No abstract

Cereal Chem. 94(1):117-123The objective of this study was to evaluate the antihypertensive potential of common bean protein hydrolysate. Protein concentrates were obtained, followed by Alcalase enzymatic hydrolysis, and then ultrafiltrated (3,000 molecular weight cutoff); the lyophilized product was named BP3. The angiotensin converting enzyme (ACE) inhibitory activity was determined as IC 50 (3.68 ± 0.07 µg/mL). The antihypertensive effect was evaluated in spontaneously hypertensive rats (SHR) by two assays; Captopril ACE inhibitor was used as a reference compound and water as a control. A short-term assay showed a maximum decrease in mean arterial pressure of -41 ± 5 mmHg in SHR, 3 h after oral administration of 500 mg of BP3/kg of body weight (bw). In a long-term assay, a significant decrease in systolic blood pressure of -24 ± 5 mmHg was observed in SHR, after 45 days of oral administration of 500 mg of BP3/kg of bw/12 h. In both assays, BP3 treatment showed antihypertensive effect over SHR, similar to Captopril treatment. The sequences of the most abundant peptides present in BP3, determined by mass spectrometry, were identified as KFPWVK, GADFRKK, and PQSPCKRVNRHS. These peptides are reported for the first time in Azufrado Higuera common beans, and they are most likely responsible for the antihypertensive effect of BP3. † Corresponding author. Phone: +52 687 87 2 96 26.

Background and Objectives: Water scarcity is limiting for tomato (Solanum lycopersicum L) production, due to its sensitive to drought in the different phases of development, so irrigation should be done in an optimal way; because of this, the objective was to evaluate four levels of irrigation in greenhouse tomato varieties. Methods: A completely randomized experimental design with factorial arrangement was used and various agronomic variables, fruit quality and biomass were measured as response variables. Results: Tomatoes were significantly affected (P?0.05) by variety factors (V), irrigation (R), and their interaction. 100% of variety P presented fruits of greater weight (122 g); while weight decreased to 84, 90, 34 and 18 g when reducing water up to 25%, in varieties Cid, P, E and C, respectively. However, in terms of yield and leaf area, 100% of the Cid variety presented the highest values, around 3.3 kg/plant and 8.6 m-2. Conclusions: Variety c was tolerant to water stress and also does not present apical rotting (calcium deficiency) in the fruit.

Jatropha curcas seeds are a suitable source of oil for biofuel, among other use. A protein‐rich meal is obtained after oilseed extraction. The goals of this study were to determine the physicochemical and functional properties of a nontoxic genotype of J. curcas defatted meal (JCDM) and the seed storage protein fractions to identify future applications. Both glutelin and globulin were the predominant protein fractions obtained from JCDM (42.03 and 20.17 g/100 g of protein, respectively). Leucine, phenylalanine + tyrosine, and histidine content of JCDM and protein fractions met the Food and Agriculture Organization/World Health Organization recommendation for children. The protein solubility (PS) profiles showed minimum values (5.3%–59.7%) at pH 5–6 and maximum at pH 2 (79.7%–81.6%) and above pH 10 (84.6%–89.8%). These findings suggest that JCDM proteins could be used in the formulation of juice or protein‐based beverages. All the proteins showed the highest values for foam expansion (231%–285%) at pH 9. JCDM and the albumin fraction formed highly stable foams at pH 9, while the globulin and glutelin foams were stable at pH 3 and 2, respectively. Protein with stable foams, like those from jatropha are suitable for application in ice cream, mousse, among others. The emulsion activity index had similar behavior as foam expansion, but did not follow a specific trend. Thus, the proteins are suitable for use in salad dressing, sausages, comminuted meats, and mayonnaise. Taken together, JCDM protein and its soluble protein fractions have strong promise as alternative proteins for food structuring.