Anti-Inflammatory Activity and Changes in Antioxidant Properties of Leaf and Stem Extracts from Vitex mollis

Vitex mollis is used in traditional Mexican medicine for the treatment of some ailments. However, there are no studies on what happens to the anti-inflammatory activity or antioxidant properties and total phenolic content of leaves and stem extracts of Vitex mollis during the digestion process; hence, this is the aim of this work. Methanolic, acetonic, and hexanic extracts were obtained from both parts of the plant. Extract yields and anti-inflammatory activity (elastase inhibition) were measured. Additionally, changes in antioxidant activity (DPPH and ABTS) and total phenols content of plant extracts before and after in vitro digestion were determined. The highest elastase inhibition to prevent inflammation was presented by hexanic extracts (leaf = 94.63% and stem = 98.30%). On the other hand, the major extract yield (16.14%), antioxidant properties (ABTS = 98.51% and DPPH = 94.47% of inhibition), and total phenols (33.70 mg GAE/g of dried sample) were showed by leaf methanolic extract. Finally, leaf and stem methanolic extracts presented an antioxidant activity increase of 35.25% and 27.22%, respectively, in comparison to their initial values after in vitro digestion process. All samples showed a decrease in total phenols at the end of the digestion. These results could be the basis to search for new therapeutic agents from Vitex mollis

Contribution and Interactions of Hydroxycinnamic Acids Found in Bran and Wholegrain Sorghum (Sorghum bicolor L. Moench): Effects on the Antioxidant Capacity and Inhibition of Human Erythrocyte Hemolysis

An imbalance between free radicals and antioxidants is known as oxidative stress, and it promotes cellular aging and the development of chronic noncommunicable diseases. The bioactive compounds present in food play an important role in preventing oxidative stress. The aim of this study was to determine the contributions and interactions of the hydroxycinnamic acids found in the bran and whole grain of sorghum and to evaluate their effects on the antioxidant capacity and inhibition of the hemolysis of human erythrocytes. Results showed that the caffeic acid, p-coumaric acid, and ferulic acid found in sorghum contributed to the scavenging of DPPH and ABTS radicals in various proportions. Ferulic acid, which was present in bound form in the bran and wholegrain sorghum, significantly inhibited the AAPH radical-induced oxidation of the erythrocyte membranes by 78.0 and 4.3%, respectively. Combinations of two, three, or four hydroxycinnamic acids may interact in an antagonistic or synergistic manner, thereby altering each other’s bioactivities. The various interactions between the different sorghum bioactives can have a significant impact on their potential bioactivities. These results can be useful in the design of functional foods that aim to deliver bioactives to mitigate cellular aging or noncommunicable diseases

Comparative kinetic characterization of the activity of glycosylated and non-glycosylated trypsin-like serine protease isolated from adults of Rhyzopertha dominica (Coleoptera: Bostrichidae) reared on the grain of three different cultivars of wheat

Rhyzopertha dominica is a pest that uses trypsin-like serine protease enzymes to hydrolyse the proteins in the cereal grains on which it feeds. The present study reveals for the first time that that there are both glycosylated and non-glycosylated serine proteases. The progeny of R. dominica reared on the grain three varieties of wheat were used to fractionate their trypsin-like serine proteases using Concanavalin A affinity chromatography. The albumin fractions from the wheat cultivars used in this study were subjected to size exclusion chromatography to fractionate the albumin inhibitors that are highly specific for the serine protease activity of R. dominica. Kinetic and thermodynamic assays were used to differentiate both types of enzymes. In general, the catalytic efficiency values Vmax/Km for glycosylated proteases were higher, indicating that glycosylation increases the affinity for the substrate. Inhibition assays using wheat albumins revealed that the glycosylated enzymes had higher Ki values, indicating a low affinity for the inhibitors than the non-glycosylated enzymes. Thermodynamic analysis indicates that glycosylation increases the activation energy Ea improving the serine proteases' catalysis. Thus it is likely that R. dominica uses glycosylated proteases in order to optimize the hydrolysis of cereal proteins and nullify the action of wheat grain protease inhibitors and increase its chances of survival