/6 mice for 6 weeks to confirm the hair-growth-promoting effects. The mice were divided into four groups: negative control (distilled water), positive control (1 mg/kg of finasteride), CP500 (500 mg/kg of CP), and CP1000 (1000 mg/kg of CP). CP treatment significantly enhanced the proliferation of hDPCs compared to 0.2 μM finasteride, in addition to enhancing hair regrowth. Particularly, CP1000 treatment achieved a hair-growth index similar to that of the PC. In H&E staining, the CP groups exhibited a high A/T ratio. Furthermore, CP increased the expression of hair growth factors (IGF-1, VEGF, krt27, Gprc5d, and Ki67) and decreased the growth inhibitory factor (TGF-β1). Furthermore, CP significantly upregulated the Wnt/β-catenin pathways and downregulated the BMP pathways. Therefore, these results indicate that CP could be used as food supplements and nutraceuticals for hair loss prevention as well as hair regrowth during alopecia.

Characterization of Purified Collagen from Marine Squid Uroteuthis Duvauceli

Collagen is the essential and most abundant structural protein found in the animal kingdom, involving almost 25-30% of the entire body protein content. It is normally found in fibrous tissues, for example, skin, tendons, ligaments, skin, corneas, ligament, bones, veins, teeth, and so on. The skin of the squid is rich in collagen and is an excellent source of raw materials that can be used for the development of collagen products. As such, the use of Uroteuthis duvauceli skin is an alternative source of collagen may be an effective way to obtain high-value-added products. In this study, - the isolated Type 1 collagen was found in Uroteuthis duvauceli (skin and muscle ). Additionally, the characterization of the Type 1 collagen from Uroteuthis duvauceli (skin and muscle ) was examined through various techniques such as SEM, FTIR, XRD, TGA. The skin and muscle showed the typical SDS-PAGE pattern of type I collagen with two different α bands, α1 and α2 and also contains β and γ chains. The fibrillar structures of collagen samples were observed by SEM. FTIR investigation showed the existence of helical arrangements of the type 1 collagen from skin and muscle. UV spectrum of Type1 collagen from Uroteuthis duvauceli skin and muscle has a maximum absorption peak near 230 nm and a minor absorption peak near 280 nm. In XRD, type1 collagen from Uroteuthis duvauceli skin and muscle one wide peak was obtained following with characteristic diffraction peaks of collagen. The results showed that type 1 collagen from skin and muscle had slight differences in molecular weight, amino acid composition, morphological structures, and thermal stability. The present data on collagens from the marine squid, could help the future endeavors to unwind the therapeutically significant, more secure collagens from marine squid for their utilization in biomedical field.&#x0D;

Comparative assessment of bone collagen recovered from different livestock and poultry species: microstructure, physicochemical characteristics and functional properties

SummaryThis study aimed to recover and characterise livestock and poultry bone collagens (LBCs) from yak (YBC), bovine (BBC), porcine (PBC) and chicken (CBC) sources and perform comparative assessment on their microstructure, physicochemical and functional properties. Amino acid compositions, SDS–PAGE and spectroscopic analysis confirmed that LBCs were intact triple‐helical collagen I of [α1(I)]2α2(I) with some structural differences. Scanning electron microscope (SEM) results showed that LBCs displayed a loose and porous fibrous meshwork. The Td values of SCI, YBC, BBC, PBC and CBC were 42.6, 42.3, 44.6, 41.9 and 42.9 °C, and 5.81, 7.15, 6.28, 6.79 and 5.33 of pI values, respectively. Structural differences also endowed LBCs with dissimilar functional properties, such as water‐holding capacity, foaming and emulsifying. The structure–function correlations analysis revealed the structure–function correlations of LBCs. This study offered a new prospect that the sustainable livestock and poultry bones (LBs) might be valorised as an alternative collagen source and provided useful information for the industrial production and fostered further rational valorisation of LBCs.

Microstructural and Physicochemical Analysis of Collagens from the Skin of Lizardfish (Saurida tumbil Bloch, 1795) Extracted with Different Organic Acids.

Marine fish collagen has attracted considerable attention due to its characteristics, including its biodegradability, biocompatibility, and weak antigenicity, and is considered a safer material compared to collagen from terrestrial animals. The aim of this study was to extract and characterize collagen from the skin of lizardfish (Saurida tumbil Bloch, 1795) with three different acids. The yields of acetic acid-extracted collagen (AESkC), lactic acid-extracted collagen (LESkC), and citric acid-extracted collagen (CESkC) were 11.73 ± 1.14%, 11.63 ± 1.10%, and 11.39 ± 1.05% (based on wet weight), respectively. All extracted collagens were categorized as type I collagen with mainly alpha chains (α1 and α2) detected and γ and β chains to some extent. Fourier transform infrared (FTIR) spectra showed an intact triple-helical structure in the AESkC, LESkC, and CESkC. UV-vis spectra and X-ray diffraction further demonstrated the similarity of the extracted collagens to previously reported fish skin collagens. AESkC (Tmax = 40.24 °C) had higher thermostability compared to LESkC (Tmax = 38.72 °C) and CESkC (Tmax = 36.74 °C). All samples were highly soluble in acidic pH and low concentrations of NaCl (0–20 g/L). Under field emission scanning electron microscopy (FESEM) observation, we noted the loose, fibrous, and porous structures of the collagens. The results suggest that the lizardfish skin collagens could be a potential alternative source of collagen, especially the AESkC due to its greater thermostability characteristic.

In vitro angiotensin-converting enzyme and dipeptidyl peptidase-IV inhibitory, and antioxidant activity of blue mussel (Mytilus edulis) byssus collagen hydrolysates

AbstractLarge quantities of mussel byssus are generated annually as a co-product of the mussel-processing industry. This fibrous material is a rich source of collagen, which when extracted has potential uses as an alternative source of collagen for food applications. However, due the complex structure of the material, the extraction of the collagenous components using food-friendly strategies has proved challenging to date. An enzyme-aided method, using a proline endoproteinase, was employed for the extraction of collagen from mussel byssus yielding 138.82 ± 2.25 mg collagen/g dry weight. Hydrolysates of the collagen extract were generated using five food-grade enzyme preparations with Corolase® PP giving the highest extent of hydrolysis. Reversed-phase and gel permeation high-performance liquid chromatography of the extracted collagen and its enzymatic hydrolysates showed significant hydrolysis of collagen. The hydrolysates generated with Corolase® PP showed the highest in vitro bioactivities: angiotensin-converting enzyme (ACE) IC50 = 0.79 ± 0.17 mg/ml, dipeptidyl peptidase-IV (DPP-IV) IC50 = 0.66 ± 0.17 mg/ml and oxygen radical absorbance capacity (ORAC) activity = 311.23 ± 13.41 µmol trolox equivalents (TE)/g. The results presented herein indicate that in addition to acting as an alternative source of collagen for food applications, mussel byssus collagen-derived hydrolysates have potential applications as functional food ingredients for the management of metabolic diseases such as type II diabetes and hypertension.

Properties and Characteristics of Acid-Soluble Collagen from Salmon Skin Defatted with the Aid of Ultrasonication

Salmon skin, a byproduct from the deskinning process, can be used as an alternative source of collagen. Due to the high fat content in skin, the defatting process is required prior to extraction. The properties and characteristics of acid-soluble collagen (ASC) from salmon skin (Oncorhynchus nerka), defatted using isopropanol without and with ultrasonication (70% amplitude for 10 min), were investigated. The ASC from the skin that was defatted with aid of ultrasonication (U-ASC) exhibited lower (p &lt; 0.05) fat content (1.86%) with extraction yield (23.18% w/w, dry weight basis). U-ASC had a higher hydroxyproline content (49.15 mg/g dry sample) and maximum transition temperature (Tmax) (11.6 °C) than C-ASC (collagen extracted from skin defatted without ultrasonication). Both of the ASCs were classified as type I collagen. C-ASC and U-ASC had isoelectric points of 7.17 and 7.40, respectively. Fourier transform infrared (FTIR) and circular dichroism spectra reconfirmed the triple-helix structure of both ASCs. The major amino acid of both collagens was glycine (297–308 residues/1000 residues). A high amount of imino acid (191–193 residues/1000 residues) was also found. After gastrointestinal digestion, the degree of hydrolysis of the digested U-ASC (23.19%) was slightly higher than that of the digested C-ASC (22.31%). However, both digests had no differences in antioxidant activities. Both of the ASCs could be therefore used as functional ingredient.

Effects of sonication on the extraction of pepsin-soluble collagens from lamb feet and product characterization

This study was conducted to extract pepsin-soluble collagen with ultrasound aided process (UPSC) from lamb feet and investigate the effects of ultrasonic treatment at different temperatures and times on collagen concentration and structure. The most effective extraction condition for collagen by ultrasonic treatment was 25 °C/60 min. The collagen concentration of the UPSC increased as the sonication time (20, 40, and 60 min) increased at the same temperature (P < 0.05). All UPSCs were characterized as Type I collagen composed of α1 and α2 chains. The Fourier transform infrared spectra showed that the collagens maintained their triple helical structure, even after ultrasonic treatment in combination with pepsin digestion. The scanning electron microscopy images of the UPSCs revealed that sonication could cause some physical changes. These results suggest that lamb feet can be an alternative source of collagen for the food, pharmaceutical, and nutraceutical industries.

In vitro and in vivo genotoxicity and cytotoxicity analysis of protein extract from Aplysina fulva sponges

This study evaluated the physicochemical and morphological properties of a marine sponge protein extract (PE) using scanning electron microscopy (SEM), Energy dispersive X-ray spectroscopy (EDS), analysis of mass loss and pH and in vitro and in vivo. Scanning electron microscopy showed that PE fibers present a granular aspect and irregular structure and the element carbon followed by oxygen was detected in the EDS analysis. Moreover, a 29% of mass loss was observed after 14 days and the pH slightly modified after 14 days. Cell viability of fibroblast cells (L929) of control and PE at a concentration of 25% demonstrated higher values compared to the groups. Osteoblast cell viability of PE at 25 and 50% was significantly higher. Comet assay on day 1 showed higher values for PE at 25%. In addition, in vivo experiments demonstrated that in the treated animals, the bone defects were filled with biomaterial particles, granulation tissue and some areas of newly formed bone. Furthermore, similar immunoexpression of Runx-2 and Cox-2 was observed. Taken together, all results suggest that PE is biocompatible, present non-citotoxicity in the in vitro studies (at the lower concentration) and in the in vivo studies and it can be considered as an alternative source of collagen for tissue engineering proposals.