Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

Rizk, Moustafa A.; Mostafa, Nasser Y.

doi:10.13005/ojc/320336

Cited by 32 publications

(18 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Collagen has been widely used in food, cosmetic, pharmaceutical and biomedical industries. This may be due to its weak antigenicity with excellent biocompatibility/ biodegradability in nature (Rizk and Mostafa, 2016). Since collagen from porcine or bovine sources has the limitation due to religious concern (Kittiphattanabawon et al, 2005), the demand for alternative commercial sources of collagen is increasing.…”

Section: Molecular Characteristics Of Acid and Pepsin Soluble Collagementioning

confidence: 99%

Molecular Characteristics of Acid and Pepsin Soluble Collagens From the Scales of Golden Carp (Probarbus Jullieni)

2017

View full text Add to dashboard Cite

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from the scales of golden carp (Probarbus jullieni). Both ASC and PSC, identified as type I collagen, contained α- and β-chains as the dominant constituents. ASC and PSC had the yields of 0.42 and 1.16 g 100 g‒1 (dry weight basis), respectively. Amino acid composition revealed that glycine constituted 1/3 of total amino acid residues and no cysteine was found. ASC and PSC had imino acid contents of 197 and 202 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) spectra indicated high integrity of the triple helical structure of both collagens. Based on differential scanning calorimetry (DSC), ASC and PSC had Tmax of 37.67 and 37.83 °C, respectively. Both collagens exhibited high solubility in acidic pH range (1‒3) and the decrease in solubility was found in the presence of NaCl at concentrations above 30 g L‒1. The overall results demonstrated that scales of golden carp could serve as another source of collagen.

show abstract

Section: Molecular Characteristics Of Acid and Pepsin Soluble Collagementioning

confidence: 99%

Molecular Characteristics of Acid and Pepsin Soluble Collagens From the Scales of Golden Carp (Probarbus Jullieni)

2017

View full text Add to dashboard Cite

show abstract

“…The presence of hydrogen bonding in amide A group is indicative of the secondary structure of all three proteins. They also showed carbon-hydrogen alkyl bond stretching peaks (νC-H) at around 2950 to 2847 cm −1 and carbon-oxygen stretching peak (νC-O) at 1035 cm −1 [28]. Res-ColBD also showed a peak between 1100 and 800 cm −1 which corresponds to C-H bond and is possibly due to the ColBD presence in resilin nanocomposite.…”

Section: Resultsmentioning

confidence: 95%

Production and Characterization of Recombinant Collagen-Binding Resilin Nanocomposite for Regenerative Medicine Applications

Mikael

Udangawa

Sorci

et al. 2019

Regen. Eng. Transl. Med.

View full text Add to dashboard Cite

Development of mechanically stable and multifunctional biomaterials for sensing, repair, and regeneration applications is of great importance. Herein, we investigate the potential of recombinant resilin-like (Res) nanocomposite elastomer as a template biomaterial for regenerative devices such as adhesive bandages or films, electrospun fibers, screws, sutures, and drug delivery vehicles. Exon I (Rec1) from the native resilin gene of Drosophila (CG15920) was fused with collagen-binding domain (ColBD) from Clostridium histolyticum and expressed in Komagataella pastoris (formerly Pichia pastoris). The 100% binding of Resilin-ColBD (Res-ColBD) to collagen I was shown at a 1:1 ratio by mass. Atomic force microscopy results in force mode show a bimodal profile for the ColBD-binding interactions. Moreover, based on the force-volume map, Res-ColBD adhesion to collagen was statistically significantly higher than resilin without ColBD. Lay Summary Designing advanced biomaterials that will not only withstand the repetitive mechanical loading and flexibility of tissues but also retain biochemical and biophysical interactions remains challenging. The combination of physical, biological, and chemical cues is vital for disease regulation, healing, and ultimately complete regeneration of functional human tissues. Resilin is a super elastic and highly resilient natural protein with good biocompatibility but lacks specific biological and chemical cues. Therefore, resilin decorated with collagen I-binding domain is proposed as a functional nanocomposite template biomaterial. Collagen I is an ideal binding target, as it is the most abundant structural protein found in human body including scars that affect unwanted adhesion. Future Work Musculoskeletal-related injuries and disorders are the second largest cause of disabilities worldwide. Significant pain, neurological discomfort, limited mobility, and substantial financial burden are associated with these disorders. Thus, biocompatible materials comprised of resilin with collagen-binding domain, such as films adhesive bandages (films, fiber matts, or hydrogels), sutures, screws and rods, three-dimensional scaffolds, and delivery vehicles, will be designed and evaluated for multiple musculoskeletal-related regeneration applications.

show abstract

“…In recent decades, inedible animal by-products are utilized to produce fertilizers, minerals, fatty acids, vitamins, protein hydrolysates, and collagen [ 62 ]. Bovine collagen is the primary source for the industrial collagen used in medicine, cosmetics, and other non-biomedical applications [ 63 ]. Sterilized purified collagen from cow skin is used as injectable bovine collagen [ 64 ].…”

Section: Sources Of Collagenmentioning

confidence: 99%

Sea Cucumber Derived Type I Collagen: A Comprehensive Review

2020

View full text Add to dashboard Cite

Collagen is the major fibrillar protein in most living organisms. Among the different types of collagen, type I collagen is the most abundant one in tissues of marine invertebrates. Due to the health-related risk factors and religious constraints, use of mammalian derived collagen has been limited. This triggers the search for alternative sources of collagen for both food and non-food applications. In this regard, numerous studies have been conducted on maximizing the utilization of seafood processing by-products and address the need for collagen. However, less attention has been given to marine invertebrates and their by-products. The present review has focused on identifying sea cucumber as a potential source of collagen and discusses the general scope of collagen extraction, isolation, characterization, and physicochemical properties along with opportunities and challenges for utilizing marine-derived collagen.

show abstract

Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications

Cited by 32 publications

References 31 publications

Molecular Characteristics of Acid and Pepsin Soluble Collagens From the Scales of Golden Carp (Probarbus Jullieni)

Molecular Characteristics of Acid and Pepsin Soluble Collagens From the Scales of Golden Carp (Probarbus Jullieni)

Production and Characterization of Recombinant Collagen-Binding Resilin Nanocomposite for Regenerative Medicine Applications

Sea Cucumber Derived Type I Collagen: A Comprehensive Review

Contact Info

Product

Resources

About