Collagen of edible jellyfish exumbrella

Nagai, Takeshi; Ogawa, Tomoe; Nakamura, Takashi; Ito, Tetsuhide; Nakagawa, Hisaki; Fujiki, Kazuhiro; Nakao, Minoru; Yano, Tomoki

doi:10.1002/(sici)1097-0010(19990501)79:6<855::aid-jsfa299>3.3.co;2-e

Cited by 39 publications

(72 citation statements)

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“…Collagen was extracted according to the method of Nagai et al (15) with slight modifi cation as described by Barzideh et al (16). All procedures were performed at 4 °C.…”

Section: Isolation Of Collagenmentioning

confidence: 99%

ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

Barzideh¹,

Latif²,

Gan³

et al. 2014

Food. Technol. Biotechnol.

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SummaryCollagen isolated from the ribbon jellyfi sh (Chrysaora sp.) was hydrolysed using three diff erent proteases (i.e. trypsin, alcalase and Protamex) to obtain bioactive peptides. Angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant activities (i.e. ferric reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity) of the peptides were measured and compared, and the eff ect of the duration of hydrolysis on the bioactivity (ACE inhibitory and antioxidant activities) of peptides was also evaluated. FRAP activity was the highest in Protamex-induced (25-27 mM) and trypsin-induced hydrolysates (24-26 mM) at 7 and 9 h, respectively. Conversely, hydrolysates produced by trypsin for 1 and 3 h showed the highest DPPH radical scavenging activities (94 and 92 %, respectively). Trypsin-induced hydrolysates (at 3 h) also showed the highest ACE inhibitory activity (89 %). The peptide sequences with the highest activities were identifi ed using tandem mass spectrometry, and the results show that the hydrolysates had a high content of hydrophobic amino acids as well as unique amino acid sequences, which likely contribute to their biological activities.

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“…Collagen was extracted according to the method of Nagai et al (15) with slight modifi cation as described by Barzideh et al (16). All procedures were performed at 4 °C.…”

Section: Isolation Of Collagenmentioning

confidence: 99%

ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

Barzideh¹,

Latif²,

Gan³

et al. 2014

Food. Technol. Biotechnol.

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“…[9][10][11] Commercial collagen has conventionally been prepared from bovine or pig skin; however, the fear of infectious diseases like bovine spongiform encephalopathy (BSE) has forced us to look for feasible alternatives to mammalian collagen, and fish collagen has emerged as the candidate. [12][13][14][15][16][17][18][19] Yellowfin tuna (Thunnus albacares) is a popular migratory fish, and grows in the area of the ocean between 20 C and 28 C. This tuna fish is widely eaten as a prestigious food in Japan, but its skin, bones, and fins are usually discarded as waste. Those parts of the fish body are composed largely of collagen and constitute a good source for it.…”

mentioning

confidence: 99%

Preparation and Structural Analysis of Actinidain-processed Atelocollagen of Yellowfin Tuna (Thunnus albacares)

Morimoto

Kunii

Hamano

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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“…The yield of pepsin-solubilized collagen from bullfrog muscle (PSC) was 33.2% (on the dry weight basis). This result was low to those for edible jellyfish exumbrella (46.4%) [19], rhizostomous jellyfish mesogloea (35.2%) [20], cuttlefish outer skin (35.0%) [21], and brown backed toadfish skin [22]. This result might suggest that there are some discrepancies in the construction of collagens among different species.…”

Section: Fëçä~íáçå=çñ=`çää~öéå=ñêçã=máééñáëümentioning

confidence: 96%

Isolation and biochemical characterization of collagens from seaweed pipefish, Syngnathus schlegeli

Khan

Qian

Ryu

et al. 2009

Biotechnol Bioproc E

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^Äëíê~Åí= Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from the seaweed pipefish (póåÖJ å~íÜìë=ëÅÜäÉÖÉäá) and partially characterized. The amount of collagens isolated in the subsequent treatments was 5.5% of ASC and 33.2% PSC on the basis of lyophilized pipefish body weight, respectively. According to the electrophoretic pattern and CM-cellulose column chromatogram, the collagens might be classified as type I collagens, containing α1 and α2 chain. The imino acid content of collagen from pipefish was lower than those of mammalian collagens as also were the denaturation temperatures (Td) of collagens were 34.8°C and 35.1°C, respectively. This study shows that there is a possibility to use pipefish collagen as the alternative source of collagen from industrial purposes and subsequently it may evaluate the economical value of the seaweed pipefish. © KSBB hÉóïçêÇëW=Åçää~ÖÉåI=ëÉ~ïÉÉÇ=éáéÉÑáëÜI=áëçä~íáçåI=ÅÜ~ê~ÅíÉêáò~íáçå

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Collagen of edible jellyfish exumbrella

Cited by 39 publications

References 0 publications

ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

Preparation and Structural Analysis of Actinidain-processed Atelocollagen of Yellowfin Tuna (Thunnus albacares)

Isolation and biochemical characterization of collagens from seaweed pipefish, Syngnathus schlegeli

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