Waste valorization by production of antioxidant protein hydrolysates derived from industrial grape pomace: optimization bioprocess and characterization of antioxidant and structural properties
摘要
Industrial grape pomace underwent an initial defatting process, followed by isolating its protein content. Subsequently, the protein was hydrolyzed using an alcalase enzyme, focusing on varying the contact time (1, 2, and 3 h) and enzyme concentration (1, 2, and 3% W/W). The analyses aimed to optimize the degree of hydrolysis, antioxidant activity, L* and hue, yielding optimal results of 23.09%, 55.99%, 17.56, and 34.40, respectively. Following the optimization, the structural characteristics of the refined sample were examined through various analytical methods such as DSC, FT-IR and XRD. Additionally, the molecular weight and amino acid profile of the optimized sample were assessed. The structural characteristics revealed the presence of both crystalline and amorphous forms. Glu and Leu emerged as the most abundant amino acids, comprising over 20.91% and 10.18% of the total, respectively. The hydrolyzed products also exhibited substantial levels of Ala (9.30%), Asp (8.01%), Phe (6.81%), Lys (6.65%), Arg (5.29%), Val (5.23%) and Ile (5.23%). In contrast, the minor amino acids included Asparagine (Asn), Glutamine (Glu) and Ornitine (Orn). Overally, 56.33% of optimized sample whole peptide molecular weight was less than 1 kDa and 90% of optimized whole sample had the molecular weight less than 10 kDa.