Biochemical properties of bone and scale collagens isolated from the subtropical fish black drum (Pogonia cromis) and sheepshead seabream (Archosargus probatocephalus)

Ogawa, Masahiro; Portier, Ralph J.; Moody, Michael W.; Bell, Jon W.; Schexnayder, Mark; Losso, Jack N.

doi:10.1016/j.foodchem.2004.02.006

Cited by 230 publications

(191 citation statements)

References 22 publications

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“…CD spectra represent backbone configuration of protein through absorption regions of peptide linkage. A minor difference was observed in ellipticity between ASC and PSC, suggesting some difference in the secondary conformation of both collagens, more likely due to telopeptide removal in PSC (Ogawa et al, 2004). Moreover, the denatured collagen possessed more distorted spectrum, reflected by the disappearance of positive peak at 221 nm.…”

Section: Spectroscopymentioning

confidence: 92%

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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Section: Spectroscopymentioning

confidence: 92%

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

2017

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“…Tropical fish collagen possesses slightly higher denaturation temperature (27-34°C) than temperate fish collagen (16-20°C) (Ogawa et al, 2004). As the unicorn leatherjacket fish is a tropical fish, collagen derived from its skin, it had an average denaturation temperature of 28°C (Muralidharan, Shakila, Sukumar, & Jeyasekaran, 2013).…”

Section: Hydrolysis Of Fish Skin Collagen By Collagenasementioning

confidence: 99%

Untitled

Kumar¹,

Shakila²,

Jeyasekaran³

2019

Turk. J. Fish. Aquat. Sci.

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In this study, skin of unicorn leatherjacket (Aluterus monoceros) was hydrolyzed using collagenase at three different temperatures viz. 5°C, 25°C and 50°C, to obtain collagen hydrolysates. Collagen peptides of low molecular masses (<3kDa) viz. CP-5, CP-25 and CP-50 were obtained by sequential ultrafiltration with tangential flow filtration (TFF) system. The results indicated that CP-5 exhibited the maximum in vitro anti-cancer, anti-diabetic and wound healing activities than CP-25 and CP-50. In MTT assay, CP-5 inhibited the viability of COLO320 cancer cells upto 49.78% at 1 mg/mL concentration, while the inhibition was only 29.92% by CP-50. Anti-diabetic activity as assessed by α-amylase inhibition was 80.45% by CP-5 at 1 mg/mL concentration, as against 75.81% and 71.17% by CP-25 and CP-50, respectively. Collagen peptides, in general, exhibited very low anti-inflammatory property, which ranged between 3.27% to 4.01%. In vitro wound healing tested by scratch assay showed good migration of 3T3-L1 cells in CP-5 treated than CP-25 and CP-50 at 0.2 mg/mL concentration. The study thus proved that collagen peptides derived from fish skin at low hydrolysis temperatures (50C) exhibited more bio-active activities than those hydrolysed at high temperatures (500C); and shall be effectively utilized in various bio-medical applications.

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“…Kolagen (C102H149N31O38) merupakan protein fibrilar, terdiri dari tiga rantai polipeptida (triple helix) sebagai komponen utama penyusun kulit dan tulang yang mewakili sekitar 25% dari total berat kering mamalia dan sangat dibutuhkan pada industri makanan, kosmetik, biomedis dan farmasi (Ogawa et al, 2004). Menurut Liu et al (2015), produksi kolagen komersial biasanya bersumber dari kulit dan tulang sapi, babi serta unggas.…”

Section: Pendahuluanunclassified

“…Menurut Ogawa et al (2004), keberadaan rantai α menunjukkan bahwa kolagen tersebut merupakan kolagen tipe I. Kolagen tipe I merupakan kolagen bentuk dasar yang dapat ditemukan pada bagian tendon dan jaringan ikat lainnya. Demikian halnya dengan gambaran mikroskopik gelembung renang ikan cunang yang menunjukkan struktur jaringan ikat kolagen dengan dominan warna biru (Gambar 1b).…”

Section: Protein Terlarut Dan Bobotunclassified

THE HISTOLOGICAL, EXTRACTION AND CHARACTERIZATION COLLAGENS YELLOW-PIKE CONGER Muarenesox talabon

Gadi

Trilaksani

Nurhayati

2018

J. Ilmu dan Teknologi Kelautan Tropis

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ABSTRAKLimbah gelembung renang Muarenesox talabon dapat digunakan sebagai bahan baku kolagen yang sangat dibutuhkan pada industri makanan, biomedis, farmaseutikal, dan kosmeseutikal. Tujuan penelitian adalah untuk mengamati histologi dan menentukan karakteristik kimia gelembung renang meliputi proksimat dan asam amino; ekstraksi kolagen larut asam dan menentukan karakteristik kolagen meliputi proksimat, pH, logam berat, mikroba, asam amino, gugus fungsi, bobot molekul, dan stabilitas termal. Morfologi gelembung renang ikan cunang terdiri dari lapisan luar, tengah dan dalam yang mengandung serabut-serabut kolagen; protein 33,67±0,71% bb yang didominasi oleh tiga asam amino yaitu, glisina, prolina, dan alanina. Pra perlakuan dengan NaOH 0,1 Molar selama 8 jam (K1T4) dan ekstraksi asam pada konsentrasi 0,25 Molar selama 72 jam (M1T3) adalah perlakuan terbaik menghasilkan rendemen kolagen 14,51±0,43%; kadar air 12,12±0,04% bb; protein 88,54±0,08% bb; lemak 1,31±0,23% bb; abu 0,17±0,03% bb; tidak terdeteksi logam berat (Pb, Hg, As, Cd); pH 4,31; negatif cemaran E. coli dan Salmonella. Asam amino utama adalah glisina 241,06 mg/g; prolina 88,73 mg/g; dan alanina 86,98 mg/g; spektrum FTIR yang mengungkapkan adanya struktrur triple helix; pola elektroforesis terdiri dari 136 kDa (α1) dan 117 kDa (α2) yang mencirikan kolagen tipe I; serta memiliki Tmax 195,59ºC dan ΔH 7,8113 J/g. Kata kunci: ekstraksi asam, gelembung renang ikan, kolagen, kestabilan termal

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Biochemical properties of bone and scale collagens isolated from the subtropical fish black drum (Pogonia cromis) and sheepshead seabream (Archosargus probatocephalus)

Cited by 230 publications

References 22 publications

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

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

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THE HISTOLOGICAL, EXTRACTION AND CHARACTERIZATION COLLAGENS YELLOW-PIKE CONGER Muarenesox talabon

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