Influence of physicochemical changes of the avocado starch throughout its pasting profile: Combined extraction.

This work focused on studying the effect of lamellae presence on the pasting profile of isolated avocado starch (C-type) obtained by a combined mechanical and ultrasonic process. Inductively Couple Plasma indicates that this starch is rich in P, K, Na, and Ca. This starch exhibits the most crystalline structure reported so far. The correlation between the morphological and structural properties throughout its pasting profile explains its apparent viscosity behavior. Granules exhibit a non-conventional irregular morphology with sizes ranging from 35 to 40 µm in their long side. DSC reveals endothermal transitions at 68 °C and 119 °C associated with the nanocrystals solvation and amylose-lipid complex, respectively. After gelatinization, the presence of lamellae originated from the partial fragmentation of the crystals. The pasting end exhibited a combined behavior between custard and hydrogel. This correlation could be considered a new methodology to understand the pasting behaviors in any starch.

Hard-to-cook bean (Phaseolus vulgaris L.) proteins hydrolyzed by alcalase and bromelain produced bioactive peptide fractions that inhibit targets of type-2 diabetes and oxidative stress.

The objective was to evaluate the effect of bioactive peptide fractions from de-hulled hard-to-cook (HTC) bean on enzyme targets of type-2 diabetes and oxidative stress. Protein isolates from Pinto Durango and Negro 8025 beans were hydrolyzed (120min) with either alcalase® or bromelain and separated into five peptide fractions (<1, 1-3.5, 3.5-5, 5-10, and >10kDa) using an ultrafiltration membrane system. The <1kDa pinto Durango-bromelain fraction showed the best inhibition of α-amylase (49.9±1.4%), and the <1kDa pinto Durango-alcalase fraction inhibited both, α-glucosidase (76.4±0.5%), and dipeptidyl peptidase-IV (DPP-IV, 55.3±1.6%). Peptides LLSL, QQEG and NEGEAH were present in the most potent fractions. Hydrolysates and peptide fractions showed antioxidant capacity (ORAC: 159.6±2.9 to 932.6±1.1mmolTE/g) and nitric oxide inhibition (57.5±0.9 to 68.3±4.2%). Hydrolysates and fractions <1 and 1-3kDa were able to increase glucose-stimulated insulin secretion from iNS-1E cells up to 57% compared to glucose control. Hydrolysates from HTC beans inhibited enzymes related to diabetes management, being the smallest peptides (<1kDa) the most potent. HTC bean could be a source of protein to produce bioactive peptides with potential antidiabetic properties.

Common bean (Phaseolus vulgaris L.) hydrolysates inhibit inflammation in LPS-induced macrophages through suppression of NF-κB pathways.

The objectives of this study were to evaluate the antioxidant capacity of protein hydrolysates of the common bean (Phaseolus vulgaris L.) varieties Negro 8025 and Pinto Durango and determine their effect on the markers of inflammation in lipopolysaccharide (LPS)-induced RAW 264.7 macrophages. Cell viability was determined and the percentage of viable cells was calculated and concentrations that allowed >80% cell viability were used to determine the markers of inflammation. Alcalase hydrolysates and pepsin-pancreatin hydrolysates showed the highest antioxidant capacity after 80 and 120min of hydrolysis, respectively. Alcalase hydrolysates of the common bean Pinto Durango at 120min inhibited inflammation, with IC50 values of 34.9±0.3, 13.9±0.3, 5.0±0.1 and 3.7±0.2µM, while var. Negro needed 43.6±0.2, 61.3±0.3, 14.2±0.3 and 48.2±0.1µM for the inhibition of cyclooxygenase-2 expression, prostaglandin E2 production, inducible nitric oxide synthase expression and nitric oxide production, respectively. Also, hydrolysates significantly inhibited the transactivation of NF-κB and the nuclear translocation of the NF-κB p65 subunit. In conclusion, hydrolysates from the common bean can be used to combat inflammatory and oxidative-associated diseases.