Characterization and Gel Properties of Gelatin Extracted from Waste Fish Scales

Abstract

The objective of this research is to compare the characteristic of gelatin prepared from waste fish scales. White perch, java barb, red tilapia and nile tilapia scales were cleaned and treated with 1.0 M NaOHfor 2 h at room temperature to remove fat and then treated 0.8 M acetic acid to restructure of fish scales. Gelatin from waste fish scales were exacted using heating the cleaned fish scales in the distilled water at 70 °C for 2 h. Gelatins were characterization by UV-vis spectrometer, viscometer, X-ray diffraction (XRD), fourier transform infrared spectrophotometer (FT-IR) and scanning electron microscopy (SEM). The results shown the amount of gelatin and percent transmittance of light of gelatin from white perch was more than that of other waste fish scales. The viscosities of all gelatins decreased with increasing temperature. The gelatin from java bard was more viscosity than that from other fish scales due to more amounts of aspartic and glutamic acid. The XRD intensity of gelatin from white perch scales and java barb scales had higher than that from other fish scales confirming the higher crystallinity of gelatin. The FT-IR resultsindicated the same function groupsof all gelatins. SEM results revealed the porous structure of all gelatins. The all results concluded that gelatin property of nile tilapia scales had less than that of other fish scales which could be used in different industry.

Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI

“…These results can explain the influence of the addition of the three proteins on the crystallization as they increasingly act as nucleating agents for the CColF films. Furthermore, the degree of crystallinity in the crystal structure of the polymer has been demonstrated as the two main factors on the influence of both content of crystallizable additive and matrix . The result of XRD is corroborating with the observation of SEM findings.…”

“…Furthermore, the degree of crystallinity in the crystal structure of the polymer has been demonstrated as the two main factors on the influence of both content of crystallizable additive and matrix. 25 The result of XRD is corroborating with the observation of SEM findings.…”

“…The film prepared with CColF shows a typical crystalline collagen with peaks located in the regions around 2 θ = 8° and 21° and these characteristic peaks are connected to the triple helix and reconstructed triple‐helix structure which exists in collagen, related to the single left‐hand helix chain and the diameter of the triple‐helix collagen molecule. The triple‐helix is an amino acid, which results in the crystal structure of collagen …”

“…The triple-helix is an amino acid, which results in the crystal structure of collagen. 24,25 J Sci Food Agric 2019; 99: 4942-4951…”

Influence of natamycin loading on the performance of transglutaminase‐induced crosslinked gelatin composite films

“…The film prepared in pure gelatin shows a typical crystalline gelatin structure with peaks located in the regions at approximately 2h = 8°a nd 20°, and these characteristic peaks are attributed to the triple-helix and reconstructed triple-helix structure which exists in gelatin from collagen, related to the single left-handed helix chain and the diameter of the triple-helix collagen molecule (Rivero et al, 2010). In gelatin, the triple-helix is amino acids, which could cause the crystal structure of gelatin (Nuamsrinuan et al, 2015). The crosslinked film has weakened peaks in some regions compared with the pure gelatin film.…”