The biological role of prolyl oligopeptidase and the procognitive potential of its peptidic inhibitors from food proteins.

Prolyl oligopeptidase (POP) is a conserved serine protease belonging to proline-specific peptidases. It has both enzymatic and non-enzymatic activity and is involved in numerous biological processes in the human body, playing a role in e.g., cellular growth and differentiation, inflammation, as well as the development of some neurodegenerative and neuropsychiatric disorders. This article describes the physiological and pathological aspects of POP activity and the state-of-art of its peptidic inhibitors originating from food proteins, with a particular focus on their potential as cognition-enhancing agents. Although some milk, meat, fish, and plant protein-derived peptides have the potential to be applied as natural, procognitive nutraceuticals, their effectiveness requires further evaluation, especially in clinical trials. We demonstrated that the important features of the most promising POP-inhibiting peptides are very short sequence, high content of hydrophobic amino acids, and usually the presence of proline residue.

Prediction of Bioactive Peptides from Chicken Feather and Pig Hair Keratins using In Silico Analysis Based on Fragmentomic Approach.

BACKGROUND: Keratin is among the most abundant structural proteins of animal origin, however it remains broadly underutilized. OBJECTIVE: Bioinformatic investigation was performed to evaluate selected keratins originating from mass-produced waste products, i.e., chicken feathers and pig hair, as potential sources of bioactive peptides. METHODS: Pepsin, trypsin, chymotrypsin, papain, and subtilisin were used for in silico keratinolysis with the use of "Enzyme(s) action" and fragmentomic analysis of theoretical products was performed using "Profiles of potential biological activity" in BIOPEP-UWM database of bioactive peptides. Bioactivity probability calculation and toxicity prediction of the peptides obtained were estimated using PeptideRanker and ToxinPred tools, respectively. RESULTS: Our results showed that the keratins are a potential source of a variety of biopeptides, including dipeptidyl peptidase IV, angiotensin converting enzyme, prolyl endopeptidase inhibitory and antioxidative. Papain and subtilisin were found to be the most appropriate enzymes for keratin hydrolysis. This study presents possible structures of keratin-derived bioactive peptides that have not been previously described. CONCLUSION: Our data suggest additional in vitro and in vivo studies to verify theoretical predictions and further investigate the possibility of using keratin-rich waste as a source of peptide nutraceuticals.

An optimal designed experiment for the alkaline hydrolysis of feather keratin.

Feathers, burdensome waste from the poultry industry, can be a cheap source of keratin, a protein with excellent physicochemical, biological, and mechanical properties. Acid and alkaline hydrolyses are usually adopted for isolation of keratin from its natural resources. This study aimed at assessing the statistically significant effect of input variables in the alkaline hydrolysis of keratin from chicken feathers on the process yield and on the molecular weight of peptides obtained. The effect of the volume ratio of 1M NaOH to the feathers' mass, the hydrolysis time, and the shaking speed of the reaction mixture on the process yield were analyzed. The use of statistical analysis at the design step of experiment allowed reducing the trial number from 27 to 9. Among the input variables analyzed, only the volume ratio of 1M NaOH to the feathers' mass had a significant effect on the process yield, while none of them significantly affected the molecular weight of the peptides obtained. All hydrolysates were dominated by two peptides' fractions, with molecular weights of ca. 130 and 250 kDa, and mixture of many peptides of weight close to 10 kDa and smaller. Alkaline hydrolysis of feather keratin yielded protein hydrolysates soluble over a wide pH range.