Extraction and characterization of collagen from sheep slaughter by-products

Vidal, Alessandra Roseline; Duarte, Letícia Pereira; Schmidt, Michele M.; Cansian, Rogério Luís; Fernandes, Ilizandra Aparecida; Mello, Renius; Demiate, Ivo Mottin; Dornelles, Rosa Cristina Prestes

doi:10.1016/j.wasman.2019.12.004

Cited by 51 publications

(34 citation statements)

References 53 publications

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“…Thus, the pepsin-aided method resulted in lower yields of type I collagen fibrils. Additionally, the yield of A-CF was higher than that of collagen by enzyme extraction reported in the literatures [15,23]. It further indicated that enzymatic hydrolysis could decrease the yield of both collagen and collagen fibrils.…”

Section: Amino Acid Componentsmentioning

confidence: 63%

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: Amino Acid Componentsmentioning

confidence: 63%

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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“…In this work, collagen was obtained from the trimmings and the splitting-derived by-products [5]. Regarding collagen extraction, it is worth noting that there are several methods reported, which include the pretreatment of raw materials with chemicals, such as sodium hydroxide, butyl alcohol, and acids, or enzymes, such as pepsin and trypsin [30]. In contrast, only sodium hydroxide and mechanical pretreatments were used in this work, reducing the use of chemicals and bringing environmental and economic benefits, since lower amounts of resources (materials, energy, time) were employed in comparison to those works that use acid and enzymatic treatments [7,8].…”

Section: Environmental Assessment Of Collagen Scaffoldsmentioning

confidence: 99%

A Green Approach towards Native Collagen Scaffolds: Environmental and Physicochemical Assessment

et al. 2020

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Native collagen scaffolds were prepared in this work, in which both materials and environmental approaches were considered with the aim of providing a global strategy towards more sustainable biomaterials. From the environmental perspective, it is worth mentioning that acid and enzymatic treatments have been avoided to extract collagen, allowing the reduction in the use of resources, in terms of chemicals, energy, and time, and leading to a low environmental load of this step in all the impact categories under analysis. With the incorporation of chitosan into the scaffold-forming formulations, physical interactions occurred between collagen and chitosan, but the native collagen structure was preserved, as observed by Fourier transform infrared (FTIR) and X-ray diffraction (XRD) analyses. The incorporation of chitosan also led to more homogenous porous microstructures, with higher elastic moduli and compression resistance for both dry and hydrated scaffolds. Furthermore, hydrated scaffolds preserved their size and shape after some compression cycles.

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“…The longer incubation time will produce the maximal hydrolysis process that eventually will produce higher yields (Noorzai et al, 2020). The skin of sheep has a collagen yield of 8.88% (Vidal et al, 2019b) and the skin of the rabbit calf has a collagen yield of 19.5% (Martinez-ortiz et al, 2015). The rapid hydrolysis rate of collagen tends to increase the number of collagen molecules produced that will be converted and will eventually increase the yield value (Muyonga et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…The extracted collagen was characterized for pH and molecular weight characteristics, following the methodology of Alfaro et al (2013) and Vidal et al (2019b). The pH of collagen was measured by weighing one gram of sample then dissolved into 100 mL of distilled water.…”

Section: Characterization Of Collagen Extracted From the Skin Of Kacang Goatmentioning

confidence: 99%

Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme

Hakim

Pratiwi

Jamhari

et al. 2021

Trop. Anim. Sci. J.

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The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE). This research was conducted in three replications, with the measured parameters include ACE inhibitory potential and collagen hydrolysate fractionation. The results showed that collagen extraction of Kacang goat skin by chymotrypsin hydrolysis yielded 9.74% (dry matter, v/v) collagen, with pH at 6.6. The extracted collagen contained α1, α2, and β collagen chains with molecular weights of 151 kDa, 141 kDa, and 240 kDa, respectively. Furthermore, the collagen hydrolysis produced protein peptides confirmed at molecular weights of 43 to 107 kDa. The hydrolysate fractionation at molecular weights of <3 kDa, 3-5 kDa, and >5 kDa showed proteins concentrations of 2.33 mg/mL, 3.81 mg/mL, and 3.93 mg/mL, respectively. The hydrolysate fractionation with molecular weight <3 kDa showed to have ACE inhibition activity with the IC50 value of 0.47 mg/mL. The study concluded that collagen hydrolysate extracted from the skin of Kacang goat had a promising potential as a source of antihypertensive agent.

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Extraction and characterization of collagen from sheep slaughter by-products

Cited by 51 publications

References 53 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

A Green Approach towards Native Collagen Scaffolds: Environmental and Physicochemical Assessment

Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme

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