Rapid isolation of high purity pepsin-soluble type I collagen from scales of red drum fish (Sciaenops ocellatus)

Si-jin, Chen; Chen, Hui; Xie, Quanning; Hong, Bihong; Chen, Junde; Fang, Hua; Bai, Kaikai; He, Jianlin; Yi, Ruizao; Wu, Hao

doi:10.1016/j.foodhyd.2015.07.027

Cited by 88 publications

(72 citation statements)

References 47 publications

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“…Extraction and purification of PSC was performed according to the description of Chen et al (2016) with slight modifications. PSC was extracted from the above operation steps with acetic acid solution (0.5 M, 1,20, w v − 1 ) containing pepsin (2000 U g − 1 substrate) for 24 h. Subsequently, the supernatant of samples was collected by centrifugation.…”

Section: Extraction and Purification Of Collagenmentioning

confidence: 99%

Effect of ultrasound power on extraction kinetic model, and physicochemical and structural characteristics of collagen from chicken lung

Zou

Zhang

et al. 2020

Food Prod Process and Nutr

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The effects of ultrasound power on extraction kinetic model, and physicochemical and structural characteristics of collagen from chicken lung were studied. Ultrasound power caused a significant increase in extraction rate and equilibrium concentration, with the maximum extraction yield (31.25%) at 150 W. The experimental data were consistent with the predicted ones in this empirical equation, in which the percentage error differences was 0.026-4.159%. Besides, ultrasound treatment did not affect their triplehelical structure. The thermal stability of pepsin-soluble collagen by ultrasound pre-treatment (UPSC) was higher, due to the higher imino acid content (20.76%). UPSC also exhibited better solubility and fibril forming capacity. Overall, the kinetic model of UPSC from chicken lung could serve the purpose of obtaining collagen, which displayed a potential alternative source to mammal collagens for application in food, biomaterials and biomedical fields.

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Section: Extraction and Purification Of Collagenmentioning

confidence: 99%

Effect of ultrasound power on extraction kinetic model, and physicochemical and structural characteristics of collagen from chicken lung

Zou

Zhang

et al. 2020

Food Prod Process and Nutr

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“…For the collagen production, the bone and skin from porcine and bovine generally are the main source due to Muslim, Jew, and Hindu cannot consume those collagens. The choice of source for collagen production, especially from fish processing by-products, including bone, skin, and scale, have gained attention as noticed by the increasing of research related to collagen extraction from fish by-products a decade ago (Chen et al, 2016;Chuaychan et al, 2015;Duan et al, 2009;Kittiphattanabawon et al, 2015;Liu et al, 2012;Matmaroh et al, 2011;Minh Thuy et al, 2014;Savedboworn et al, 2017;Sinthusamran et al, 2013). Most of the fish collagens were extracted from the skin because of the high yield obtained.…”

Section: Characteristics Of Acid and Pepsin Solubilized Collagens Fromentioning

confidence: 99%

Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale

et al. 2019

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In Thailand, the production of tilapia is about 140,000 tons, which is the sixth tilapia production in the world. From the processing, the scale was generated as waste. To produce a value-added product, the production of collagen from tilapia scale could be an alternative. Generally, collagen from fish scale possesses a less fishy odor and flavor than that from fish bone and skin. From the results, the fish scale is an interesting alternative source for collagen extraction. The objectives of this study were to extract collagen from Nile tilapia (Oreochromis niloticus) scale from the production of frozen tilapia fillet as well as to study its properties. Extraction of acid (ASC) and pepsin soluble collagens (PSC) from Nile tilapia scale, as well as the determination of their yield, amino acid compositions, SDS-PAGE patterns, FTIR spectra, thermal denaturation temperature (Tmax) and zeta potential, was conducted. ASC and PSC had a yield of 0.77 and 0.71% based on dry basis), respectively. The major amino acid found in both collagens was glycine (322-332 residues/1000 residues). Also, they had a high amount of imino acid (199-205 residues/1000 residues). Based on SDS-PAGE pattern, both collagens were classified as type I collagen ((α1)2α2-heterotrimer). The similar FTIR spectra of both collagens were found. Their amide peaks had no shift in wavenumber. ASC and PSC had Tmax of 36.15 and 34.70 °C, respectively. From zeta potential analysis, ASC and PSC had the zero of net chart at pH 5.09 and 5.84, respectively. Based on the characteristics of the collagen, the scale could be an alternative source for collagen production, however their yield should be improved to serve as a potential source for further application.

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“…Other sources such as marine collagen are arising as a relevant alternative to their mammalian counterparts. Several organisms such as marine sponges [5,6], jellyfish [7,8], squid [9,10], and fishes [11][12][13][14] have been exploited for the extraction of marine collagen. About 75% of a fish's…”

Section: Introductionmentioning

confidence: 99%

Cosmetic Potential of Marine Fish Skin Collagen

et al. 2017

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Many cosmetic formulations have collagen as a major component because of its significant benefits as a natural humectant and moisturizer. This industry is constantly looking for innovative, sustainable, and truly efficacious products, so marine collagen based formulations are arising as promising alternatives. A solid description and characterization of this protein is fundamental to guarantee the highest quality of each batch. In the present study, we present an extensive characterization of marine-derived collagen extracted from salmon and codfish skins, targeting its inclusion as component in cosmetic formulations. Chemical and physical characterizations were performed using several techniques such as sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier Transformation Infrared (FTIR) spectroscopy rheology, circular dichroism, X-ray diffraction, humidity uptake, and a biological assessment of the extracts regarding their irritant potential. The results showed an isolation of type I collagen with high purity but with some structural and chemical differences between sources. Collagen demonstrated a good capacity to retain water, thus being suitable for dermal applications as a moisturizer. A topical exposure of collagen in a human reconstructed dermis, as well as the analysis of molecular markers for irritation and inflammation, exhibited no irritant potential. Thus, the isolation of collagen from fish skins for inclusion in dermocosmetic applications may constitute a sustainable and low-cost platform for the biotechnological valorization of fish by-products.

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Rapid isolation of high purity pepsin-soluble type I collagen from scales of red drum fish (Sciaenops ocellatus)

Cited by 88 publications

References 47 publications

Effect of ultrasound power on extraction kinetic model, and physicochemical and structural characteristics of collagen from chicken lung

Effect of ultrasound power on extraction kinetic model, and physicochemical and structural characteristics of collagen from chicken lung

Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale

Cosmetic Potential of Marine Fish Skin Collagen

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