Fish scale collagen. Preparation and partial characterization

Nagai, Takeshi; Izumi, Masami; Ishii, Masahide

doi:10.1111/j.1365-2621.2004.00777.x

Cited by 129 publications

(110 citation statements)

References 16 publications

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“…The amino acid contents of both fish types vary among the three tissues selected (skin, scales, and fins). Similar results have been reported by Nagai et al (2004), who observed that the collagen amino acid contents correlated with the water temperature of their normal habitat. Methionine and cysteine were negligible in the C. catla and C. mrigala skin, scales, and fins from the three weight groups.…”

Section: Amino Acid Analysissupporting

confidence: 79%

“…2). Nagai and Suzuki (2000); Nagai et al (2004); Rodziewicz-Motowidlo et al (2008) and Nagai et al (2008) reported that collagen is the primary protein in preparing 75 % of the protein contents. The remaining 25 % is composed of smaller fragments that appear under the α bands corresponding to the molecular weight ranging from 73 to 155 kDa, including the probable elastin bands (8 %) and the remaining unidentified proteins and peptides (17 %).…”

Section: Resultsmentioning

confidence: 99%

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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

116

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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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Section: Amino Acid Analysissupporting

confidence: 79%

Section: Resultsmentioning

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

116

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“…The amino acid composition of gelatin from tilapia scales is also determined and given in Table 1. The glycine content was most abundant, which was similar to that of gelatins from sardine, red sea bream and Japanese sea bass scales (Nagai et al 2004). The imino acid (proline and hydroxyproline) content of tilapia scale gelatin was 212 residues per 1,000 amino acid residues, which was similar to that of warm-water fish gelatins (Nagai et al 2004;Avena-Bustillos et al 2006) and higher than that of tilapia skin gelatin (Weng et al 2013).…”

Section: Resultsmentioning

confidence: 59%

Water resistance and mechanical property improvement of tilapia (Tilapia zillii) scale gelatin films by dehydrated thermal treatment

Weng

2014

J Food Sci Technol

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The effect of dehydrated thermal treatment on the tilapia scale gelatin films was investigated to improve their water resistance and mechanical properties. The gelatin extracted from tilapia scales was mainly composed of β-chain, α-chain and their degraded products with imino acid content of 21.2 %. When the films prepared from tilapia scale gelatin were heated at 80°C, no significant changes in the properties of films were observed. As heating temperature was increased to 100 or 120°C, the tensile strength of films was increased gradually with increasing thermal treatment time, while film solubility and protein solubility were decreased. Based on the SDS-PAGE analysis and the protein solubility of the gelatin films in various protein denaturant solutions, it was found that the cross-linking in the gelatin film network between β-chain and α-chain could be induced by heating at 120°C. It was revealed that the main interactions involved in the gelatin film formation were changed from ionic bonds and hydrogen bonds to hydrophobic interactions and covalent bonds, leading to improve water resistance properties of films.

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“…The marine collagens showed high solubility at acidic pH (4 to 5) and the solubility markedly decreased in the presence of NaCl up to 2%. Type I collagen has also been extracted from skin, bone, fins, and scales of fresh water and marine fishes, chicken skin and different marine animals such as squid, octopus, jellyfish, starfish and fish (Swatschek et al, 2002;Sadowska et al, 2003;Nagai et al, 2004;Falguni et al, 2010). Collagens from these sources were evaluated for their potential applications as alternatives to mammalian collagen.…”

Section: Solubility Of Collagensmentioning

confidence: 99%

Comparison of the properties of collagen extracted from dried jellyfish and dried squid

Jankangram¹,

Chooluck²,

Pomthong³

2016

Afr. J. Biotechnol.

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With increased recent interest in the utilization of industrial by-products, finding different sources, optimizing extracting conditions and characterization of collagen extracts have recently become important research topics. This study addresses the isolation of acid-soluble and pepsin-soluble forms of collagen from dried jellyfish and squid, and their partial characterization. The properties of these proteins have been studied and a comparison made of the protein patterns of collagen extracted from marine organisms with those from other organisms, to determine which collagen subtypes are present, and in what proportions. Pepsin-soluble collagen (PSC) from dried jellyfish and dried squid contained a collagen form classified as type I, of molecular composition comparable with that of collagen type I from rat tail. Peptide maps of collagens digested by achromopeptidase were slightly different, indicating some differences in amino acid sequence or conformation. The collagen showed high solubility at acidic pH (4-5) but its solubility markedly decreased in the presence of sodium chloride (NaCl) up to 2%. Collagen type I from dried jellyfish and dried squid could be a useful alternative to mammalian collagen, with potential use in the biomedical, pharmaceutical and nutraceuticals industries.

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Fish scale collagen. Preparation and partial characterization

Cited by 129 publications

References 16 publications

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

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

Water resistance and mechanical property improvement of tilapia (Tilapia zillii) scale gelatin films by dehydrated thermal treatment

Comparison of the properties of collagen extracted from dried jellyfish and dried squid

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