Superworm-Derived Protein Hydrolysate: Functional Properties and Activity Following Enzymatic Processing

Abstract

The increasing global demand for sustainable protein sources has driven interest in edible insects because of their high nutritional value and low environmental impact of their production. This study aimed to obtain and characterize protein hydrolysates from defatted Zophobas morio (superworm) flour using two enzymes, pepsin (PEP) and Brauzyn (BRA), under controlled temperature and pH conditions. Two treatments were studied: HP, protein hydrolysate obtained from the defatted flour of superworms using the PEP enzyme, and HB, protein hydrolysate obtained from the defatted flour of superworms using the BRA enzyme. The HP treatment was selected because it showed the best results compared to the HB treatment (p < 0.05), with the degree of hydrolysis (20.0% for HP and 1.3% for HB) and yield (59.2% for HP and 16.0% for HB). The physicochemical and technological properties of the treated samples were analyzed using ANOVA (p < 0.05) and Tukey's test, with a 95% confidence interval. The resulting hydrolysate exhibited a high protein content (69.21%) and satisfactory solubility (99.08%), oil absorption (3.23 g 100 g⁻¹), emulsifying capacity (58.67%), and emulsion stability (58.10%). It also exhibited antioxidant activity, with 2.2-Diphenyl-1-picrylhydrazyl (DPPH•) and Ferric Reducing Antioxidant Power (FRAP) values of 40.19 and 74.78 μmol TE g⁻¹. These results demonstrate that enzymatic hydrolysis significantly improves the functional and bioactive properties of Z. morio proteins, making them promising alternatives to conventional protein sources. Additionally, this study underscores the importance of developing insect-based bioprocesses to meet the global demand for sustainable functional ingredients and highlights the potential applications of Z. morio protein hydrolysates in the food and nutraceutical industries.