Isolation of collagen from the skins of Baltic cod (Gadus morhua)

Sadowska, Maria; Kołodziejska, Ilona; Niecikowska, Celina

doi:10.1016/s0308-8146(02)00420-x

Cited by 241 publications

(157 citation statements)

References 13 publications

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“…The T d of other fish and calf collagen ranged from 19.4 to 40.8°C (Merly and Smith 2013;Kittiphattanabawon et al 2010;Muyonga et al 2004;Wang et al 2014). In the present study, the Td of collagen was quite higher than those reported for skin collagen of allied teleosts such as cod (15°C) and carp (28°C) (Duan et al 2009;Sadowska et al 2003). However, it was lower than that of collagen from eel fish skin (35.0°C), brownbanded bamboo shark (36.73°C), porcine skin (37°C) and chick sternal cartilage (43.8°C) (Nagai et al 2008;Veeruraj et al 2013;Cao et al 2013;Kittiphattanabawon et al 2010).…”

Section: Maximum Absorbancecontrasting

confidence: 67%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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A low molecular weight type-II collagenous polypeptide (CIIp) from whale shark (WS) cartilage was prepared by thermolysin digestion; and examined for their physico-functional and antioxidant properties. The purified collagen was composed of an identical (α 1 ) 3 chains and was characterized as type-II. After hydrolysis with thermolysin, the α-chain of the WS collagen was degraded into smaller peptides with molecular weight ranging from 70 to 20KDa. CIIp was successfully separated from the hydrolysates with molecular weight of approximately 37 kDa. Amino acid analysis of CII, and CIIp indicated imino acid contents of 155 and 121 amino acid residues per 1000 residues, respectively. Differing Fourier transform infrared (FTIR) spectra of CII and CIIp were observed, which suggested that the hydrolysis process by thermolysin affected the secondary structure and molecular order of collagen, particularly the triple-helical structure. The denaturation temperature of CII (34°C) was higher than that of CIIp. Low content of glycoprotein was observed in CII than CIIp due to removal of some polypeptides by thermolysin digestion. The antioxidant activity against 1,1-diphenyl-2-picrylhydrazyl radicals and the reducing power of CIIp was greater than that of CII. The results proposed that the purified CIIp from WS cartilage with excellent antioxidant activities could be the suitable biomaterial for therapeutic applications.

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Section: Maximum Absorbancecontrasting

confidence: 67%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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“…Pretreatment and extraction of chicken skin and bone could be enhanced by cutting them into small pieces prior to pretreatment. Sadowska et al [20] found that the mincing and homogenization of fish skin had a crucial influence on the yield of collagen. They achieved the largest percentage of collagen extracted (90%) by treating minced homogenized skins rather than using whole skins (20 to 40%).…”

Section: Proximate Analysis Of Chicken Skin and Bone And Theirmentioning

confidence: 99%

Chicken Collagen from Law Market Value By-Products as an Alternate Source

Munasinghe

Schwarz

Nyame

2014

Journal of Food Processing

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There has been much interest in investigating possible means of making collagen from underutilized chicken by-products and it will lead to an alternate source of collagen for use in various industries such as pharmaceuticals, cosmetics, biomedical materials, and the food industry. The objective of this research was to find methods to extract collagen from chicken skins and bones to compare the corresponding yield differences and analyze their properties. Collagen extracted by acetic acid, citric acid, alkali, one-step acetic acid and pepsin, and two-step acetic acid and pepsin extraction procedures was compared. Complete randomized design, Student's t-test, and Tukey's test were used to analyze the samples ( < 0.05). The recovered dry weights for the skin extractions were 6.1, 6.2, 5, 38.7, and 40.4% and those of bone extractions were 4.4, 4.1, 4.1, 19.1, and 20.6%, respectively. Protein, fat, and inorganic material contents of collagen preparations for skin were 62.7%, 1.5%, and 0.7% and for bone were 30.4%, 1.4%, and 0.7%, respectively. This study indicates that chicken by-products have high potential use as an alternate source of collagen.

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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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Isolation of collagen from the skins of Baltic cod (Gadus morhua)

Cited by 241 publications

References 13 publications

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Chicken Collagen from Law Market Value By-Products as an Alternate Source

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

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