Optimum conditions for extracting collagen from the tunica albuginea of immunologically castrated pig testes and the functional properties of the isolated collagen

Simões, Gislaine Silveira; Silveira, Expedito Tadeu Facco; Oliveira, Simone Raymundo de; Poleze, Evandro; Allison, Jim; Ida, Elza Iouko; Shimokomaki, Massami

doi:10.1016/j.meatsci.2013.10.038

Cited by 14 publications

(11 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The chicken keel bone cartilage was subjected to extraction with organic acid (the acid used was the one that resulted in the highest collagen yield in the pretreatment step) and the pepsin enzyme according to methodology adapted from Simões et al (2014). The pre-shredded cartilage was immersed in an acetic acid solution (0.5 mol/L) at a 1:10 (w/v) ratio for 24 hours at 18 °C.…”

Section: Soluble Collagen Pepsin Extractionmentioning

confidence: 99%

“…The amino acid profile further indicated that 72.97% of the amino acids found were hydrophobic, and 26.8% were hydrophilic. Simões et al (2014) reported that collagen was a molecule consisting of approximately 60% hydrophobic amino acids and 40% hydrophilic amino acids; the hydrophobic amino acids are responsible for providing suitable emulsification properties in emulsified products.…”

Section: Partial Chemical Composition and Amino Acid Content Of The Cmentioning

confidence: 99%

“…The composition of collagen from the cartilage of aquatic and terrestrial animals has been the object of study by researchers (Gómez-Guillén et al, 2011;Simões et al, 2014;Araújo et al, 2018) to identify bioactive compounds derived from cartilage with potential beneficial health properties. However, only one study published by Losso & Dgawa (2014) has focused on the extraction of collagen from chicken keel bone cartilage and its thermal stability.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

et al. 2020

View full text Add to dashboard Cite

The aim of this study was to investigate the effect of acid pretreatment, temperature and enzyme concentration on the acid-enzymatic extraction of soluble collagen from chicken keel bone cartilage. A chemical composition analysis and protein profile characterization of this slaughter by-product were also conducted. The cartilages were extracted with 0.5 mol/L of acetic, lactic and citric acids for 24, 48 and 72 hours. Subsequently, optimization with a 2 2 factorial design was performed with three replications at the central point for a total of 7 experiments; the analyzed response was the collagen content of the obtained isolates. The cartilage under study has a high protein content (90.27% dry basis) consisting of approximately 35.7% collagen and is a source of essential and predominantly hydrophobic amino acids. Pretreatment with acetic acid for 24 hours led to greater extraction potential and consequently, a better collagen yield (30.12%). The electrophoretic profile of the obtained collagens revealed the existence of an α1 chain, indicating that this collagen was type OO. Statistical analysis demonstrated that the acid-enzymatic procedure favored a temperature of 30 °C.

show abstract

Section: Soluble Collagen Pepsin Extractionmentioning

confidence: 99%

Section: Partial Chemical Composition and Amino Acid Content Of The Cmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

et al. 2020

View full text Add to dashboard Cite

show abstract

“…In order to isolate soluble collagen from bovine tendon, we adapted a protocol for collagen extraction from tunica albuginea [7]. This adapted protocol (Fig.…”

Section: A Collagen Isolationmentioning

confidence: 99%

Printing Collagen 3D Structures

2015

View full text Add to dashboard Cite

Abstract-Collagen is a biomaterial with an excellent biocompatibility due to its biodegradability and weak antigenicity. Its main applications in tissue engineering field are in burns -to accelerate wound healing-and drug delivery. Collagen gels and solutions are widely used for building scaffolds or threedimensional cultures, some of them constructed by threedimensional bioprinting. This work presents an adaptation of a protocol in order to isolate collagen from bovine tendon and also the development of a three-dimensional bioprinter. The preliminary results we preset are 3D structures constructed by the developed bioprinter, using the collagen obtained from bovine tendon, after application of the proposed protocol. These results are promising as they show the capability of the presented protocol to obtain collagen from bovine tendon and the potential of the bioprinting technique for building biocompatible three-dimensional structures designed by Computer Aided Design (CAD) or replicating anatomical structures from standard medical imagining studies. Further studies are needed in order to assess the mechanical and biochemical properties of the printed structures.

show abstract

“…For the extraction of collagen, acid and enzymatic hydrolysis methods are the most used, with the extraction experiments with acetic acid and pepsin being the most efficient. Pepsin is necessary to hydrolyze protein in cross-linking sites because the collagen triple helix structure protects of the enzymatic action (Simões et al, 2014). Enzyme activity can be increased at low pH and temperature close to the human body, but at low temperature it is possible to obtain native collagen (Lin & Liu, 2006b).…”

Section: Introductionmentioning

confidence: 99%

Optimal conditions for obtaining collagen from chicken feet and its characterization

et al. 2018

View full text Add to dashboard Cite

The objective of this study was to extract collagen from chicken feet, determining optimal extraction conditions according to acetic acid concentration, pepsin content and time of enzymatic hydrolysis. A factorial design 2 3 was used, with three replications at the central point, totaling 11 experiments. The response variable studied was the collagen content of the isolate obtained. In addition to the optimization, the characterization of the isolates with higher and lower collagen content, in relation to the amino acid profile, electrophoretic profile, peptide hydrophobicity and functional properties, such as water solubility, water retention capacity and emulsifying activity, were carried out. The proposed model was statistically significant, with conditions of higher collagen content of 0.3 mol/L of acetic acid, 0.2% of pepsin and 12 hours of hydrolysis. The collagen isolate under these conditions showed higher iminoacids content, higher sum of peptide areas, higher solubility in water and water retention at 60 °C. The treatment with lower collagen content showed high emulsifying activity. The collagen isolate of the chicken feet presented characteristics makes it suitable for application in the food industry.Practical Application: Collagen extraction allows the chicken feet to be recovered with high biological value for industry.

show abstract

Optimum conditions for extracting collagen from the tunica albuginea of immunologically castrated pig testes and the functional properties of the isolated collagen

Cited by 14 publications

References 37 publications

Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

Printing Collagen 3D Structures

Optimal conditions for obtaining collagen from chicken feet and its characterization

Contact Info

Product

Resources

About