Biochemical properties of acid-soluble collagens extracted from the skins of underutilised fishes

Bae, Inwoo; Osatomi, Kiyoshi; Yoshida, Asami; Osako, Kazufumi; Yamaguchi, Atsuko; Hara, Kenji

doi:10.1016/j.foodchem.2007.10.039

Cited by 182 publications

(124 citation statements)

References 28 publications

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“…The hydroxyproline content was lower than the values of gelatin from shark (10%), tuna (10%) (Shyni et al, 2014) and cobia (9%) (Silva et al, 2014), and higher than those of gelatins from rohu (7%) (Shyni et al, 2014), tilapia (5%), tuna (7%) (Aewrisi et al, 2008), seabass (8%) (Sae-leaw, Benjakul, Nora, & Kideki, 2016) and carp (7%) (Duan et al, 2011). In general, collagen extracted from fish living in cold water has a lower imino acid content than that from fish living in a warm environment (Bae, Osatomi, Yoshida, Osako, Yamaguchi, & Hara, 2008).…”

Section: Estimated Amino Acid Composition Of Gelatinsmentioning

confidence: 97%

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Hue¹,

Hang²,

R.G.³

2017

Turk. J. Fish. Aquat. Sci.

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The main purpose of this study was to extract and characterize gelatin from skins of fishes: European perch (Perca fluviatilis) and Volga pikeperch (Sander volgensis), which were collected from the Volga-Caspian basin in Russia. The gelatins were prepared using an alkaline pretreatment. The gelatin yield was in the range of 10.2-13.8% on a wet weight basis, and the gel strength exceeded 184 and 193 g for samples from European perch and Volga pikeperch skins, respectively. The pH values of gelatins were 5.49 and 5.73, melting points were 24.5 and 25.5 o C and protein content was 88.6 and 91.0%, respectively. Water-holding and fat-binding capacities of gelatins were 227-235 and 439-453%, respectively. The gelatins were composed of α-chains, β-chains, and γ-chains. The apparent valine content of the two gelatins was significantly higher than those of gelatins from other fish species. The total apparent proportions of imino acids were 192 and 203 residues/1000 residues. The gelatins from European perch and Volga pikeperch skins had relatively high gel strengths, melting points, water-holding and fat-binding capacities as compared with those of other types of fish and could be recommended as potential replacements for mammalian gelatin in the food industry.

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Section: Estimated Amino Acid Composition Of Gelatinsmentioning

confidence: 97%

Untitled

Hue¹,

Hang²,

R.G.³

2017

Turk. J. Fish. Aquat. Sci.

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“…Conversely, NaCl at high concentrations led to the drastic decline in solubility of ASC and PSC. The marked decreased in solubility might be caused by 'salting out' effect of collagen (Bae et al, 2008). At high salt concentration, hydrophobic interaction between proteins chains was enhanced.…”

Section: Effect Of Naclmentioning

confidence: 99%

Molecular Characteristics of Acid and Pepsin Soluble Collagens From the Scales of Golden Carp (Probarbus Jullieni)

2017

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Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from the scales of golden carp (Probarbus jullieni). Both ASC and PSC, identified as type I collagen, contained α- and β-chains as the dominant constituents. ASC and PSC had the yields of 0.42 and 1.16 g 100 g‒1 (dry weight basis), respectively. Amino acid composition revealed that glycine constituted 1/3 of total amino acid residues and no cysteine was found. ASC and PSC had imino acid contents of 197 and 202 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) spectra indicated high integrity of the triple helical structure of both collagens. Based on differential scanning calorimetry (DSC), ASC and PSC had Tmax of 37.67 and 37.83 °C, respectively. Both collagens exhibited high solubility in acidic pH range (1‒3) and the decrease in solubility was found in the presence of NaCl at concentrations above 30 g L‒1. The overall results demonstrated that scales of golden carp could serve as another source of collagen.

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“…The differences between the two fish species and three weight groups for amino acid composition of collagen isolated from skin, scales and fins were statistically highly significant (p<0.01), thereby, indicating a qualitative difference in the collagen of cattle cattle and Cirrhinus mrigala (Table 5, 6 and 7). Pyrrolidine rings of proline and hydroxyproline impose restrictions on the conformation of the polypeptide chain and help to strengthen the triple helix (Bae et al 2008). Hydroxylysine of 4-6 residues/1,000 residues was found in both collagens, suggesting the partial cross-linking of collagen via covalent bond (Mechanic et al 1987).…”

Section: Amino Acid Analysismentioning

confidence: 99%

Isolation and characterization of collagen from fish waste material- skin, scales and fins of Catla catla and Cirrhinus mrigala

Mahboob

2014

J Food Sci Technol

122

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The collagen of skin, scales and fins of Catla catla and Cirrhinus mrigala were isolated and characterised. Nine fishes of each fish species of three weight groups were collected from a commercial fish farm. Collagen characterisation using SDS-PAGE revealed the molecular weights (kDa) of the C. catla skin, scales, and fins which ranged from 120 to 210, 70 to 201, and 68 to 137 kDa, respectively. The size of the collagen of C. mrigala skin, scales and fins ranged from 114 to 201, 77 to 210, and 70 to 147 kDa, respectively. Glycine and alanine were the most abundant amino acid, whereas tryptophan was totally absent in all selected tissues. Thus, significant variation exists in type of collagen and amino acid profile within the weight groups of the two fish species. The imino acid (proline and hydroxyproline) contents estimated in C. catla and C. mrigala skin (161-165 and 160-168), scales (155-159 and 152-161) and fins (162-171 and (152-155) residues/1,000 residues, respectively. The proximate analysis was also performed for skin, scales and fins. The maximum protein content of the skin was determined as 26.10 % and 22.90 % in the C. catla and C. mrigala, respectively, from the W 3 weight group. The scales of the W 3 weight group exhibited maximum protein contents of 25.90 and 21.77 % for C. catla and C. mrigala, respectively. The maximum protein contents (19.04 % and 18.12 %) were recorded for C. catla and C. mrigala, respectively in the fins.

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Biochemical properties of acid-soluble collagens extracted from the skins of underutilised fishes

Cited by 182 publications

References 28 publications

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Molecular Characteristics of Acid and Pepsin Soluble Collagens From the Scales of Golden Carp (Probarbus Jullieni)

Isolation and characterization of collagen from fish waste material- skin, scales and fins of Catla catla and Cirrhinus mrigala

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