Molecular, Structural, and Rheological Characterization of Camel Skin Gelatin Extracted Using Different Pretreatment Conditions (original) (raw)
Related papers
Structural characteristics of camel-bone gelatin by demineralization and extraction
International Journal of Food Properties, 2016
Camel bone was demineralized through HCl acidulation process at different concentrations (0.0%, 1.5%, 3.0%, and 6.0%) over 1-5 days. The level of demineralization was acid concentration and soaking time dependent. Highest demineralization (62.0%) was recorded in bone sample treated with 6.0% dilute acid for 5 days. Energy dispersive X-ray spectroscopy (EDX) elemental analysis revealed reduction in Ca and increase in N and H, while O remains unaffected. Particulate characteristics by scanning electron microscope showed an increased surface roughness of bone after demineralization. Fourier transform infrared (FT-IR) analysis of ossein depicted the presence of functional group similar to that of bone protein (collagen). Statistical optimization by central composite design (CCD) revealed a significant quadratic model for optimum values of extraction temperature, pH, and extraction time. The highest gelatin yield from camel bone was 23.66% at optimum extraction condition (71.87°C, pH 5.26, and 2.58 h) and the bloom was 205.74 g. Camel bone is suitable for production of gelatin with good potentials in food and nonfood applications.
EXTRACTION AND CHARACTERIZATION OF GELATIN: A FUNCTIONAL BIOPOLYMER
International Journal of Pharmacy and Pharmaceutical Sciences, 2017
Objective: Gelatin is widely used biopolymer in various industries due to its excellent biocompatibility, biodegradability properties. In the present study, gelatin was extracted from fish wastes, as an alternative source. Methods: This biopolymer was extracted from the scales of freshwater fish, Labeo rohita. After extraction, the proximate analysis and physicochemical analysis of the fish scale gelatin were carried out. This functional polymer was also characterized using different analytical methods, such as UV-vis spectroscopy, scanning electron microscopy (SEM), and X-ray diffraction (XRD) for the evaluation of crystalline and surface morphology, and fourier transform infrared spectroscopy (FTIR) for structural determination. Results: The scales of L. rohita yield 24% (dry weight basis) of gelatin, indicating this fish species as potential source of gelatin. The proximate analysis determined was low moisture content (4.2%), ash (1.4%) and high protein (90%) content. The result of the study confirms the effectiveness of extraction method used. Conclusion: The fish scales of L. rohita are found to be a sustainable and renewable source of gelatin with desirable functionalities and it is the best alternative for mammalian gelatin in food and other industries.
2021
To clarify the feasibility of replacing commercial gelatin with chicken skin gelatin, we investigated the gel properties and nanostructures of chicken skin gelatin (CG), commercial porcine skin gelatin (PG), and tilapia skin gelatin (FG). Compared with PG and FG, CG exhibited the better gel strength, hardness, chewiness, melting point, gelling temperature, and thermostability. The different physicochemical properties of CG might be caused by its higher imino acid content (25.43 residues/100 total residues), which make it more liable to form intramolecular H-bonds (lower amplitude of amide A wave number). In addition, atomic force microscopy (AFM) result was shown that CG contained larger spherical aggregates (483 nm) than PG and FG (334 and 224 nm, respectively), and the lack of chain and ring-like structure promoted the formation of a dense rigid gel. These results revealed that the intramolecular H-bond and the aggregation behavior are the fundamental explanations for the different gel properties of gelatins from three sources. Practical Application: This research provides guidance for the application of chicken skin gelatin as a replacer for commercial gelatin. And the results provide a theoretical basis for the modification of chicken skin gelatin.
Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin
Food Hydrocolloids, 2013
The aims of this study were to report for the first time, the extraction and physico-chemical properties of chicken skin gelatin compared to bovine gelatin. Extracted chicken skin gelatin 6.67% (w/v) had a higher bloom value (355 AE 1.48 g) than bovine gelatin (259 AE 0.71 g). The dynamic viscoelastic profile of chicken gelatin exhibited higher viscous and elastic modulus values compared to bovine gelatin for a range of concentrations and frequencies. Thermal properties studied by differential scanning calorimetry (DSC) showed that the melting temperature of 6.67%, chicken skin gelatin was significantly greater (p < 0.05) than that of bovine gelatin, indicating lower stability of bovine gelatin compared to chicken skin gelatin. Results obtained in this study showed that Gly (33.70%), Pro (13.42%), H.Pro (12.13%) and Ala (10.08%) were the most dominant amino acids in chicken skin gelatin which contributed to the higher gel strength and stability. Raman spectra of chicken skin and bovine gelatin were similar and displayed typical protein spectra. Chicken gelatin showed strong hydrogen bonding compared to bovine gelatin as the tyrosine doublet ratio (I 855 /I 830 ) of chicken gelatin was significantly lower than that of bovine gelatin. Significantly, the alpha helix and b-sheet type structures were higher for chicken skin gelatin compared with bovine gelatin. The average molecular weight of chicken gelatin was 285,000 Da. These findings, obtained for the first time for chicken skin gelatin, show that it has high potential for application as an alternative to commercial gelatin.
Chemical and functional properties of bovine and porcine skin gelatin
International Food Research Journal
The ability to compare bovine and porcine skin gelatin based on their amino acid composition, polypeptides pattern, bloom strength, turbidity and foaming properties were investigated. Amino acid composition of both gelatin showed that the content of glycine, proline and arginine in porcine gelatin were higher than bovine gelatin. However, the polypeptides pattern between both gelatin is closely similar. The bloom strength of porcine gelatin was higher than bovine gelatin from pH 3 to pH 10. Both gelatin possessed highest bloom strength at pH 9. The lowest bloom strength of bovine gelatin was at pH 3 while porcine gelatin at pH 5. The highest turbidity of bovine gelatin obtained at pH 7 while porcine gelatin at pH 9. Foam expansion and foam stability of bovine gelatin were higher than porcine gelatin at all concentrations.
Gelatin extraction yield increased with the increase of acetic acid concentration and temperature. Gelatin extracted from shaari skin using 0.1 N acid solutions and temperatures of 323 and 353 K gave highest protein content comparable to that of commercial bovine and porcine gelatins. In general, gelatin extracted from shaari gelatin showed lower onset of glass transition temperature than mammalian gelatins. For shaari skin gelatin, the onset of glass transition temperature decreased with the increase of extraction temperature up to 323 K and then remained nearly constant. The decrease in glass transition was more pronounced for gelatin extracted at 0.01 N compared to the 0.1 and 1.0 N samples. Unfolding temperature decreased exponentially with the increase of extraction temperature. The unfolding temperature shifted to lower temperature, and the decrease was more pronounced in the case of higher (1.0 N) concentrated samples. The extraction concentration and temperature did not show significant effect on the onset solids-melting temperature. Keywords Fish skin gelatin Á Glass transition Á Solidsmelting Á Shaari Á Amino acid List of symbols T gi Onset temperature of glass transition (K) T gp Peak temperature of glass transition (K) T ge End temperature of glass transition (K) T mi Onset temperature of solids-melting (K) T mm Maximum slope temperature of solids-melting (K) T mp Peak temperature of solids-melting (K) T me End temperature of solids-melting (K) T ui Onset unfolding temperature (K) T um Maximum slope of unfolding temperature (K) T up Peak of unfolding temperature (K) X w Moisture content (g/100 g sample) DC p Change of specific heat (J/kg K) DH u Enthalpy change for unfolding (kJ/kg) DH m Enthalpy change for solids-melting (kJ/kg)
Optimization Of Curing And Extraction Time On Production Of Base Gelatin From Bovine Skin Material
2018
To explore gelatin materials used in any purposes for food additive with Indonesian local sources, gelatin in this study was prepared from bovine skin via base method. The effects of curing (10, 30, and 50 days) and extraction time (4, 5, and 6 hours) on yield percentage, pH, viscosity, organoleptic properties (odor, taste, and color), water contents, as well as the ash content of its material were invested. The results showed that the bovine gelatin with longer curing time and longer extraction time exhibited biomaterial with higher yield percentage, higher pH, lower viscosity, darker color, higher water and ash content. No obvious differences were detected from physical shape, odor and texture of bovine material that prepared with longer stirring time and longer extraction time. To sum up, the bovine skin gelatin which produced with 30 days curing time and 5 hours extraction time showed better water content, viscosity, and organoleptic properties compared to the others. Despite pr...
Impact of Curing and Extraction Time on Yield and Quality of Base Gelatin from Goat Skin
IOP Conference Series: Earth and Environmental Science
The impact of curing and extraction time on yield and quality (water and ash content, gel and organolaptic properties) of the base gelatin from goat skin was investigated. The yield, water and ash content also gel strength of goat gelatin (GG) increased with increasing curing (10-50 days) and extraction time (4-5 hours). Higher water and ash content was observed with 30 days curing and 5 hours of extraction compared with the others conditions. In line with these, the higher gel strength was observed under the same conditions. The ash content of GG with 30 days curing and 5 hours extraction time increased by 0,26% compared to the GG with lower curing and extraction time. The Gel strength of all gelatins increased as the curing and extraction time of gelatin increased. To know the effect of curing and extraction time on gelatin organoleptic properties, ie color, has been analysed using Visible UV spectrophotometer. The results showed that there has been a detectable increase in color ...
Frontiers in Nutrition
The poultry processing industrial wastes are rich sources of gelatin protein, which can be utilized for various industrial sectors. The present investigation was conducted to evaluate the effect of freeze-drying (FD) and hot air drying (HAD) on the physicochemical, structural, thermal, and functional characteristics of chicken feet gelatin. The yield (%) of extracted FD and HAD gelatin was 14.7 and 14.5%, respectively. The gelatin samples showed lower percent transmittance in the UV region. The FTIR bands were at 3,410–3,448 cm−1, 1,635 cm−1, 1,527–334 cm−1, and 1,242–871 cm−1 representing amide-A, amide-I, amide-II, and amide-III bands, respectively. The water activity of HAD was higher (0.43) than in FD (0.21) samples and pH were 5.23 and 5.14 for HAD and FD samples, respectively. The flow index (n) of 6.67% gelatin solutions was 0.104 and 0.418 with consistency coefficient (k) of 37.94 and 31.68 for HAD and FD samples, respectively. The HAD sample shows higher gel strength (276 g...
Physicochemical Properties of Gelatin Extracted from Buffalo Hide Pretreated with Different Acids
The acid pretreatment of collagen molecules disrupts their crosslinks and assists in the release of acid-soluble proteins, fats, and other components. Generally, to achieve optimum extraction efficiency, strong acids may be used at a lower acid concentration compared to weak acids. This study aimed to determine the yield and physicochemical properties of gelatins extracted from buffalo hides pretreated with different acids. Hides were extracted with hydrochloric, citric, and acetic acids at concentrations of 0.3, 0.6, 0.9, 1.2, and 1.5 M. A completely rando-mized design and the least significant difference test were used in the experimental design, and all measurements were performed in triplicate. The highest yield (29.17%) was obtained from pretreatment with 0.9 M HCl. The gel strength did not differ significantly (p>0.05) according to acid type (280.26-259.62 g Bloom), and the highest viscosity was obtained from the 0.6 M citric acid pretreatment. All the gelatins contained α-and β-chain components and several degraded peptides (24-66 kDa). The color and Fourier-transform infrared spectrum of the gelatin extracted using 0.9 M HCl were similar to those of commercial bovine skin gela-tin. In general, the physicochemical properties of the gelatin complied with the industry standard set by the Gelatin Manufacturers Institute of America, revealing that buffalo hide could serve as a potential alternative source of gelatin.