Sequential extraction of gel-forming proteins, collagen and collagen hydrolysate from gutted silver carp (Hypophthalmichthys molitrix), a biorefinery approach

Abdollahi, Mehdi; Rezaei, Masoud; Jafarpour, Ali; Undeland, Ingrid

doi:10.1016/j.foodchem.2017.09.045

Cited by 118 publications

(92 citation statements)

References 37 publications

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“…In the SDS-PAGE system, collagen fibrils were degraded as its intermolecular hydrogen bonds, intramolecular hydrogen bonds and covalent bonds were gradually destroyed [26]. The subunit compositions of A-CF and P-CF from bovine tendon are visualized in the electrophoretogram (Figure 1).…”

Section: Sds-page Patternmentioning

confidence: 99%

Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Liu

Zhang

et al. 2020

Materials

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Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

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Section: Sds-page Patternmentioning

confidence: 99%

Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Liu

Zhang

et al. 2020

Materials

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“…Zhou et al () indicated that the absorbance of chicken feet‐soluble collagen by FT‐IR is amide A in 3,308 cm −1 , amide B in 2,932 cm −1 , amide I in 1629 cm −1 , amide II in 1548 cm −1 , and amide III in 1,242 cm −1 similar with the collagen extracted from yak rumen smooth muscle. Moreover, AbdollahiRezaei, Jafarpour, and Undeland () also reported that collagen from gutted silver carp ( Hypophthalmichthys molitrix ) had the similar absorption peaks of collagen from yak rumen smooth muscle. However, the collagen of yak rumen smooth muscle absorption peaks of amides A, B, I, II, and III have some different with collagen from chicken feet, gutted silver carp, and black carp skin; the results indicated the collagen from yak rumen smooth muscle has its own characteristic.…”

Section: Discussionmentioning

confidence: 91%

“…Collagen has a helical structure composed of three peptide chains, and the types of collagens from different sources are also different (Ficai et al, ; Powell, Hunt, & Dikeman, ). At present, at least 27 collagen types have been identified, and each differs considerably in its molecular structure, amino acid sequence, and function (Abdollahi et al, ; Shoulders & Raines, ). The MS can detect the peptides of different proteins based on scores, the number of peptides sequences, and coverage of protein sequences.…”

Section: Discussionmentioning

confidence: 99%

Extraction and characterization of collagens from yak rumen smooth muscle

2019

Animal Science Journal

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This study reports an effective method using enzymatic methods to extract collagen from yak rumen smooth muscle. The enzymatic extraction methods were optimized by response surface methodology. Additionally, the properties of the extracted collagen were analyzed by Fourier transform infrared (FT‐IR) spectroscopy and mass spectrometry (MS). The results showed that the optimal conditions were as follows: the pepsin addition was 0.95%, the enzymatic hydrolysis time was 21 hr, and the solid‐to‐solvent ratio was 1:11. Under these conditions, the collagen extraction rate could reach 3.62/100 g. The results of FT‐IR revealed that the amide A, amide B, amide I, amide II, and amide III bands of the collagen appeared at 3,293.18, 3,068.18, 1654.94, 1,540.58, and 1,236.58 cm−1, respectively. The MS identified seven types of collagen, which were type I, type III, type IV, type V, type VI, type VIII, and type XII. The results demonstrated that the enzymatic method can extract collagen from yak rumen smooth muscle with a considerably high yield and can preserve the intact structure of the collagen.

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“…Collagen molecules, composed of three α-chains intertwined in the so-called collagen triple-helix, adopt a 3D structure that provides an ideal geometry for inter-chain hydrogen bonding, which stabilizes the triple helices (Nijenhuis, 1997). Collagen is generally extracted with mild acid or alkaline hydrolysis and solubilized without altering its triple helix (Abdollahi et al, 2018;Hernández-Briones et al, 2009;Regenstein and Zhou, 2007). The composition of collagen encompasses all 20 amino acids (Schrieber and Gareis, 2007) and it is the only mammalian protein that contains large amounts of hydroxyproline and hydroxylysine, and it is also high in its content of imino acids (proline and hydroxyproline) (Balian and Bowes, 1977).…”

Section: Collagen and Gelatinmentioning

confidence: 99%

Utilization of marine by-products for the recovery of value-added products

Shahidi¹,

Varatharajan²,

Han³

et al. 2019

Journal of Food Bioactives

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The world fisheries resources have exceeded 160 million tons in recent years. However, every year a considerable amount of total catch is discarded as by-catch or as processing leftovers, and that includes trimmings, fins, frames, heads, skin, viscera and among others. In addition, a large quantity of processing by-products is accumulated as shells of crustaceans and shellfish from marine bioprocessing plants. Recognition of the limited marine resources and the increasing environmental pollution has emphasized the need for better utilization of the by-products. Marine by-products contain valuable protein and lipid fractions, minerals, enzymes as well as many other components. The major fraction of by-products are used for feed production-in making fish meal/oil, but this has low profitability. However, there are many ways in which the fish and shellfish waste could be better utilized, including the production of novel food ingredients, nutraceuticals, pharmaceuticals, biomedical materials, fine chemicals, and other value-added products. In recent times, much research is conducted in order to explore the possible uses of different by-products. This contribution primarily covers the characteristics and utilization of the main ingredients such as protein, lipid, chitin and its derivatives, enzymes, carotenoids, and minerals originating from marine by-products.

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Sequential extraction of gel-forming proteins, collagen and collagen hydrolysate from gutted silver carp (Hypophthalmichthys molitrix), a biorefinery approach

Cited by 118 publications

References 37 publications

Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Extraction and characterization of collagens from yak rumen smooth muscle

Utilization of marine by-products for the recovery of value-added products

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