Collagen Yield Research Articles

Sea grapes powder with addition of tempe rich in collagen: An anti-aging functional food.

Background: This study aimed to determine the potential anti-aging effects of sea grapes and tempe (Fermented soybeans) collagen particle size, by measuring the activities of anti-glycation, antioxidant and tyrosinase inhibitors. Methods: Collagen was isolated from sea grapes and tempe freeze dried powder and treated with different NaOH concentrations (0.10 M; 0.20 M; 0.30 M), and CH 3COOH 1 M solution, separately. The collagen particle size was adjusted by stirring at 1000 rpm for 5 and 10 hours. 2,2-diphenyl-1-picrylhydrazyl (DPPH) was used to measure the antioxidant activity, and L-tyrosine and L-DOPA (l-3,4-dihydroxyphenylalanine) were used as a marker of tyrosine inhibition. Results: The collagen treated with 0.10 M NaOH produced the highest collagen yield (11.65%), and largest particle size (2455 nm). Additionally, this collagen, when treated for 5 hours, exhibited 24.70% antioxidant activity, 62.60% anti-glycation, 8.97% L-tyrosine, and 26.77% L-Dopa inhibition activities. Meanwhile, the collagen treated for 10 hours had a 9.98% antioxidant activity, 41.48% anti-glycation, 7.89% L-tyrosine, and 2.67% L-Dopa inhibition activity. Conclusion: Sea grapes and tempe collagen powder treated with 0.10 M NaOH and stirred for 5 hours, as functional foods have anti-aging properties.

CHARACTERISTICS OF FRESHWATER MUSSEL SHELL (Pilsbryoconcha sp.) COLLAGEN ORIGINATING FROM SUNGAI PAKU WATERS EXTRACTED WITH DIFFERENT ACETIC ACID CONCENTRATIONS

This study was aimed to determine the characteristics of freshwater mussel shell collagen originating from Paku river waters extracted with different concentrations of acetic acid and to determine the best concentrations of acetic acid to produce the highest collagen yields. The different concentration of acetic acids to produce collagen was 0.50 M, 0.75 M and 1 M. The parameters of the analysis observed were collagen yield, proximate analysis (moisture, ash, fat, and protein content), pH and heavy metal analysis (Pb and Cd). The use of 0.50 M acetic acid concentration was the best concentration to produce collagen with the characteristics of a yield value of 18.76%, a moisture content value of 6.64%, ash content value of 82.60%, fat content value of 0.28%, protein content value of 6.81%, a pH value of 6.77, The heavy metal content of Pb 0.53 mg/kg and Cd 0.07 mg/kg.

Comparison of collagen characteristic from the skin and swim bladder of Gulf corvina (Cynoscion othonopterus)

Collagens extracted from different tissues and fish species display different physicochemical properties, thus novel sources require characterization. Gulf corvina (Cynoscion othonopterus) is processed industrially for food. Of the by-products, the swim bladder is used for fish maw, but other tissues are treated as waste. In the present study, pepsin‐soluble collagen from Gulf corvina skin and swim bladder was extracted and characterized. Skin produced a higher collagen yield (82 ± 1.53 %) than swim bladder (69 ± 1.60 %). Both collagens exhibited electrophoresis bands corresponding to ([α1(I)]2α2(I)) and β chains, all characteristic of type I collagen. Spectra analysis showed the collagens to maintain their triple-helix structure. The skin collagen had a lower denaturation temperature (29.8 °C) than the swim bladder collagen (32.5 °C), due to its relatively low imino acid content (168 vs. 190 /1000 residues, respectively). Both collagens were highly soluble in acidic pH ranges; Zeta potential values were 5.5 for the skin collagen and 6.2 for the swim bladder collagen. Gulf corvina skin and swim bladder are excellent sources of type I collagen with similar physicochemical properties.

Review Article: Fish Bone Collagen

Fishbone collagen is an alternative source of bovine and pig collagen. The purpose of this article is to review the types, benefits, extraction methods and characterization of collagen from fish bones, especially freshwater fish. The result of the review shows that the collagen from tilapia bones is shaped like a sheet with a slight porous surface and is of type I. Collagen extraction begins with bone disease from the remaining fat, then degreasing and the next step is extraction. After the extraction process is complete, filtration is carried out to store the filtrate or residue, then the collagen is purified by salting-out with NaCl. Collagen yield and collagen pH value from collagen extraction were different for each type of fish bone. The difference in yield value and protein and amino acid content in the resulting collagen can be caused by differences in the extraction method, the concentration of the solution used, whether acid or alkaline, and the neutralization process and the type of raw material. Fishbone collagen has good benefits in the cosmetic and pharmaceutical fields.

Proteome Variation with Collagen Yield in Ancient Bone.

Isotope analyses are some of the most common analytical methods applied to ancient bone, aiding the interpretation of past diets and chronology. For this, the evaluation of “collagen yield” (as defined in radiocarbon dating and stable isotope research) is a routine step that allows for the selection of specimens that are deemed adequate for subsequent analyses, with samples containing less than ∼1% “collagen yield” normally being used for isotopic analysis but discounted for radiocarbon dating. The aims of this study were to use proteomic methods of MALDI–TOF (matrix assisted laser desorption ionization time-of-fligh mass spectrometry) and LC−ESI−MS/MS (liquid chromatography electrospray ionization tandem mass spectrometry) to investigate the endogeneity of the dominant proteinaceous biomolecules within samples that are typically considered to contain poorly preserved protein. Taking 29 archaeological samples, we evaluated the proteome variability between different acid-soluble fractions removed prior to protein gelatinization and considered waste as part of the radiocarbon dating process. We then correlated these proteomes against the commonly used “collagen yield” proxy for preservation. We found that these waste fractions contained a significant amount of both collagenous and noncollagenous proteins (NCPs) but that the abundance of these was not correlated with the acquired “collagen yield”. Rather than a depleted protein load as would be expected from a low “collagen yield”, the variety of the extracted NCPs was comparable with that commonly obtained from ancient samples and included informative proteins useful for species identification, phylogenetic studies, and potentially even for isotopic analyses, given further method developments. Additionally, we did not observe any correlation between “collagen yield” and peptide mass fingerprint success or between the different fractions taken from the same sample but at different radiocarbon pretreatment stages. Overall, these findings highlight the value in retaining and analyzing sample fractions that are otherwise discarded as waste during the radiocarbon dating process but more importantly, that low “collagen yield” specimens that are often misinterpreted by archaeologists as being devoid of protein can still yield useful molecular sequence-based information.

Distinctive characteristics of collagen and gelatin extracted from Dosidicus gigas skin

SummarySquid skin, often discarded as processing by‐product, is a good resource of collagen/gelatin. In this study, acid soluble collagen (ASC), pepsin soluble collagen (PSC) and water soluble gelatin (WSG) were extracted from squid (Dosidicus gigas) skin and physicochemically examined. The lowest yield of 33.5% was obtained for ASC extracted at 4 °C, and the addition of pepsin increased the collagen yield by around 35.0% (PSC). The highest yield of 81.9% (WSG) was achieved by thermal extraction at 60 °C. A low temperature can largely retain the native helix structures of ASC and PSC, contrariwise, thermal treatment converted collagen into gelatin with unordered and renatured structures. The proline and hydroxyproline contents of ASC, PSC and WSG were 183/1000 residues, 194/1000 residues and 175/1000 residues, respectively. In addition, WSG showed a denaturation temperature at 80.7 °C which was much higher than that of ASC (24.2 °C) and PSC (26.2 °C), while a significant lower resistance towards enzymatic digestion.

“Here we go again”: the inspection of collagen extraction protocols for 14C dating and palaeodietary analysis

ABSTRACT Archaeological bone collagen is highly useful for radiocarbon (14C) dating and palaeodietary reconstruction. However, collagen preservation and carbon contamination are essential considerations when extracting collagen, becoming especially crucial close to the limit of the method (50,000 years before present = BP). Strong progress has been achieved in the past two decades by 14C and stable isotopic laboratories in removing contamination from archaeological bones, but different pretreatment protocols have been proven to produce varying results. Here we compare three collagen extraction protocols used for palaeodietary studies and 14C dating, considering collagen yield, elemental and stable isotopic data, FTIR analysis, and 14C dates. We focus on the impact of ultrafiltration on the yield and quality of the extracted material. The results again underline the importance of rigorous decontamination methods to gain accurate 14C dates and demonstrate that different protocols have significant effects on the quality and yield of extracted collagen.

Using bone bioapatite yield for quality control in stable isotope analysis applications

Since the late 1970s, stable isotope analysis of bone has become a routine method in archaeological science for reconstructing an individual’s life history. There is published guidance for assessing bone quality prior to stable isotope analysis, including measurement of bioapatite molecular structure, collagen yield, and collagen element content. This study investigated bioapatite yield as an additional quality indicator. Bioapatite and collagen were extracted from 182 modern (20th Century) and 272 prehistoric (5420–230 cal BP) human skeletal elements. As expected, modern remains were well-preserved, with ranges of 3–28% for collagen yield and 3.1–3.4 for the atomic carbon-to-nitrogen (C:N) ratio; bioapatite yield ranged from 21% to 63%. There was a significant, but only fair, negative correlation between bioapatite and collagen yields of modern samples (r = -0.31, p < 0.0001). Conversely, no correlation was observed between bioapatite and collagen yields of prehistoric samples, suggesting preservation of one is not indicative of preservation of the other. Prehistoric sample condition was evaluated by measuring the infrared splitting factor (IR-SF) to evaluate bioapatite crystallinity and the carbonate-to-phosphate (C/P) ratio to measure carbonate concentration; yield and C:N ratio were used to evaluate collagen condition. Prehistoric samples in the best condition had bioapatite yields between 29% and 62%, within the range of modern samples. In contrast, prehistoric samples in poor condition had significantly higher bioapatite yields, suggesting diagenetic addition of material. The range of bioapatite yields from modern bone samples, 21–63%, is proposed as the least conservative acceptable threshold for screening bone prepared for stable isotope analysis.

SUITABILITY OF ACID-SOLUBLE AND ACID-INSOLUBLE LEATHER FRACTIONS IN RADIOCARBON DATING

ABSTRACTLeather has been produced by a variety of methods throughout human history, providing researchers unique insight into multiple facets of social and economic life in the past. Archaeologically recovered leather is often fragile and poorly preserved, leading to the use of various conservation and restoration efforts that may include the application of fats, oils, or waxes. Such additives introduce exogenous carbon to the leather, contaminating the specimen. These contaminants, in addition to those accumulated during interment, must be removed through chemical pretreatment prior to radiocarbon (14C) dating to ensure accurate dating. DirectAMS utilizes organic solvents, acid-base-acid (ABA) and gelatinization for all leather samples. Collagen yield from leather samples is variable due to the method of production and the quality of preservation. However, evaluating the acid-soluble collagen fraction, when available, provides the most accurate 14C dates for leather samples. In instances where gelatinization does not yield sufficient material, the resulting acid-insoluble fraction may be dated. Here we examine the effectiveness of the combined organic solvent and ABA pretreatment with gelatinization for leather samples, as well as the suitability of the acid-insoluble fraction for 14C dating.

Linking structural and compositional changes in archaeological human bone collagen: an FTIR-ATR approach

Collagen is the main structural and most abundant protein in the human body, and it is routinely extracted and analysed in scientific archaeology. Its degree of preservation is, therefore, crucial and several approaches are used to determine it. Spectroscopic techniques provide a cost-effective, non-destructive method to investigate the molecular structure, especially when combined with multivariate statistics (chemometric approach). In this study, we used FTIR-ATR spectroscopy to characterise collagen extracted from skeletons recovered from necropoleis in NW Spain spanning from the Bronze Age to eighteenth century AD. Principal components analysis was performed on a selection of bands and structural equation models (SEM) were developed to relate the collagen quality indicators to collagen structural change. Four principal components represented: (i) Cp1, transformations of the backbone protein with a residual increase in proteoglycans; (ii) Cp2, protein transformations not accompanied by changes in proteoglycans abundance; (iii) Cp3, variations in aliphatic side chains and (iv) Cp4, absorption of the OH of carbohydrates and amide. Highly explanatory SEM models were obtained for the traditional collagen quality indicators (collagen yield, C, N, C:N), but no relationship was found between quality and δ13C and δ15N ratios. The observed decrease in C and N content and increase in C:N ratios is controlled by the degradation of protein backbone components and the relative preservation of carbon-rich compounds, proteoglycans and, to a lesser extent, aliphatic moieties. Our results suggest that FTIR-ATR is an ideal technique for collagen characterization/pre-screening for palaeodiet, mobility and radiocarbon research.

Physicochemical characterization and self-assembly of human amniotic membrane and umbilical cord collagen: A comparative study

The diverse application of collagen has created a need to discover renewable and economical sources with prevailing/improved physico-chemical properties. To address this scenario, the present study has extracted collagen from Human Amniotic Membrane (AM) and Umbilical cord, which are treated as medical waste and compared its physico-chemical properties. Collagen was extracted by pepsin solubilization using various salt concentrations (1 M, 2 M and 4 M). Umbilical Cord Collagen (UC) yield was 10% higher than Amniotic Membrane Collagen (AC). UC reported 58% higher sulphated glycosaminoglycan content than AC. Electrophoretic pattern of AC and UC in both disulphide bond reducing and non-reducing conditions showed bands corresponding to collagen type I, III, IV, V and XV. Collagen morphology was examined using SEM and the amino acid content was quantified by HPLC and LC-MS/MS. Triple helicity was confirmed by CD and FTIR spectra. Thermal transition temperature of AC and UC was found equivalent to animal collagen. Self-assembly, fibril morphology and spatial alignment was studied using AFM and DLS. Biocompatibility was analyzed using 3T3 fibroblast cells. In conclusion, UC with higher yield, presented with better physico-chemical, structural and biological properties than AC could serve as an efficient alternative to the existing animal collagen for diverse applications.

Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

Abstract The aim of this study was to investigate the effect of acid pretreatment, temperature and enzyme concentration on the acid-enzymatic extraction of soluble collagen from chicken keel bone cartilage. A chemical composition analysis and protein profile characterization of this slaughter by-product were also conducted. The cartilages were extracted with 0.5 mol/L of acetic, lactic and citric acids for 24, 48 and 72 hours. Subsequently, optimization with a 22 factorial design was performed with three replications at the central point for a total of 7 experiments; the analyzed response was the collagen content of the obtained isolates. The cartilage under study has a high protein content (90.27% dry basis) consisting of approximately 35.7% collagen and is a source of essential and predominantly hydrophobic amino acids. Pretreatment with acetic acid for 24 hours led to greater extraction potential and consequently, a better collagen yield (30.12%). The electrophoretic profile of the obtained collagens revealed the existence of an α1 chain, indicating that this collagen was type II. Statistical analysis demonstrated that the acid-enzymatic procedure favored a temperature of 30 °C.

Isolation and characterization of collagen from local goat bone using pepsin hydrolysis

Goat bone is one of by-product which has not commonly used in Indonesia. Collagen is one of proteins which contained a bone which characterizing its uniq function. The purpose of experiment was to isolate and characterize collagen from local goat bone with pepsin enzymatic hydrolysis in various concentration. The experiment consisted of bone preparation, Isolating by leaching method, and the hydrolysis of collagen bone using pepsin enzyme in various concentration (0.1; 0.3; 0.5; and 1%). Variables observed were collagen yield, soluble protein, pH, Fourier Tansform Infrared Spectroscopy (FTIR) spectra, thermal stability using Differential Scanning Calorimetry (DSC), and molecular weight using Sodium Dodesyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). The results showed that soluble protein concentration of collagen solution was not affected by pepsin concentrations. The soluble protein of 0.1; 0.3; 0.5 and 1 % of enzym were 0.203±0,013; 0.244±0,045; 0.295±0,065; and 0.257±0,066 mg/ml for, respectively. The results of collagen yield was significant, and it were 7.12; 7.54; 13.3; dan 8.81 %. The results of pH showed significant, it was 6.37; 5.96; 6.88; 5.92. The FTIR spectra showed that all of the sample has not changed into gelatin. The thermal stability in DSC analysis showed that the collagen start to gelation at 56.72 to 57.40 °C and Tmax for each sample were 128.20; 189.32; 131.35; 124.43 °C, respectively. In conclusion, collagen could be isolated from goat bone using enzymatic treatment and showed the fine properties as well as collagen from skin.

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin.

Skin waste from tuna processing needs to be utilized, such as extraction of its collagen and gelatin. Their functional properties can be improved by enzymatic hydrolysis for conversion to peptides. Thus, the research objectives were to examine the characteristics and antioxidant activity of collagen, gelatin, and the derived peptide from yellowfin tuna skin. Collagen was extracted using 0.75 M acetic acid at 4 °C, while gelatin was prepared using 0.25% citric acid and extracted at 65 °C. Hydrolysis was carried out with 2% Alcalase, followed by fractionation with a molecular weight cut off sieve for both collagen and gelatin. Collagen yield was 22.6% with pH value of 6.63 and whiteness of 96.7%. Gelatin yield was 20.0% with pH value of 4.94 and whiteness of 51.0%. Hydrolysis for three hours resulted in 52.7% and 45.2% degree of hydrolysis for collagen and gelatin, respectively. The molecular weights of collagen peptides ranged from 2.94 to 11.93 kDa, while those of gelatin peptides ranged from 3.54 to 16,620 kDa. Antioxidant activities of these peptides were higher than those before hydrolysis. The high antioxidant activity (IC50) of collagen peptides were found in <3, 3–10, and 10–30 kDa fractions as well as in the gelatin peptides.

Determination of Nano-Collagen Quality from Sea Cucumber Holothuria scabra

Sea cucumber contains high collagen protein and potential to be used in cosmetics and health. The aim of this study are to determine the quality of sea cucumber collagen using hydrochloric acid with different concentrations and the quality of nano-collagen using stirrer magnetic in different stirring times. This study was conducted by an experimental method using stages of the collagen extraction process and manufacture of nano-collagen. Process of extracting sea cucumber meat collagen using different concentrations of HCl (4%, 5%, and 6%), and process of making nano-collagen using 96% ethanol solution with different stirring times (one, two, three hours). Sea cucumber collagen with the 6% HCl extraction process obtained optimally results with collagen yield of 20.76%, white degree 73.97%, moisture level 10.99%, protein 98.3%, ash 0.86%, fat 0.59%, and collagen pH 3.92. The functional groups in collagen in accordance with the standard collagen compounds. The nano-collagen obtained was in the form of a creamy white powder (79.25% white degree), moisture 9.11%, ash 0.68%, fat 0.51%, protein 98.9%, pH 3.98, and particle size 285 nm.

Twenty years on, a new date with Lascaux. Reassessing the chronology of the cave’s Paleolithic occupations through new 14C AMS dating

Aside from the stylistic debates and quarrels fueled by the studies of its painted and engraved walls, the Lascaux Cave stands out by its very weak and contradictory radiometric framework (Delluc and Delluc 2012). In addition to this, no comprehensive, interdisciplinary study of the rich archaeological assemblages has been conducted for almost forty years (Leroi-Gourhan and Allain 1979). The LAsCO project (Langlais and Ducasse coord.) aims to fill this gap by proposing a global reassessment of the osseous and lithic artifacts, ornaments, ochres and lamps. As part of this work, a new effort has been made to clarify the Paleolithic chronology of the human activities documented by this stratified evidence. Five reindeer remains taken from the cave’s main areas (Axial Gallery, Passageway, Nave, Shaft), some showing clear evidence of anthropic exploitation, were therefore selected to be dated in order to test (1) the chronological homogeneity of the occupations, as already suggested by a high typo-technological coherence and, if this was confirmed, (2) the hypothesis of an attribution to the Badegoulian-to-Magdalenian transition phase, as indicated by prior inter-site comparisons (Langlais 2010 ; Ducasse et al. 2011; DEX_TER project: Ducasse and Langlais coord.). All the selected samples were sent to the Oxford Radiocarbon Accelerator Unit (ORAU) and run on a MIni CArbon DAting System (MICADAS) after an ultrafiltration pretreatment. While the sample from the Passageway area failed due to low collagen yield, the other four produced reliable and highly comparable measurements centered on a 14C age of 17,600 uncal. BP (21.5-21 cal ka BP). These results confirm the two basic assumptions described above and contradict the diachronic framework defined by the 1948-2002 radiometric data, while restoring a certain degree of chronological consistency which fits well with the main typo-technological features of the lithic and osseous equipment (Allain 1979, Leroy-Prost 2008 and ongoing analysis). After a brief outline of the existing radiometric data and a detailed description of the sampling and dating strategy, the reliability of the results and their impact on our understanding of the cave’s phase(s) of occupation(s) are discussed in depth. While the issue of the precise “cultural” attribution of the dated assemblages and the links between the latter and the parietal art are beyond the scope of this paper, these new data represent a first but significant step towards a global renewal of the highly controversial chronological framework of the Lascaux Cave.

Acid-Pepsin Soluble Collagen from Saltwater and Freshwater Fish Scales

Extraction and characterization of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from scales of Giant groupers (saltwater fish) and Nile tilapia (freshwater fish) were carried out in this research. Due to a higher protein content in scales, collagen yield extracted from the Giant groupers scales was higher than that of the Nile tilapia scales. The yield increased as extraction time increased for both ASC and PSC and pepsin extraction resulted in higher yields than acid extraction. Even though there were differences in collagen yields, collagen characteristics were independent of the scale sources but some differences were observed for the ASC and PSC. The peptide hydrolysis patterns of the ASC showed a wide range of molecular weights whereas all of the PSC had similar molecular weight of around 42 kDa. FTIR spectra showed that all the collagens remained the triple helical structure though ASC might be self-aggregated. From zeta potential analysis, net charge of zero was found at pH 3.2-4.0 and the dynamic light scattering suggested that the average particle sizes at pH 11-12 were around 100-200 nm. The denaturation temperatures (T(d)s) in a range of 35-42 degrees C indicated that the collagens were considerably thermally stable.

New Strategy to Cope with Common Fishery Policy Landing Obligation: Collagen Extraction from Skins and Bones of Undersized Hake (Merluccius merluccius).

In order to promote sustainable fishing practices within European fishing fleets and to avoid the large waste of valuable fish biomass through the practice of fish discarding, the new reform of the common fisheries policy includes the obligation of landing all species under total allowable catch (TAC) regulations. The new policy also prohibits the use of specimens under minimum conservation reference size for direct human consumption. In this context, it is necessary to find new uses for undersized fish, which might help to alleviate the costs associated with the landing obligation but without prompting the creation of a market. European hake (EH) (Merluccius merluccius), which is one of the most important commercial fish species for the Spanish fishing industry, with a total TAC for 2018 of 37,423 t, is used for this study. Consistent with the current policy framework and taking into account the commercial importance of this species, the aim of this work is to study a new strategy for the extraction of collagen from the skin and bone fraction of Merluccius merluccius undersized discards. Three collagen fractions are successfully isolated for the first time from the skin of M. merluccius skin and bone discarded raw material: acid-soluble collagen (ASC) fraction 1 and pepsin-soluble collagen (PSC) fraction 2 from the skin and ASC fraction 3 from bones. The total collagen yield of the process is 13.55 ± 3.18% in a dry basis (g collagen/100 g of skin and bone fraction (SBF)) and 47.80 ± 9.83% (g collagen/100 g of collagen determined by the hydroxyproline content in SBF). The three fractions are further characterized by using different physical and chemical analysis techniques, with the conclusion drawn that the triple helix structure is preserved in the three fractions, although ASC fractions (F1 and F3) present more or stronger hydrogen bonds than the PSC fraction (F2). With the process herein presented, deboned and skinned hake specimens could represent an interesting source of high quality type I collagen, which could be useful as a raw material for the biomedical, cosmetic, and nutraceutical industries.

The Difference Characteristicsof Collagen from Tilapia (Oreochromis niloticus) Bone, Skin, and Scales

Tilapia (Oreochromis niloticus) is one of the main commodities of freshwater fish in Indonesia. Mostly, tilapia is exported in the form of fillets which produce residual processing including bobe, skin, and scales which can reach 50 to 70% of the total weight of fish. The aimed of this study was to extract and characterize collagen from bone, skin, and scales of tilapia. The research method used a Completely Randomized Design (CRD) by treating the different types of collagen raw materials, namely bone, skin, and scales of tilapia. The results showed that the type of raw material affected the yield, water content, color, and pH (p&lt;0.05). The collagen yield in this study was 0.53% (bone), 0.63% (scales) and 0.94% (skin). The small amount of amendment was caused by the concentration of acetic acid being too low. the smallest water content in tilapia fish collagen 2.17%; the best brightness of collagen in fish bones 76.91%; the value of the largest degree of white on fish scales 75.95%; pH content close to neutral fish collagen scales 6.49; Morphological results of collagen produced using SEM, the presence of pores seen in the collagen of tilapia fish due to the space between the collagen fibers while. Collagen from the skin and scales has the same morphology, which is shaped in small squares and smooth surface without pores

Extraction and structural characterization of collagen from fishbone by high intensity pulsed electric fields

AbstractCollagen was extracted from fishbone by high intensity pulsed electric fields (PEF) and its structure was characterized. A maximum collagen yield of 16.13 mg/mL was achieved under the following conditions: pepsin dosage of 1%, material‐liquid ratio of 1:10, electric field strength of 20 kV/cm, and pulse number of 8. The change of each secondary structure component content was highly correlated with the PEF operating parameters (R2 &gt; .900). The tertiary structure of collagen was changed by PEF. The surface hydrophobicity increased first and then decreased with the PEF operating parameters. Scanning electron microscopy results showed the tissues changes of sample particles from dispersed and disorganized to uniform by PEF, but the high electric field strength (&gt;30 kV/cm) and pulse number (&gt;8) causes samples over agglomerated, which were dispersed disorderly. This article has proposed a new approach for comprehensive utilization of fishbone, which has important research significance for the promotion of PEF.Practical ApplicationsCollagen was extracted from fishbone by high intensity pulsed electric fields. The prepared fishbone collagen can be widely used in foods, cosmetics, biology, fertilizers, medical materials, and other fields. This article provides a new technique for comprehensive utilization of fishbone. The structure of extracted collagen was characterized. This opens up a new dimension in the study of the impact of PEF technology on protein structure.