Characteristics and Functional Properties of collagen extracted from Nile tilapia (Oreochromis niloticus) skin

Abdel-Aal, H.A.; Mohamed, H. M. A.; Saleh, Safaa F.; Koriem, Reem

doi:10.21608/jmr.2020.37541.1034

Cited by 3 publications

(1 citation statement)

References 44 publications

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“…Meanwhile, for the OAC test, ASBS and CSBS were higher compared to the LSBS sample, with a significant difference ( p < 0.05). The WACs and OACs of acid-solubilized barracuda skin collagens had greater values than those observed in glutelin [ 56 ], but our current study had lower WAC and OAC values in comparison with other fish collagens, e.g., red stingray ( D. akaje ) skin [ 20 ] and Nile tilapia ( O. niloticus ) skin [ 57 ]. In general, OAC is closely associated with non-polar amino acid groups, while WAC is related to hydrophilic groups.…”

Section: Resultscontrasting

confidence: 56%

Type I Collagen from the Skin of Barracuda (Sphyraena sp.) Prepared with Different Organic Acids: Biochemical, Microstructural and Functional Properties

Matarsim

Jaziri

Shapawi

et al. 2023

JFB

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This study was carried out to compare the extractability and characteristics of barracuda (Sphyraena sp.) skin collagen using various organic acids. Acetic-solubilized collagen (ASBS), lactic-solubilized collagen (LSBS) and citric-solubilized collagen (CSBS) yielded 6.77 g/100 g, 10.06 g/100 g and 8.35 g/100 g, respectively, and those yields were significantly different (p < 0.05). All acid-solubilized collagens were considered as type I because of their two alpha chains (α1 and α2) detected in acrylamide gel after electrophoresis. Ultraviolet–visible (UV–vis) analysis confirmed that ASBS, LSBS and CSBS had similar absorption peaks (230.5 nm) and the results were in accordance with other fish collagens. Under infrared (IR) and X-ray diffraction (XRD) analysis, the triple helical structure of type I collagens extracted from barracuda skin was maintained. From a thermostability study, all type I collagens showed a higher maximum transition temperature (Tmax = 40.16 to 41.29 °C) compared to other fish skin collagens. In addition, the functional properties of the extracted collagens revealed the ASBS had higher water and oil absorption capacities than the CSBS and LSBS samples. The highest level of the emulsion ability index (EAI) (>200 m2/g) was detected under acidic conditions (pH 4), while lower EAIs were recorded under the alkaline (pH 10) and neutral treatments (pH 7). All type I collagens had a higher relative solubility (>60%) at a low pH test but the solubility level sharply decreased at a neutral pH. In addition to this, a lower concentration of NaCl (0–20 g/L) showed the higher percentage of solubility (>60%) while adding over 30 g/L of NaCl decreased solubility (>40%). From a microstructural test, all type I samples had an irregular and dense flake structure with random coiled filaments. Overall, collagen extracted from the barracuda skin may be applied as an alternative collagen from an industry perspective.

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Section: Resultscontrasting

confidence: 56%

Type I Collagen from the Skin of Barracuda (Sphyraena sp.) Prepared with Different Organic Acids: Biochemical, Microstructural and Functional Properties

Matarsim

Jaziri

Shapawi

et al. 2023

JFB

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A review on the processing technique, physicochemical, and bioactive properties of marine collagen

Shaik,

Rahman,

Yusri

et al. 2024

Journal of Food Science

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Collagens are conventionally derived from bovine and porcine sources. However, these sources were commonly associated with infectious diseases such as bovine spongiform encephalopathy, foot and mouth disease, autoimmune and allergic reactions, and religious constraints. The significant amount of collagen available in marine species, especially fish skins, scales, fins, and bones, shows that marine species can be a potential alternative source to mammalian collagen. Therefore, this review aims to give a clearer outlook on the processing techniques of marine collagen and its physicochemical and bioactive properties as a potential alternative to mammalian collagen. The two most suitable extraction methods for marine collagen are pepsin‐soluble extraction and ultrasound‐assisted extraction. Additionally, marine collagen's physicochemical and bioactive properties, such as antioxidants, wound healing, tissue engineering, and cosmetic biomaterial have been thoroughly discussed in this review.Practical ApplicationCollagen extracted from marine sources showed its potential in physicochemical and bioactive properties, including antioxidants and wound‐healing capabilities, as an alternative to mammalian collagen. The significant amount of collagen found in marine species, particularly in fish skins, scales, bones, and sea cucumbers, suggests that marine sources could be a viable alternative to land mammal collagen due to their abundance and accessibility. The ultrasound‐assisted extraction technique has improved the extracted marine collagen's physicochemical and bioactivity properties and quality properties.

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Characterization of biochemical and optical properties of Nile tilapia (Oreochromis niloticus) corneal collagen

Abd-Elrahman,

Omar,

Elnashar

2024

Futur J Pharm Sci

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Background Collagen extracted from fish body parts is a promising biological material. It has an important role in many pharmaceutical, medical applications and tissue engineering such as corneal regeneration and stromal replacement. The present work investigates a new trend to extract collagen from the fish cornea, as a prospected substituent of human corneal collagen by characterizing some biochemical and optical properties of the fish corneal collagen. Results Examination of the corneal tissue of Nile tilapia; Oreochromis niloticus was conducted using electron microscopy, Fourier transform infrared (FTIR) spectroscopy, UV–visible spectrophotometry, optical properties, and thermal properties. The fish were divided into 10 groups each of which consisted of 5 fish. 2 groups of fish were examined for each technique. Results indicated that the corneal layers of O. niloticus are thin at the center and thicker at the periphery with the stroma consisting of a triple helical structure collagen type I. The fish cornea showed very weak transmission at the UV regions (190 nm) and maximum transmission at the visible regions. The values of transmission (T), reflected light (R) and scattered light (S) were 2.685 mw, 100 × 10−3 mw at 45° and 40 × 10−3 mw, respectively. Consequently, the percentage of absorbed light is 21.76%. The denaturation temperature of the fish corneal stroma is 22.27 °C. Conclusions The method for obtaining fish collagen affects the specific properties of collagen and consequently its further uses as a potential biomedical substituent for mammalian collagen. Specification of the fish species and tissue type is crucial in identifying the quality as well as the physical and functional properties of the extracted collagen.

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Characteristics and Functional Properties of collagen extracted from Nile tilapia (Oreochromis niloticus) skin

Cited by 3 publications

References 44 publications

Type I Collagen from the Skin of Barracuda (Sphyraena sp.) Prepared with Different Organic Acids: Biochemical, Microstructural and Functional Properties

Type I Collagen from the Skin of Barracuda (Sphyraena sp.) Prepared with Different Organic Acids: Biochemical, Microstructural and Functional Properties

A review on the processing technique, physicochemical, and bioactive properties of marine collagen

Characterization of biochemical and optical properties of Nile tilapia (Oreochromis niloticus) corneal collagen

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