Influence of Degree of Hydrolysis on the Functional Properties of Cowpea Protein Hydrolysates

Abstract

The effects of limited enzymatic hydrolysis with pepsin on the functional properties and molecular characteristics of cowpea protein concentrate (CPC) were investigated. Hydrolysates were prepared at degrees of hydrolysis (DH) 5-30%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis demonstrated that globulin was the major protein component of CPC, and enzymatic breakdown of polypeptides was selective. As a result, significant changes in the functional properties of hydrolysates were noticed as compared to the protein concentrate. Then, cowpea protein hydrolysates (CPHs) showed good water solubility index at pH 7 (>95%) and pH 4.5 (>55%), at DH 20 and 30%, respectively. Oil-holding capacity, emulsifying activity and foaming capacity were also improved by the enzymatic hydrolysis, while proteolysis was detrimental to foam stability and did not improve emulsion stability at DH 10-30%. Therefore, CPHs showed good potential for utilization in food formulations. PRACTICAL APPLICATIONSCowpea is a good nutritional value and available protein source, which could be used for a large-scale production of protein hydrolysates. Enzymatic hydrolysis of food proteins is mostly used to produce ingredients or supplements in food and beverages. In this regard, functional properties of protein hydrolysates are largely dependent on the degree of hydrolysis (DH), which needs to be controlled to avoid excessive proteolysis that can impair functionality and cause unfavorable effects. Then, functional properties of cowpea protein concentrate hydrolyzed by pepsin at DH 5-30% were investigated. The results showed that solubility and oilholding capacity were higher at DH 20-30%. Emulsifying activity and foaming capacity were also improved following hydrolysis, while de-decreasing molecular weight of protein was detrimental to foam stability of hydrolysates. In summary, cowpea protein hydrolysates showed adequate functional properties for utilization as food ingredient and the peptides produced could turn out to present some biological activities.

The synergistic effect of heat treatment on alcalase-assisted hydrolysis of wheat gluten proteins: Functional and antioxidant properties

“…According to presented results, it can be emphasized that AWGH‐16.1% contained larger peptides and more medium‐hydrophobic peptides than the other prepared AWGHs. In contrast, other studies indicated that enzyme hydrolysis produce a significant increase in oil capacity of bean protein concentrate (Mune Mune, ), cowpea protein concentrate (Mune Mune, ), and soy protein isolate (Achouri, Zhang, & Shiying, ).…”

Enzymatic Production, Bioactivity, and Bitterness of Chickpea (Cicer arietinum) Peptides

“…Degree of hydrolysis is often measured by either monitoring the amount of acid or base that must be added to a solution to keep a constant pH as a protein is hydrolyzed or by spectrophotomet-rically measuring chemical conjugates formed from the reaction of a reporter molecule and an amine group of a protein or peptide (Rutherfurd, 2010). In food products, the functionality of a hydrolyzed protein ingredient, such as its emulsification and foaming capacity, can be heavily influenced by its degree of hydrolysis (Ghribi, Maklouf Gafsi, et al, 2015;Mune Mune, 2015). Under similar experimental conditions, chickpea protein concentrate had a higher degree of hydrolysis when hydrolyzed by alcalase than papain or pancreatin (Medina-Godoy et al, 2012).…”

Antibacterial Peptides Produced by Alcalase from Cowpea Seed Proteins

“…Nowadays, there is long-term use and misuse of conventional antibiotics and consequently, bacterial drug resistance is developed and leads to a severe health issue worldwide [1][2][3][4][5][6]. Asthe discovery of other novel antibiotics is difficult, recent perspectives are challenged to find out an innovative way to inhibit multi drug-resistant microbial variants including the use of natural peptide [7], probiotics [8], natural plant extracts either singly or in combination with antibiotics [9][10][11], nanoparticles [12,13],and phage therapy [14].Therefore, it is not surprising that the World Health Organization (WHO) ranked antibiotic resistance as a priority disease encouraging the development of novel antibiotics [10][11][12][13].The best choice and most promising candidates are still cationic antimicrobial peptides or proteins (AMPs) [15].…”

“…The kind of enzyme utilized in bioactive peptide preparations defines hydrolysate properties and the peptides that can be separated [32]. In previous studies, successive enzymatic systems, such as Alcalase ® -Flavourzyme ® (AF) and pepsin-pancreatin (PP), were used for the generating of hydrolysates and peptides which had useful effects on antidiabetics [31][32][33][34][35], antihypertension [32], hypocholesterolemia activity [36], antioxidant activity [37], and functional properties [7,38].…”