Development and characterization of spray-dried chia oil microcapsules using by-products from chia as wall material

This research deals with the characteristics of spray-driedchia oil microcapsules formulated with different wall materials,including new encapsulant agents from chia seed (protein rich fraction,PRF; chia mucilage, Muc). The performance of six different wall materialscombinations was studied: sodium caseinate and lactose (NaCas+L), NaCasand maltodextrin (NaCas+Mx), PRF and Mx (PRF+Mx), and each of theprevious three with the addition of Muc. The particle size, rheology, andstability of the parent emulsions were analyzed. The characterization ofthe powders obtained by spray-drying the parent emulsions was carried outby their moisture content, water activity, microencapsulation efficiency,glass transition temperature, morphology, oxidative stability, anddispersibility. Emulsions were reconstituted from the powders atdifferent storage times and analyzed by their particle size andstability. The encapsulation efficiencies were NaCas+L+Muc(96.23±0.40%)~NaCas+L (95.20±0.42%) >NaCas+Mx+Muc (86.65±0.27%)>NaCas+Mx(71.26±0.06%)>PRF+Mx (57.74±3.49%)~ PRF+Mx+Muc (53.37±0.99%). Theaddition of Muc significantly improved the ME% in microcapsules withNaCas+Mx. The induction time values (ti) of NaCas+L, PRF+Mx and NaCas+Mxsystems were about two, three, and five times higher than that of chiabulk oil, respectively. Thus, the studied wall materials were efficientto protect chia seed oil against the oxidation process.Fil: Us Medina, Ulil. Universidad Autónoma de Yucatán; MéxicoFil: Julio, Luciana Magdalena. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Segura Campos, Maira R.. Universidad Autónoma de Yucatán; MéxicoFil: Ixtaina, Vanesa Yanet. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Facultad de Ciencias Agrarias y Forestales. Universidad Nacional de La Plata; ArgentinaFil: Tomás, Mabel Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentin

Effect of Jatropha curcas Peptide Fractions on the Angiotensin I-Converting Enzyme Inhibitory Activity

Hypertension is one of the most common worldwide diseases in humans. Angiotensin I-converting enzyme (ACE) plays an important role in regulating blood pressure and hypertension. An evaluation was done on the effect of Alcalase hydrolysis of defatted Jatropha curcas kernel meal on ACE inhibitory activity in the resulting hydrolysate and its purified fractions. Alcalase exhibited broad specificity and produced a protein hydrolysate with a 21.35% degree of hydrolysis and 34.87% ACE inhibition. Ultrafiltration of the hydrolysate produced peptide fractions with increased biological activity (24.46–61.41%). Hydrophobic residues contributed substantially to the peptides’ inhibitory potency. The 5–10 and <1 kDa fractions were selected for further fractionation by gel filtration chromatography. ACE inhibitory activity (%) ranged from 22.66 to 45.96% with the 5–10 kDa ultrafiltered fraction and from 36.91 to 55.83% with the <1 kDa ultrafiltered fraction. The highest ACE inhibitory activity was observed in F2 ( μg/mL) from the 5–10 kDa fraction and F1 ( μg/mL) from the <1 kDa fraction. ACE inhibitory fractions from Jatropha kernel have potential applications in alternative hypertension therapies, adding a new application for the Jatropha plant protein fraction and improving the financial viability and sustainability of a Jatropha-based biodiesel industry