scholarly journals Physicochemical characteristics of acid soluble collagen from the skin of Parang parang fish (Chirocentrus dorab)

2019 ◽  
Vol 22 (3) ◽  
pp. 441-452
Author(s):  
Mega Safithri ◽  
Kustiariyah Tarman ◽  
Pipih Suptijah ◽  
Neni Widowati
Keyword(s):  
Acetic Acid ◽  
Fourier Transform ◽  
Transition Temperature ◽  
Physicochemical Characteristics ◽  
Denaturation Temperature ◽  
Spectra Analysis ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Collagen Protein ◽  
The Fourier Transform

Waste of parang parang fish (Chirocentrus dorab) skin can be used as a source of collagen. Collagen isolation can be done chemically by the Acid Soluble Collagen (ASC) method. The objective of this research was to isolate collagen with ASC method and characterize their physicochemical. Collagen isolation consisted of pretreatment and hydrolysis with acids. The pretreatment used NaOH 0.1 M for 12 hours, while hydrolysis used acetic acid 0.5 M. Pretreatment results indicated that the concentration of non-collagen protein was 0.1243 mg/mL, while the yield collagen was 2.61%. The collagen had the viscosity of 6.50 cP, the denaturation temperature of 4°C, the transition temperature of 77.30°C, and the melting temperature of 153.90°C. The obtained collagen also had pH of 6.25. The fourier transform infrared (FTIR) spectra analysis showed the collagen contained amide A (3425.58), B (2924.09), I (1647.21), II (1543.05), and III (1246.02) (cm-1). The collagen also contained glycine (26.69%), proline (12.24%) and alanine (9.51%).

scholarly journals Characterization of Acid Soluble Collagen from Redbelly Yellowtail Fusilier Fish Skin (Caesio cuning)

2016 ◽  
Vol 19 (1) ◽  
pp. 79 ◽  
Author(s):  
Ika Astiana ◽  
Nurjanah Nurjanah ◽  
Tati Nurhayati
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Raw Material ◽  
Fish Skin ◽  
Soaking Time ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Collagen Protein ◽  
Acid Process

<p>Fish skin can be used as raw material for producing collagen. The collagen can be extracted by chemical<br />or combination of chemical and enzymatic processes. Extraction of collagen chemically can do with the<br />acid process that produces acid soluble collagen (ASC). This study aimed to determine the optimum<br />concentration and time of pretreatment and extraction, also to determine the characteristics of the acid<br />soluble collagen from the skin of yellow tail fish. Extraction of collagen done by pretreatment using NaOH at<br />the concentration of 0.05; 0.1; and 0.15 M and extraction using acetic acid at the concentration of 0.3; 0.5; and<br />0.7 M. Pretreatment NaOH with concentration 0.05 M and soaking time of 8 hours is the best combination<br />for eliminating non collagen protein. Combination treatment of acetic acid at the concentration of 0.3 M<br />for 3 days obtained the best solubility. The yield of collagen ASC was 18.4±1.49% (db) and 5.79±0.47%<br />(wb). Amino acid composition that is dominant in the ASC collagen was glycine (25.09±0.003%), alanine<br />(13.71±0.075%), and proline (12.15±0.132%). Collagen from yellow tail fish skin has α1, α2, β and γ<br />protein structure with the molecular weight of 125, 113, 170-181, and 208 KDa. The transition and melting<br />temperatures of collagen were 67.69oC and 144.4oC. The surface structure of collagen by analysis of SEM has<br />fibers on the surface.<br />Keywords: cholesterol, fatty acids, meat tissue, proximate, red snapper (L. argentimaculatus)</p>

Acetic acid-soluble collagen in human scars

1959 ◽  
Vol 24 (6) ◽  
pp. 618
Author(s):  
W G Banfield ◽  
D C Brindley
Keyword(s):  
Acetic Acid ◽  
Soluble Collagen ◽  
Acid Soluble Collagen

scholarly journals Diluted Acetic Acid Softened Intermuscular Bones from Silver Carp (Hypophthalmichthys molitrix) by Dissolving Hydroxyapatite and Collagen

Foods ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 1
Author(s):  
Yueyue Liu ◽  
Huiman Jiang ◽  
Longteng Zhang ◽  
Yuqing Tan ◽  
Yongkang Luo ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Fourier Transform ◽  
Silver Carp ◽  
Hydroxyl Groups ◽  
Consumer Health ◽  
Hypophthalmichthys Molitrix ◽  
Physical Hazards ◽  
Collagen Molecules ◽  
Calcium And Phosphorus ◽  
The Fourier Transform

Intermuscular bones (IBs) pose physical hazards that threaten consumer health and food safety. This study aimed to investigate the mechanism of softening IBs from silver carp with diluted acetic acid. IBs (separated from muscle) and fillets (without removing IBs) were treated with diluted acetic acid. Analyses of sensory attributes and the hardness of treated IBs indicated that diluted acetic acid (<10 mmol/L) could soften IBs effectively. Additionally, 0.5 mmol/L acetic acid softened IBs within fillets without significantly affecting the texture and flavor of fillets. Analyses of microstructure, minerals (calcium and phosphorus) and collagen content, and the Fourier transform infrared (FTIR) spectra of IBs indicated that acetic acid broke connections (formed by collagen that shared hydroxyl groups) between collagen molecules, and between collagen and hydroxyapatite (HAP), thus inducing the dissolution of collagen and HAP. The dissolution of HAP contributed more to IBs softening than collagen.

Analysis and improvement of stability of pepsin-solubilized collagen from skin of carp (Cyprinus carpio)

2012 ◽  
Vol 66 (7) ◽  
Author(s):  
Rui Duan ◽  
Jun-Jie Zhang ◽  
Kunihiko Konno ◽  
Mei-Hua Wu ◽  
Jing Li ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Cyprinus Carpio ◽  
Short Peptides ◽  
Type I ◽  
Improved Method ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Dialysis Solution ◽  
Sds Page ◽  
Carp Cyprinus Carpio

AbstractPepsin is widely used for the extraction of pepsin-solubilized collagens (PSC) from many resources. PSC-A and PSC-P were prepared from carp skin using 0.1 mol L−1 acetic acid and 0.02 mol L−1 Na2HPO4 (pH 7.2) as the dialysis solution, respectively. SDS-PAGE patterns showed PSC-A and PSC-P as type I collagens, as well as acid soluble collagen (ASC). When incubated at 40°C, no degradation was observed for ASC, but PSC-A and PSC-P were degraded into short peptides, showing lower stability than ASC. The results indicate that pepsin remaining in the PSCs resulted in their degradation, which was confirmed by the inhibition using pepstatin. This research revealed the behavior of the remaining pepsin in pepsin-solubilized collagens and an approach to the PSC stability improvement was proposed. Chromatography profiles showed that new PSC prepared by the improved method had almost the same stability as ASC.

Isolation and characterisation of acid- and pepsin-soluble collagen from the skin of Cervus korean TEMMINCK var. mantchuricus Swinhoe

2018 ◽  
Vol 58 (3) ◽  
pp. 585 ◽  
Author(s):  
Gaurav Lodhi ◽  
Yon-Suk Kim ◽  
Eun-Kyung Kim ◽  
Jin-Woo Hwang ◽  
Hyung-Sik Won ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Thermal Denaturation ◽  
Peptide Hydrolysis ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Thermal Denaturation Temperature ◽  
Skin Collagen ◽  
Pepsin Soluble Collagen ◽  
Calf Skin

Acid-soluble collagen and pepsin-soluble collagen were extracted from the skin of deer, Cervus korean TEMMINCK var. mantchuricus Swinhoe. The two types of collagen were then characterised using sodium dodecyl sulfate–polyacrylamide gel electrophoresis, amino acid composition analysis, peptide hydrolysis patterns, thermal denaturation temperature, differential scanning calorimetry, Fourier transform infrared spectroscopy, and nuclear magnetic resonance imaging. The yield of pepsin-soluble collagen (9.62%) was greater than that of acid-soluble collagen (2.24%), but both types of collagen showed similar electrophoretic patterns with each other and with calf skin collagen. The peptide hydrolysis pattern results suggested that calf skin collagen and pepsin-soluble collagen from deer skin may be similar in terms of their primary structure. The thermal denaturation temperature of acid-soluble collagen and pepsin-soluble collagen were 36.67°C and 36.44°C, respectively, and their melting temperatures were 110°C and 120°C, respectively, which suggest high thermal stability. Fourier transform infrared showed a triple helical structure and nuclear magnetic resonance confirmed the presence of ‘hydration’ water. These results provide a basis for large-scale production and further application as alternatives to other mammalian collagens.

scholarly journals Pepsin treatment of avian skin collagen. Effects on solubility, subunit composition and aggregation properties

1972 ◽  
Vol 129 (3) ◽  
pp. 677-681 ◽  
Author(s):  
D. W. Bannister ◽  
Anne B. Burns
Keyword(s):  
Acetic Acid ◽  
Subunit Composition ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Aldehyde Content

1. Collagen was extracted from chick skin with dilute acetic acid followed by dilute acetic acid containing pepsin. 2. The solubilized collagens were purified and portions subjected to further digestion by pepsin. 3. This treatment decreased the aldehyde content but contamination by hexosamine was not diminished. 4. Pepsin treatment converted practically all the acid-soluble collagen into monomeric subunits (α-chains), but the pepsinsolubilized material retained a significant amount of higher subunits (β- and γ-chains). 5. Treatment lowered the rate of fibrillogenesis by acid-soluble collagen, but was without effect on pepsin-solubilized collagen.

scholarly journals Isolation and properties of collagen extracted from mixed by-products obtained from different fish species

Biotecnia ◽  
2021 ◽  
Vol 23 (3) ◽  
pp. 109-116
Author(s):  
Celia Olivia García-Sifuentes ◽  
Julio Cesar Zamorano-Apodaca ◽  
Marcel Martinez-Porchas ◽  
Susana Maria Scheuren-Acevedo ◽  
Miguel Angel Mazorra-Manzano
Keyword(s):  
Fish Species ◽  
Type I Collagen ◽  
Helical Structure ◽  
Extraction Process ◽  
Type I ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
By Products

Fish by-products consisting of skin, bones, or scales are collagen sources. Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) mixed by-products derived from different fish species were extracted and evaluated. The properties evaluated for both collagens were chemical composition, amino acid- and SDS-PAGE- protein profiles, Fourier transform infrared spectroscopy (FTIR), denaturation temperature (Tmax), enthalpy (ΔH), and solubility. The ASC and PSC registered a protein content of 48.56 and 38.80 %, respectively. From the total amino acids detected, hydroxyproline accounted for 7 % and 6 % for ASC and PSC, respectively. The electrophoretic profile showed the presence of the type I collagen bands (α1, α2, β, and γ), whereas FTIR spectrum showed the presence of diverse collagen functional groups (Amide A, B, I, II, and III) for both extracted types, and demonstrated that the extraction process did not affect the collagen´s triple-helical structure. The Tmax of ASC and PSC were 38.27 and 38.07° C, respectively, whereas ΔH were 0.64 and 0.33 J g-1. The lowest solubility was registered at pH 5 for ASC and pH 9 for PSC. The caractheristics of the collagen extracted, indicated that a mixture of by-products from different species could be an alternative for their reutilization by the local markets.

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