In vitro inhibition of glucose gastro-intestinal enzymes and antioxidant activity of hydrolyzed collagen peptides from different species.

The growing value of industrial collagen by-products has given rise to interest in extracting them from different species of animals. Intrinsic protein structure variation of collagen sources and its hydrolysis can bring about different bioactivities. This study aimed to characterize and evaluate the differences in vitro biological potential of commercial bovine (BH), fish (FH), and porcine hydrolysates (PH) regarding their antioxidant and hypoglycemic activities. All samples showed percentages above 90% of protein content, with high levels of amino acids (glycine, proline, and hydroxyproline), responsible for the specific structure of collagen. The BH sample showed a higher degree of hydrolysis (DH) (8.7%) and a higher percentage of smaller than 2 kDa peptides (74.1%). All collagens analyzed in vitro showed inhibition of pancreatic enzymes (α-amylase and α-glucosidase), with the potential to prevent diabetes mellitus. The PH sample showed higher antioxidant activities measured by ORAC (67.08 ± 4.23 µmol Trolox Eq./g) and ABTS radical scavenging (65.69 ± 3.53 µmol Trolox Eq./g) methods. For the first time, DNA protection was analyzed to hydrolyzed collagen peptides, and the FH sample showed a protective antioxidant action to supercoiled DNA both in the presence (39.51%) and in the absence (96.36%) of AAPH (reagent 2,2'-azobis(2-amidinopropane)). The results confirmed that the source of native collagen reflects on the bioactivity of hydrolyzed collagen peptides, probably due to its amino acid composition. PRACTICAL APPLICATIONS: Our data provide new application for collagen hydrolysates with hypoglycemiant and antioxidant activity. These data open discussion for future studies on the additional benefits arising from collagen peptide consumption for the prevention of aging complications or hyperglycemic conditions as observed in chronic diseases such as diabetes mellitus type II (DM 2). The confirmation of these results can open new market areas for the use of collagen with pharmacological applications or to produce new supplements. Furthermore, provides a solution for waste collagen from meat industries and adds value to the product.

Bioaccessibility of cashew nut kernel flour compounds released after simulated in vitro human gastrointestinal digestion.

Cashew nuts are mainly consumed as a roasted and salted snack. Lately, the industry has gained interest in broken kernels because of their added value. In this study, defatted cashew nut flour (DCF) underwent simulated gastrointestinal digestion to obtain a soluble (CDs) and an insoluble (CDi) digested fraction. These fractions, which resulted from the digestion of a complex matrix, were evaluated for antioxidant capacity of bioaccessible compounds (present on the soluble digested fraction, CDs) and their potential prebiotic effect, considering that the insoluble digested fraction (CDi) could be fermented by the microbiota in the gut. The DCF had a high protein content (40.74%), being nutritionally characterized as a balanced source of amino acids, with a predominance of aromatic amino acids (phenylalanine and tyrosine), threonine and histidine. The digested DCF presented 76.90% of the soluble components of low molecular weight (0.1-2 kDa), which is typical of antioxidant peptides. The soluble digested fraction (CDs) significantly increased the antioxidant capacity in relation to flour in the ORAC and ABTS assays and the aqueous extract presented the highest values (526.0 and 76.64 as µmol Trolox Eq./g sample, respectively). The CDs protected 29.03% of the supercoiled DNA band and ratified the potential antioxidant capacity after GID in a physiological assay. In addition, the insoluble digested fraction showed a potential prebiotic effect for Bifdobacterium lactis BB-12. Finally, simulated gastrointestinal digestion improves the bioaccessibility of CDF antioxidant compounds as a complex matrix, containing low molecular weight peptides and phenolic compounds, which become more available to react with reactive oxygen species (ROS). In addition, the potential prebiotic effect of defatted cashew nut flour has yielded a promising solution for the total reuse of broken cashew nut kernel as a functional food ingredient.

Isolation and Sequencing of Cu-, Fe-, and Zn-Binding Whey Peptides for Potential Neuroprotective Applications as Multitargeted Compounds.

This study aims to isolate metal-binding peptides and synthesize promising amino acid sequences to potentially act as neuroprotective compounds in the future, targeting different mechanisms. Fractions of whey metal-binding peptides (Cu, Fe, and Zn) isolated by immobilized metal affinity chromatography showed different amino acid profiles according to the metal. The Cu-binding peptides presented roughly twofold increase in the in vitro antioxidant, as assessed by oxygen radical absorbance capacity and anticholinesterase activities over the hydrolysate. This is probably because of the higher concentration of aromatic and basic residues, the latter being crucial for binding to the anionic sites of acetylcholinesterase. Six peptide sequences were synthesized based on the metal-binding sites, molecular mass, hydrophobicity, and bioactivity probability. Among the synthetic peptides, the VF dipeptide stood out both for its in vitro antioxidant and anticholinesterase activities. This peptide, as well as the fraction of Cu-binding peptides, should be further studied because it may act through different mechanisms related to neurodegenerative diseases, in addition to the chelation of the excess of metals in the central nervous system.