Acetic acid-soluble collagen in human scars

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%).

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

Chemical Papers ◽

10.2478/s11696-012-0172-0 ◽

2012 ◽

Vol 66 (7) ◽

Cited By ~ 1

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.

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

Jurnal Pengolahan Hasil Perikanan Indonesia ◽

10.17844/jphpi.v19i1.11699 ◽

2016 ◽

Vol 19 (1) ◽

pp. 79 ◽

Cited By ~ 4

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

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

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

Biochemical Journal ◽

10.1042/bj1290677 ◽

1972 ◽

Vol 129 (3) ◽

pp. 677-681 ◽

Cited By ~ 21

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.

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