Northern pike ( Esox lucius ) collagen: Extraction, characterization and potential application

Kozłowska, Justyna; Sionkowska, Alina; Skopińska-Wiśniewska, Joanna; Piechowicz, K.

doi:10.1016/j.ijbiomac.2015.08.002

Cited by 93 publications

(62 citation statements)

References 46 publications

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“…The denaturation temperature (T d ) was obtained by measuring the viscosity using a circumvolving viscometer (MCR101, Anton Parr Ltd., Shanghai, China) (Kozlowska et al, 2015). Fractional viscosity was calculated as (Equation 2):…”

Section: Determination Of Denaturation Temperaturementioning

confidence: 99%

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

2017

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Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin byproducts of paddlefish (ASC-P and PSC-P) and globefish (ASC-G and PSC-G) were purified and characterized. The imino acid contents of ASC-P, PSC-P, 197.9, 186.4 and 189.7 residues/1000 residues, respectively. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) confirmed that all four samples composed of two different α1-and α2-chains with integrated triple-helical structure. Denaturation temperatures of ASC-P, PSC-P, ASC-G and PSC-G were 29.6, 28.2, 27.4 and 26.9 °C, respectively. Based on Transmission electron microscopy (TEM) observation, all four samples could assemble into fibrils in vitro with D-periodicity. However, the fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Scanning electron microscopy (SEM) analysis confirmed well-defined fibril morphologies,the diameter of fibrils from ASC-P and PSC-P was thicker than those of ASC-G and PSC-G after 24 h incubation. These results indicated that paddlefish and globefish skin collagens could be alternatives to terrestrial collagens for applications in food-packaging, nutraceutical and pharmaceutical industries.Keywords: paddlefish; globefish; collagen; physicochemical property; fibril-forming property; fibril morphology.Practical Application: Utilization of paddlefish and globefish skin byproducts by extracting collagen with good physicochemical and fibril-forming properties.

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Section: Determination Of Denaturation Temperaturementioning

confidence: 99%

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

2017

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“…In general, fish collagen has lower thermal stability than mammal collagen, and this characteristic is directly correlated with relative abundances of imino acids in the molecule (Kozlowska, Sionkowska, Skopinska, & Piechowicz, ). Additionally, there is a positive correlation between the amounts of these imino acids in collagen molecules, fish habitat temperature, and collagen denaturation temperature in fishes (Pati, Adhikari, & Dhara, ).…”

Section: Introductionmentioning

confidence: 99%

Biochemical study of type I collagen purified from skin of warm sea teleost Mahi mahi ( Coryphaena hippurus ), with a focus on thermal and physical stability

Akita

Kono²,

Lloyd

et al. 2019

J Food Biochem

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Acid‐ and pepsin‐soluble collagen were purified from the skin of mahi mahi (mmASC and mmPSC). The Pro+Hyp content of the latter (185/1,000 residues) was highest among all marine teleost fishes. Fourier transform infrared spectroscopy and Circular Dichroism (CD) analysis showed the typical structure of type I collagen. The ratio of positive over negative peak intensity calculated from the CD spectrum was approximately 1.19 in mmPSC, which is remarkably high, and indicates the stability of the triple helix. The denaturation temperatures (Td) of mmASC and mmPSC were the highest (29.5 and 28.8°C, respectively) among the marine teleost fishes previously studied. atomic force microscope and scanning electron microscope images showed that even after pretreatment, the fibrils presented their structure and fiber orientation. These results indicate the robustness of both collagens, which can be attributed to the high value of Pro+Hyp stabilizing the helix structure of the collagen molecule. Practical applicationsWhile Mahi mahi is highly valuable for its meat, other parts such as skin is not fully utilized in seafood industry. On the contrary, it has been empirically shown that the skin of Mahi mahi has high thermal stability, thus, the skin has been used for leather products in some areas located in the tropical and subtropical zones. In this study, we focused on collagen a major component in skin and investigated the structure and the biochemical characteristics of it. Some results showed that collagen from skin has high physical stability. The collagen from skin of Mahi mahi will be a new fishery resource which could be used as a material for collagen products.

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“…Collagen for biomedical applications is mainly isolated from animal tissues (bovine or porcine skin and bovine or equine Achilles tendons). Type I collagen has also been extracted from skin, bone, fins, and scales of fresh water and marine fishes . It is worth mentioning that fish scales together with their inorganic component form a perfect composite that have potential for future applications.…”

Section: Collagen As Biomaterialsmentioning

confidence: 99%

The review of versatile application of collagen

Sionkowska

Skrzyński

Śmiechowski

et al. 2016

Polymers for Advanced Techs

147

137

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This review reports recent advances in the versatile application of collagen. Collagen materials have attracted great attention because they exhibit properties required in cosmetic preparations, in the biomedical field, and in the tanning industry leading to leather production. Herein, the structure and application of collagen are discussed in general, and detailed examples are also drawn from scientific literature and practical work. Copyright © 2016 John Wiley & Sons, Ltd.

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Northern pike ( Esox lucius ) collagen: Extraction, characterization and potential application

Cited by 93 publications

References 46 publications

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

Biochemical study of type I collagen purified from skin of warm sea teleost Mahi mahi ( Coryphaena hippurus ), with a focus on thermal and physical stability

The review of versatile application of collagen

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