Extraction and characterization of new biocompatible gelatin from camel slaughter by-products: biochemical, sensory, interfacial, and textural properties

The study investigated the impact of pepsin pretreatment and extraction temperature (70 and 90 °C) on the biochemical, interfacial, and textural properties of gelatin extracted from camel skin. The highest concentration of low molecular mass peptides (< 5 kDa) was observed in gelatins extracted with pepsin pretreatment. Moreover, the total free amino acids content showed a direct correlation with the concentration of low molecular mass peptides, ranging from 6 to 15 mg/g of gelatin. Proline was identified as the predominant free amino acid (from 2.39 to 4.92 mg/g) in gelatin samples, with levels significantly increased after pepsin treatment. Regarding textural properties, gel hardness was found to be the highest in gelatin extracted at 70 °C (380.12 g), while it was observed that the combination of pepsin pretreatment with higher temperatures led to decrease the gel strength (301.89 g). However, despite this lower gel strength, this gelatin showed the highest emulsifying activity index (34.76–37.82 m²/g). These findings highlighted the importance of pepsin pretreatment and extraction temperature in modulating the biochemical and textural characteristics of camel skin gelatin, thereby providing insights for optimizing gelatin extraction processes as a function of the target application.