The structure of the protein is usually enhanced with enzyme and heat treatment. Another way to improve the functional properties of the final product is a covalent protein with polysaccharide during the Maillard reaction. We aimed to investigate the impacts of pepsin enzyme on camel whey protein (CWP). To reach this goal, covalent linkage of 2% (w/v) camel whey protein isolated and 0.5%, 1% and 2% (w/v) Gum Arabic were analysed during wet heat treatment (15 min at 85°C). During the Maillard reaction, the grafting of CWPI to GA was confirmed by Fourier transformation infrared spectra (FT-IR) and UV-vis spectroscopy. The formation of Amadori and browning compounds was then measured. The solubility properties of CWP improved by adding pepsin enzyme (1:100) during 360 min. The solubility of all samples, therefore, were compared to CWPI over the wide range of pH. Grafting of CWPI and GA was then compared with CWPI. Indicated high heat stability, especially at the pH near isoelectric point (pI) when subjected to 95°C for 30 min. The results show that pepsin enzyme, wet heating conditions and GA, significantly boosted the properties of pure CWP. In conclusion, the optimal samples were related to conjugate of CWPI with 0.5% GA.

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