ResearchArticle PredictionandEvaluationofBioactivePropertiesofCowpea Protein Hydrolysates MuneMuneMartinAlain Faculty of Science, University of Maroua, P.O. Box 814, Maroua, Cameroon Correspondence should be addressed to Mune Mune Martin Alain; alainmune@gmail.com Received 24 November 2022; Revised 13 January 2023; Accepted 27 January 2023; Published 13 February 2023 Academic Editor: Muhammad Sajid Arshad Copyright © 2023 Mune Mune Martin Alain. Tis is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Cowpea protein hydrolysates were prepared using thermolysin, alcalase, and trypsin and analysed for bioactive properties, and then, the release of bioactive peptides was investigated insilico. It was found that the degree of hydrolysis reached 48% after 24 h hydrolysis with alcalase. Te hydrolysate prepared using alcalase showed higher ACE inhibitory (62%) and DPPH scavenging activity (19%). SDS-PAGE analysis revealed that vignin was the major protein in cowpea protein isolate. Insilico analysis indicated the presence of potential bioactive peptides with potent bioactivity in the primary structure of proteins. Te 3D structure of proteins was built, upon which bioactive peptides were mapped using their location in the primary structure. Te secondary structure and solvent accessible surface around each bioactive peptide were then calculated. On this basis, the higher degree of hydrolysis and bioactive properties of cowpea protein hydrolysate prepared by alcalase were explained, and structural factors infuencing the release of bioactive peptides were investigated. 1.Introduction Cowpea (Vigna unguiculata (L.) Walp) is a valuable crop widely cultivated in the world, and increasingly in Africa, due to its important nutritional properties and the partic- ularity to resist to heat and drought. Production and con- sumption of cowpea are far beyond that of common dry beans in Africa, where cowpea is the second most important legume after groundnut (Arachis hypogea) [1, 2]. Cowpea seeds are rich in protein (22–30%, dwb) with all essential amino acids and low in fat content although they contain poly-unsaturated fatty acids [3]. Teir proteins present high functional properties, particularly solubility and emulsion capacity. Cowpea seeds also contain essential minerals and vitamins. Cowpea protein is then an important ingredient in food and non-food formulations. Recently, cowpea con- sumption has been linked to the prevention of cardiovas- cular disease (CVD), type-2 diabetes (T2D), and cancer. Tese properties were related to bioactive peptides encrypted in the protein sequences and polyphenols [4, 5]. Bioactive peptides are usually released through the action of enzymes or microorganisms or by the gastrointestinal proteases. Efcient release of these bioactive peptides from cowpea protein could enhance the application of cowpea hydrolysates in food formulations and then contribute to reducing the high prevalence of CVD and T2D in developing countries. Generally, enzymatic hydrolysis of plant proteins pro- duced hydrolysates which exhibited a high potential for inhibiting key enzymes for CVD and T2D, as well as cancer cell proliferation and antioxidant properties [6]. Segura Campos et al. [7] hydrolyzed cowpea protein extract with alcalase, favourzyme, and pepsin-pancreatin and obtained degrees of hydrolysis ranging from 38 to 59%, IC 50 for angiotensin-converting enzyme inhibitory activity ranging from 1.4 mg/mL to 2.6 mg/mL, and hydrolysates also showed signifcant antioxidant activity. Lower values for ACE inhibitory activity were obtained by Rudolph et al. [8] when hydrolyzing plant proteins with chymotrypsin and thermolysin. Furthermore, our previous study on the hy- drolysis of Bambara bean protein with alcalase, thermolysin, and trypsin produced hydrolysates with high ACE inhibitory Hindawi Journal of Food Biochemistry Volume 2023, Article ID 9095113, 12 pages https://doi.org/10.1155/2023/9095113