Effect of Ultrasound Pre-Treatment on Extraction and Characterization of Collagen from Bactrian Camel Skin

Abstract

The objective of this study was to evaluate the effect of ultrasound pre-treatment on the characterization from Bactrian camel skin. It was possible to produce and characterize collagen extracted from Bactrian camel skin. The results showed that the yield of collagen was higher in ultrasound pre-treatment (UPSC) (41.99%) than the pepsin-soluble collagen extraction (PSC) (26.08%). All extracts were identified as type I collagens using sodium dodecyl sulfate polyacrylamide gel electrophoresis and retained their helical structure, as confirmed through Fourier transform infrared spectroscopy. The scanning electron microscopy analysis of UPSC revealed that some physical changes were caused by sonication. UPSC had smaller particle size than PSC. The viscosity of UPSC always plays a leading role in the range of 0–10 Hz. However, the contribution of elasticity to the solution system of PSC increased in the range of 1–10 Hz. Moreover, ultrasound-treated collagen had superior solubility property at pH 1–4 and at <3% (w/v) NaCl than non-ultrasound treated collagen. Therefore, the utilization of ultrasound for the extraction of pepsin soluble collagen is a good alternative technology to expand the application at industrial level.

Proteomic Identification and Characterization of Collagen from Bactrian Camel (Camelus bactrianus) Hoof

“…In this experiment, the collagen yield of CHC was 35.77 ± 2.06%. This is similar to the results of collagen extraction from Bactrian camel skin [16].…”

“…After 24 h of placement, the difference in humectancy between CHC (52.06 ± 1.55%) and glycerol (59.45 ± 2.21%) was small and continued for a more extended time, up to 48 h. The change in their humectancy was not significant. This is The change in the humectancy of CHC was slightly more significant than that of glycerol but lower than that of fish scale collagen and camel skin collagen [16,39]. The humectancy of CHC and glycerol steadily decreased with time (Figure 5a).…”

“…At 48 h of placement, it reached 8.57 ± 0.13%, higher than snakehead skin collagen [32]. This indicates that the number and type of hydrophilic groups exposed by CHC molecules are higher than those of soft-shelled turtle calipash and camel skin [13,16].…”

“…At 48 h of placement, it reached 8.57 ± 0.13%, higher than snakehead skin collagen [32]. This indicates that the number and type of hydrophilic groups exposed by CHC molecules are higher than those of soft-shelled turtle calipash and camel skin [13,16]. because collagen contains an abundance of hydrophilic amino acids, like glycine, hydroxyproline, and hydroxylysine, that prevent water loss [40].…”

“…This decreases the potential on the surface of the emulsion droplets, which lowers the repellent force barrier of the emulsion system and makes it easier for the droplets to aggregate, which reduces the stability and emulsification of collagen [3,38]. The change in the humectancy of CHC was slightly more significant than that of glycerol but lower than that of fish scale collagen and camel skin collagen [16,39]. The humectancy of CHC and glycerol steadily decreased with time (Figure 5a).…”