Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Yan, Mingyan; Li, Bafang; Zhao, Xue; Qin, Song

doi:10.1016/j.foodhyd.2012.02.014

Cited by 77 publications

(39 citation statements)

References 33 publications

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“…Collagen was initially dissolved in 0.5 m acetic acid solution with the concentration of 2 mg mL −1 , and then, the solution was centrifuged to collect the supernatant for studying the self‐assembly property. Previous study suggested that an increased collagen concentration caused an increase in the rate of reconstruction (Noitup et al ., ; Yan et al ., ), and it was observed that not all collagen could be dissolved in acetic acid solution in the experiment; therefore, the solubility of collagen was assessed. The dissolution ratios of collagen by different methods are shown in Table .…”

Section: Resultsmentioning

confidence: 99%

“…All procedures were performed as previously described (Yan et al ., ). Type I collagen (200 mg) was dissolved in 0.5 m acetic acid (100 mL) by stirring for 48 h at 4 °C.…”

Section: Methodsmentioning

confidence: 97%

“…Self‐assembly of soluble collagen into fibrils in vitro was observed more than 50 years ago (Li et al ., ). Not only the fibrillogenesis of collagen from bovine dermal (Li et al ., ; He et al ., ), bovine achilles tendon (Chung et al ., ) and rat tail (Harris et al ., ) was investigated, but also some studies majored in the self‐assembly of collagen extracted from marine animals, such as bester sturgeon (Zhang et al ., ), silver‐line grunt skin (Aukkanit & Garnjanagoonchorn, ) and walleye pollock skin (Yan et al ., ). Fessler said that the amino acid composition of the collagen alpha chains varied with species and tissues (Fessler, ).…”

Section: Introductionmentioning

confidence: 97%

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Study on the self‐assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods

Yan

Qin

2015

Int J of Food Sci Tech

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SummaryType I collagen was prepared from tilapia (Oreochromis niloticus) skin by acetic acid and pepsin process at 4°C, respectively (ASC and PSC), and hot-water method separately at 25, 35 and 45°C (C-25, C-35 and C-45). Their structure and self-assembly property were discussed. SDS-PAGE patterns suggested that pepsin hydrolysis and the 35 and 45°C extraction produced collagen with much reduced proportions of a-and bchains. Fourier transform infrared spectroscopy spectra revealed that pepsin hydrolysis did not change the conformation of collagen, but higher extraction temperature did. Self-assembly curves and atomic force microscopy (AFM) observations showed that only ASC, PSC and C-25 could self-assemble into fibrils with D-periodicity, but the reconstruction rate of C-25 was lower. Besides, PSC had relatively higher resolution ratio compared with others. Overall, pepsin-extracted collagen displayed higher solubility and better fibrilforming capacity, having the potential of applying in biomaterials and food-packaging materials.

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Section: Resultsmentioning

confidence: 99%

“…All procedures were performed as previously described (Yan et al ., ). Type I collagen (200 mg) was dissolved in 0.5 m acetic acid (100 mL) by stirring for 48 h at 4 °C.…”

Section: Methodsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 97%

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Study on the self‐assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods

Yan

Qin

2015

Int J of Food Sci Tech

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“…This fibrous protein can be obtained from different sources and it is the main component of skins, bones and tendons (Ahmad & Benjakul, 2010;Delvin, 2004;Huang, Shiau, Chen, & Huang, 2011;Jongjareonrak, Benjakul, Visessanguan, Nagai, & Tanaka, 2005;Yan, Li, Zhao, & Qin, 2012). At least 29 different types of collagen with a singular amino acid sequence, structure and function have been identified (Li et al, 2013;Liu, Liang, Regenstein, & Zhou, 2012).…”

Section: Introductionmentioning

confidence: 99%

Extraction and characterization of collagen from rabbit skin: partial characterization

Martínez-Ortiz

Hernández-Fuentes

Pimentel-González

et al. 2014

CyTA - Journal of Food

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(2015) Extraction and characterization of collagen from rabbit skin: partial characterization, CyTAJournal of Food, 13:2, 253-258, DOI: 10.1080/19476337.2014 To link to this article: https://doi.org/10. 1080/19476337.2014 Extraction and characterization of collagen were carried out in rabbit skins as a new alternative for collagen type I. Acetic acid and pepsin were for the extraction of soluble and insoluble collagen, respectively. The enzymatic treatment yielded higher amount of collagen (71%). The average pH value was 6.3, no matter what the method of extraction was. Denaturation temperature of collagen was found at 36°C approximately in two different techniques: Rheometer and Differential Scanning Calorimetry (DSC). Despite the amount of collagen in solution was low, its viscosity was high because of the hydrodynamic behaviour of collagen molecules. Sodium dodecyl sulphate polyacrylamide gel electrophoresis results showed three different bands that reflected two alpha-chains and one beta-chain with molecular weights of 102, 118 and 220 kDa, respectively. Determination of hydroxyproline gave evidence that the extracted material was collagen. It was concluded that rabbit skin could be an alternative source for the extraction of collagen.Keywords: collagen; rabbit skin; extraction; thermal analysis Se realizó la extracción y caracterización de colágeno en pieles de conejo como una nueva alternativa para colágeno tipo I. Se usaron ácido acético y pepsina para la extracción de colágeno soluble e insoluble respectivamente. El tratamiento enzimático fue el que rindió alta cantidad de colágeno (71%). El pH promedio fue de 6,3 sin importar cuál fue el método de extracción. La temperatura de desnaturalización del colágeno se encontró a 36°C aproximadamente mediante dos diferentes técnicas: Reometría y DSC. A pesar de que la cantidad de colágeno en la solución fue bajo, su viscosidad fue alta debido a el comportamiento hidrodinámico de las moléculas. Los resultados de SDS-PAGE mostraron tres diferentes bandas en las que se reflejaron dos cadenas alfa y una cadena beta con pesos moleculares de 102, 118 and 220 kDa respectivamente. La determinación del contenido de hidroxiprolina dio evidencia de que el material extraído fue colágeno. Se concluyó que la piel de conejo podría ser una alternativa de materia prima para la extracción de colágeno.

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“…In the past few decades, elucidating the mechanism of collagen assembly and controlling its aggregating architectures have achieved considerable attentions as its assembled states have profound influence on the physicochemical properties of the biomaterials (1)(2)(3)(4)(5)(6)(7)(8). In vivo, the collagen molecules aggregate into hierarchical architectures at nano-, micro-and macro-scales, which are pivotal in serving as docking sites for some growth factors as well as maintaining the bio-functions of connective tissues (9)(10)(11).…”

Section: Introductionmentioning

confidence: 99%

A Reconsideration of the Effect of Procyanidin on the Assembly of Collagen Type I

Wang

Jin

2018

Preprint

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In order to elucidating the exact effect mechanism of polyphenols on the assembly of collagen, the assembled architectures of collagen treated with different amounts of procyanidin (PA) were investigated in details. The assembled morphologies of collagen were greatly influenced by the content of PA according to atomic force microcopy (AFM) images.When the content of PA was more than 20% (w/w), the fibrillar morphologies were substituted by globular aggregates, which were driven by the intense hydrogen bonding action originating from PA. While the formation of the non-fibrous aggregates was due to the coiling and entangling of flexible collagen molecules rather than their gelatinization based on the appearance of typical adsorption peaks at 222nm and 197nm on circular dichroism (CD) spectra. After being crosslinked by glutaraldehyde (GA), not only the diameters but also the lengths of fibrils increased. Unfortunately, the fibrillogenesis was still inhibited when the collagen suffered from 20% PA firstly and then 4% GA. Conversely, the fibrous morphologies of the fibrils stabilized by 4% GA and then underwent 20% PA maintained well, in spite of accompanying with grievous intertwining. This difference was derived from the change of flexibilities of collagen before and after being crosslinked by GA. Additionally, the differential scanning calorimeter (DSC) analysis confirmed the PA had no positive effect on the improvement of thermal stability of hydrous collagen, whereas the denaturation temperature of hydrated collagen stabilized by 4% GA increased from 40 °C to 80 °C.

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Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Cited by 77 publications

References 33 publications

Study on the self‐assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods

Study on the self‐assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods

Extraction and characterization of collagen from rabbit skin: partial characterization

A Reconsideration of the Effect of Procyanidin on the Assembly of Collagen Type I

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