Effect of heat treatment on the enzymatic stability of grass carp skin collagen and its ability to form fibrils <i>in vitro</i>

Yang, Huan; Wang, Haibo; Yan, Zhao; Wang, Haiyin; Zhang, Hanjun

doi:10.1002/jsfa.6724

Cited by 42 publications

(26 citation statements)

References 32 publications

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“…Fibrillogenesis appears to be an entropy‐driven self‐assembly process that is driven by solvent molecule losses from the surface of proteins, resulting in assemblies with a globular cross‐section, which minimises the surface area/volume ratio of the final assembly. The high NaCl concentration led to the higher ionic strength of solution that may lead to higher fibrillogenesis of the isolated collagen . Similar results were reported in collagen fibril formation from the Bester sturgeon and grass carp .…”

Section: Resultssupporting

confidence: 82%

Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu (Labeo rohita)

et al. 2016

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The rohu swim bladder type I collagen was successfully extracted using an enzymatic method with a yield of 465.2 g kg (dry weight basis) and was characterised as a well maintained triple helical structure. The extracted collagen exhibited a high fibril-forming ability. The results of the present study confirm that utilisation of rohu swim bladder will open up a new avenue for the better disposal of by-products and also help to minimise environmental pollution issues. © 2016 Society of Chemical Industry.

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Section: Resultssupporting

confidence: 82%

Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu (Labeo rohita)

et al. 2016

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“…CD was performed to confirm that the extracts were in the native state, being an effective technique to identify whether the triple helical structure was intact. ASCsb CD spectrum shown in Figure 4 depicts a positive peak at 221 nm (maximum positive cotton effect), characteristic of the presence of triple helix, and a negative peak at 198 nm (maximum negative cotton effect), with a crossover point (zero rotation) at approximately 215 nm, compatible with the observed by other authors [36,37]. However, the spectrum of PSCsb shows only a very small positive peak at 219 nm and a well-defined negative peak at 197 nm, which is indicative of a partially denaturation of the protein and consecutive loss of triple helix, which supports the discussion made above for the thermal characterization of the samples.…”

Section: Chemical Characterization Of Ascsb and Pscsbsupporting

confidence: 87%

Acid and enzymatic extraction of collagen from Atlantic cod (Gadus Morhua) swim bladders envisaging health-related applications

Sousa

Alves

Carvalho

et al. 2019

Journal of Biomaterials Science, Polymer Edition

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Atlantic cod is processed industrially for food purposes, with several by-products being directed to animal feed and other ends. Looking particularly into swim bladders, the extraction of collagen can be a valuable strategy for by-product valorization, explored in the present work for the first time. Collagen was extracted using acetic acid (ASCsb) and pepsin (PSCsb) with yields of 5.72% (w/w) and 11.14% (w/w), respectively. SDS-PAGE profile showed that the extracts were compatible with type I collagen. FTIR, CD and XRD results suggest that the PSCsb structure underwent partial denaturation, with microDSC showing a band at 54 C probably corresponding to a melting process, while ASCsb structure remained intact, with preserved triple helix and a denaturation temperature of 29.6 C. Amino acid composition indicates that the total content of proline-like amino acids was 148/1000 residues for ASCsb and 141/1000 residues for PSCsb, with a hydroxylation degree of about 37%. The extracts exhibited a typical shear thinning behavior, interesting property regarding their further processing toward the development of biomaterials. In this regard, assessment of metabolic activity of human fibroblast cells cultured in the presence of collagen extracts with concentrations up to 3 mg/mL revealed the absence of cytotoxic behavior. Collagen extracts obtained from Atlantic cod swim bladders shown attractive properties regarding their use in cosmetic or biomedical applications. ARTICLE HISTORY

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“…CD was performed to assess the structural organization of the proteins in the extracts, as alpha chains, random coils and triple helices are responsible for very distinct and characteristic signals. In particular, a collagen extract in which the protein keeps its native structure, with preserved triple helix, is characterized by a CD spectrum exhibiting a positive peak at 221 nm (maximum positive cotton effect) and a negative peak at 198 nm (maximum negative cotton effect), with a crossover point (zero rotation) at approximately 213 nm [25,27]. The CD spectrum of AWC, illustrated in Fig.…”

Section: Circular Dichroism Analysismentioning

confidence: 99%

Collagen from Atlantic cod (Gadus morhua) skins extracted using CO2 acidified water with potential application in healthcare

et al. 2020

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The extraction of collagen from fish skins is being proposed as strategy for valorization of marine origin by-products, being a sustainable alternative to mammal collagen. The method commonly uses solutions of organic acids, but new methodologies are arising, aiming to improve process yields and/or the properties of the resulting products. In this work, skins removed from salt brine Atlantic cod (Gadus morhua) were used to extract collagen, using water acidified with CO 2 , obtaining an extraction yield of 13.8% (w/w). Acidified water extracted collagen (AWC) presented a total content of proline-like amino acids of 151/1000 residues, with a degree of hydroxylation of 38%, and its SDS-PAGE profile is compatible with type I collagen. Moreover, FTIR, CD and XRD results suggest the presence of preserved triple helix, having a denaturation temperature of 32.3°C as determined by micro-DSC. AWC exhibited a typical shear thinning behavior, interesting regarding their further processing, namely in jelly-like formulations. Additionally, the presence of AWC in MRC-5 human fibroblasts culture did not affect cell viability, demonstrating the non-cytotoxic behavior. Overall, the results support the efficiency of the proposed approach for collagen extraction and further enable the design of methodologies to address AWC use in biomedical or cosmetic context.

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Effect of heat treatment on the enzymatic stability of grass carp skin collagen and its ability to form fibrils in vitro

Abstract: The onset endothermic temperature (To ) rather than the denaturation temperature (Td ) is the threshold temperature for configurational stability of GCS collagen in acidic solution, and the biological properties would obviously change if the collagen was heat treated at this temperature.

Cited by 42 publications

References 32 publications

Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu (Labeo rohita)

Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu (Labeo rohita)

Acid and enzymatic extraction of collagen from Atlantic cod (Gadus Morhua) swim bladders envisaging health-related applications

Collagen from Atlantic cod (Gadus morhua) skins extracted using CO2 acidified water with potential application in healthcare

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