Collagen from common minke whale (Balaenoptera acutorostrata) unesu

Nagai, Takeshi; Suzuki, Nobutaka; Nagashima, Toshio

doi:10.1016/j.foodchem.2008.03.087

Cited by 121 publications

(105 citation statements)

References 28 publications

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“…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). Wang et al (2014) suggested that the difference in thermal stability of collagens from Amur sturgeon skin may be due to the level of hydration and the number and nature of covalent cross-linkages.…”

Section: Maximum Absorbancecontrasting

confidence: 73%

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: 73%

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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“…The high imino acid content, especially the hydroxyproline content, is extremely important because it affects the functional properties of collagen (Gómez-Guillén et al, 2002), suggesting that the giant red sea cucumber collagen hydrolysates may have wider applications in food industry. Giant red sea cucumber collagen hydrolysates also displayed a similar amino acid composition to that of common whale pepsin-solubilized collagen (Nagai et al, 2008).…”

Section: Amino Acid Composition Of Hydrolysatesmentioning

confidence: 78%

Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates

Liu

Su²,

Zeng³

2011

J. Ocean Univ. China

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Giant red sea cucumber (Parastichopus californicus) is an under-utilized species due to its high tendency to autolysis. The aim of this study was to evaluate the functional properties of collagen hydrolysates from this species. The degree of hydrolysis (DH), amino acid composition, SDS-PAGE, emulsion activity index (EAI), emulsion stability index (ESI), foam expansion (FE), and foam stability (FS) of hydrolysates were investigated. The effects of pH on the EAI, ESI FE and FS of hydrolysates were also investigated. The results indicated that the β and α 1 chains of the collagen were effectively hydrolyzed by trypsin at 50℃ with an Enzyme/Substrate (E/S) ration of 1:20 (w:w). The DH of collagen was up to 17.3% after 3 h hydrolysis with trypsin. The hydrolysates had a molecular weight distribution of 1.1−17 kDa, and were abundant in glycine (Gly), proline (Pro), glutamic acid (Glu), alanine (Ala) and hydroxyproline (Hyp) residues. The hydrolysates were fractionated into three fractions (< 3 kDa, 3−10 kDa, and > 10 kDa), and the fraction of 3−10 kDa exhibited a higher EAI value than the fraction of > 10 kDa (P<0.05). The fraction of > 10 kDa had higher FE and FS values than other fractions (P<0.05). The pH had an important effect on the EAI, ESI, FE and FS. All the fractions showed undesirable emulsion and forming properties at pH 4.0. Under pH 7.0 and pH 10.0, the 3−10 kDa fraction showed higher EAI value and the fraction of > 10 kDa showed higher FE value, respectively. They are hoped to be utilized as functional ingredients in food and nutraceutical industries.

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“…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%

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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Collagen from common minke whale (Balaenoptera acutorostrata) unesu

Cited by 121 publications

References 28 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)

Amino acid composition and functional properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates

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

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