Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition

ACE inhibitory activity was studied for different hydrolysates obtained from protein concentrates of two lentil varieties by in vitro gastrointestinal simulation, Alcalase/Flavourzyme, papain and bromelain. Protein/peptide profiles studied by electrophoresis and HPLC-SEC showed a rich composition of the hydrolysates in small peptides ranging in size from 0.244 to 1.06 kDa. ACE inhibitory activity was measured using the HPLC Hippuryl-His-Leu (HHL) substrate method. Significantly different (P < 0.05) IC₅₀ values ranging between 0.053 and 0.190 mg/ml were obtained for different hydrolysates. Furthermore, the inhibition mechanism investigated using Lineweaver–Burk plots revealed a non-competitive inhibition of ACE with inhibitor constants (K_i) between 0.16 and 0.46 mg/ml. These results demonstrate that hydrolysates of lentil proteins obtained by different enzymatic digestions may contain bioactive components.     

Angiotensin I-converting enzyme inhibitory properties and SDS-PAGE of red lentil protein hydrolysates

Several research studies have shown that protein hydrolysates from milk and soy contain peptides that possess angiotensin I converting enzyme (ACE) inhibitory properties and may help to prevent hypertension. To date, no studies have been conducted to determine if red lentil (Lens culinaris) proteins contain peptides with ACE-inhibitory properties. The objective of the present work was to characterize the proteins present in red lentils and determine if tryptic hydrolysis could liberate peptides with ACE-inhibitory properties. Red lentil protein extracts were prepared and fractionated to obtain enriched albumin, legumin and vicilin fractions. Protein/peptide profiles were studied by electrophoresis and ACE-inhibitory activity was measured using the HPLC hippuryl-His-Leu (HHL) substrate method. Our results revealed that red lentil protein hydrolysates posses ACE-inhibitory properties. Furthermore, we demonstrated that the ACE-inhibitory property of the hydrolysates varied as a function of the protein fraction with the total lentil protein hydrolysate having the lowest half maximal inhibitory concentration (IC₅₀) (111 ± 1 μmol/L) (i.e., highest ACE-inhibitory activity), followed by the enriched legumin (119 ± 0.5 μmol/L), albumin (127 ± 2 μmol/L) and vicilin (135 ± 2 μmol/L) fractions, respectively.     

In vitro binding of bile salts by lentil flours, lentil protein concentrates and lentil protein hydrolysates

The binding capacity of bile salts by lentil flours produced from two varieties, Blaze and Laird and their protein concentrates and hydrolysates were studied. Sodium cholate, sodium deoxycholate, sodium taurocholate, sodium glycocholate and sodium chenodeoxycholate were tested individually, and their binding interactions with the lentil products were analyzed using the Trinity Biotech Bile Acids Kit 450-10 and compared to cholestyramine. All tested samples bound the bile salts investigated, and the amount of bile salts bound (> 70%) was sometimes greater than that bound by cholestyramine. Overall, there were no major differences in the bile salt binding capacities of similar samples prepared from the two varieties of lentil. In vitro digestion of the lentil proteins by pepsin/trypsin/??-chymotrypsin, alcalase/flavourzyme and papain significantly reduced the bile salt binding capacity compared to the undigested samples except in the case of sodium deoxycholate where no significant differences in bile salt binding were observed before and after hydrolysis. Binding of bile salts has been linked to cholesterol reduction, thus, the ability of the lentil products to bind bile salts is of interest as it may suggest that lentils could potentially have cholesterol-reducing properties.     

Viscometric Behavior of Reconstituted Tomato Concentrate

The rheological properties of tomato concentrates produced by hot and cold break have been extensively studied by many authors. Only a few studies, however, focus specifically with the rheology of reconstituted concentrates from tomato powders. In this study, the rheological properties of reconstituted tomato concentrate from lyophilized freeze-dried tomato juice were evaluated using rotational viscometer at temperatures 20 °C, 30 °C, 40 °C, 50 °C, and 60 °C and at concentrations of 9.7%, 12.9%, 20.5%, and 26.8% total soluble solids. Using power law model, both flow behavior index (n) and consistency coefficient (k) were determined. The calculated values of flow behavior index (n) were less than unity (0.03–0.28) at all temperatures and concentrations indicating the shear-thinning characteristic of the concentrate. The effect of temperature and concentration on the consistency coefficient (k) was studied. Positive correlation between k in the range of 1.57 and 38.33 Pa s ⁿ and inverse absolute temperature (1/T) has been shown by Arrhenius model. Additionally, linear correlation between consistency coefficient (k) and concentration (C) was determined. The activation energies were found in the range of 3.63 and 7.36 kJ/mol K depending on concentration. The results of this study might be useful to improve the design of processing operations dealing with tomato powder reconstitution.     

Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates

ACE inhibitory activity was studied for different hydrolysates obtained from protein concentrates of chickpea (kabuli and desi) and yellow pea (Golden) using in vitro gastrointestinal simulation, alcalase/flavourzyme, and papain. Protein/peptide profiles studied by SDS–PAGE and SE-HPLC, showed a rich composition of the hydrolysates in small peptides having MWs under 4 kDa. Papain hydrolysed yellow pea proteins showed the highest ACE inhibitory activity. In addition, chickpea desi proteins hydrolysed by in vitro gastrointestinal simulation showed higher ACE inhibition (IC₅₀ of 140 ± 1 μg/ml) compared to its digests obtained by alcalase/flavourzyme (IC₅₀ of 228 ± 3 μg/ml) or papain (IC₅₀ of 180 ± 1 μg/ml) and to chickpea kabuli hydrolysed by gastrointestinal simulation (IC₅₀ of 229 ± 1 μg/ml). The results demonstrate that enzymatic hydrolysates of chickpea and pea proteins contain bioactive ACE inhibitory peptides; furthermore, the type of enzyme used for hydrolysis affects the ACE inhibitory activity.     

Bioactivity of α-lactalbumin related to its interaction with fatty acids: a review

α-Lactalbumin (α-LA) is a whey protein that has been extensively studied for its folding properties and its ability to bind several cations. An interesting property of α-LA is its ability to interact with fatty acids, although this interaction requires the previous unfolding of the protein by removing the Ca(2+) bound. The main function of α-LA is to participate in lactose biosynthesis. However, other biological functions have been attributed to the protein in the last decade. It has been reported that a particular form of human and bovine apo-α-LA induces apoptosis in tumoral and immature cells though spares healthy differentiated cells. The conversion of α-LA to the active apoptotic form requires the unfolding of the protein and the binding of specific fatty acids, mainly unsaturated C18 fatty acids in the cis-conformation. Likewise, it has been shown that a folding variant of α-LA and also some peptidic fragments have a bactericidal activity. The proposed functions for α-LA open new perspectives for its use as a potential ingredient to be added in functional foods or in nutraceutical products. This review summarizes the current state of knowledge on the subject of the interaction of α-LA with fatty acids, and the consequences of this interaction on its bioactivity.