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Peptidomics refers to the comprehensive profiling of endogenous peptides obtained from biological sources. The formation of endogenous peptides is dependent on not only endogenous factors but also exogenous factors such as microbial proteases or process conditions, including fermentation. This study analyzed the probiotic strains of Lactobacillus rhamnosus LOCK900 (LOCK), Bifidobacterium animalis ssp. lactis BB-12 (BB12), and potential probiotic Lactobacillus acidophilus Bauer Ł0938 (BAUER) to assess their ability of fermentation and peptide production in dry-cured pork loin. The peptides obtained after in vitro digestion were characterized by liquid chromatography–tandem mass spectrometry. Based on the sequences identified, the degree of similarity or differences between the peptides was determined and presented graphically on the factor plane. The charts showed that the meat products aged for 180 and 270 days were the most diverse when BB12 or BAUER were used as starter cultures. Myosin and keratin were identified as the most likely precursors of bioactive peptides in products obtained using this strain of lactic acid bacteria (LAB). The knowledge acquired from this study may contribute to the design of functional meat products as the results revealed not only the peptidogenic potential of the LAB strains indicated on their beneficial effect on the bioactivity of peptides. [ABSTRACT FROM AUTHOR] more...

Peptidomics refers to the comprehensive profiling of endogenous peptides obtained from biological sources. The formation of endogenous peptides is dependent on not only endogenous factors but also exogenous factors such as microbial proteases or process conditions, including fermentation. This study analyzed the probiotic strains of Lactobacillus rhamnosus LOCK900 (LOCK), Bifidobacterium animalis ssp. lactis BB-12 (BB12), and potential probiotic Lactobacillus acidophilus Bauer Ł0938 (BAUER) to assess their ability of fermentation and peptide production in dry-cured pork loin. The peptides obtained after in vitro digestion were characterized by liquid chromatography–tandem mass spectrometry. Based on the sequences identified, the degree of similarity or differences between the peptides was determined and presented graphically on the factor plane. The charts showed that the meat products aged for 180 and 270 days were the most diverse when BB12 or BAUER were used as starter cultures. Myosin and keratin were identified as the most likely precursors of bioactive peptides in products obtained using this strain of lactic acid bacteria (LAB). The knowledge acquired from this study may contribute to the design of functional meat products as the results revealed not only the peptidogenic potential of the LAB strains indicated on their beneficial effect on the bioactivity of peptides. more...

Neuropeptides exert essential functions in animal physiology by controlling e.g., reproduction, development, growth, energy homeostasis, cardiovascular activity and stress response. Thus, identification of neuropeptides has been a very active field of research over the last decades. This review article presents the various methods used to discover novel bioactive peptides in vertebrates. Initially identified on the basis of their biological activity, some neuropeptides have also been discovered for their ability to bind/activate a specific receptor or based on their biochemical characteristics such as C-terminal amidation which concerns half of the known neuropeptides. More recently, sequencing of the genome of many representative species has facilitated peptidomic approaches using mass spectrometry and in silico screening of genomic libraries. Through these different approaches, more than a hundred of bioactive neuropeptides have already been identified in vertebrates. Nevertheless, researchers continue to find new neuropeptides or to identify novel functions of neuropeptides that had not been detected previously, as it was recently the case for nociceptin. more...

Neuropeptides exert essential functions in animal physiology by controlling e.g. , reproduction, development, growth, energy homeostasis, cardiovascular activity and stress response. Thus, identification of neuropeptides has been a very active field of research over the last decades. This review article presents the various methods used to discover novel bioactive peptides in vertebrates. Initially identified on the basis of their biological activity, some neuropeptides have also been discovered for their ability to bind/activate a specific receptor or based on their biochemical characteristics such as C-terminal amidation which concerns half of the known neuropeptides. More recently, sequencing of the genome of many representative species has facilitated peptidomic approaches using mass spectrometry and in silico screening of genomic libraries. Through these different approaches, more than a hundred of bioactive neuropeptides have already been identified in vertebrates. Nevertheless, researchers continue to find new neuropeptides or to identify novel functions of neuropeptides that had not been detected previously, as it was recently the case for nociceptin. [ABSTRACT FROM AUTHOR] more...

Sodium caseinate hydrolysates (NaCaH) contain biologically active peptides that can positively influence human health. However, their intense bitterness hinders their inclusion in food products. To our knowledge, no studies have investigated whether a correlation between bitterness and bioactivity exists in NaCaH, so it is not yet known what effect selective removal of bitterness has on NaCaH bioactivity. A deeper understanding of the physicochemical characteristics affecting both bitterness and bioactivity is therefore needed. The aim of this study was to use in silico analysis to elucidate the relationship between bitterness and bioactivity of the insulinogenic NaCaH. The NaCaH fractions were generated by membrane filtration and flash chromatography and were subsequently evaluated for bitterness by a sensory panel. In this present study, peptidomic and bioinformatic processing of these NaCaH fractions allowed for the identification of insulinogenic peptides as well as other literature-identified peptides in each of the fractions. The results showed that the most bitter fraction contained the highest abundance of insulinogenic peptides, whereas another bitter fraction contained the highest abundance of other literature-identified bioactive peptides exhibiting angiotensin-converting enzyme-inhibition activity. Although some bioactive peptides were identified in the least bitter fractions, the abundance of these peptides was very low. These observations show a correlation between bitter taste and bioactivity, highlighting potential complications in removing bitterness while maintaining bioactivity. However, as the most bitter fraction contained the highest abundance of insulinogenic peptides, there is potential for using a lower dose of this enriched bioactive fraction to exert health benefits. The second most bitter fraction contained a very low abundance of insulinogenic peptides and other bioactive peptides. Therefore, removal of this fraction could reduce the Na-CaH product's bitterness without significantly altering overall bioactive potential. [ABSTRACT FROM AUTHOR] more...

The wheat varietal selection undertaken by breeders in recent decades has been tailored mainly to improve technological and productivity-related traits; however, the latter has resulted in a considerable impoverishment of the genetic diversity of wheat-based products available on the market. This pitfall has encouraged researchers to revalue the natural diversity of cultivated and non-cultivated wheat genotypes in light of their different toxic/immunogenic potential for celiac disease and wheat-allergic patients. In the present investigation, an advanced proteomic approach was designed for the global characterization of the protein profile of selected tetraploid wheat genotypes (Triticum turgidum). The approach combined proteins/peptides sequence information retrieved by specific enzymatic digestions (single and dual proteolytic enzymes) with protein digestibility information disclosed by means of in-vitro simulated human gastroduodenal digestion experiments. In both cases, the peptide pools were characterized by discovery analysis with liquid chromatography high-resolution tandem mass spectrometry, and specific amino acid sequences were identified via commercial software. The peptide list was screened for in silico toxicity/immunogenicity risk assessment, with the aid of various open-source bioinformatics tools for epitopes matching. Given the global information provided by the designed proteomic approach, the in silico risk assessment not only tackled toxicity implication for celiac disease patients, but also scouted for immunogenic sequences relevant for wheat allergic patients, achieving a comprehensive characterization of the protein profile of the selected genotypes. These latter were assessed to encrypt a variable number of toxic/immunogenic epitopes for celiac disease and wheat allergy, and as such they could represent convenient bases for breeding practices and for the development of new detoxification strategies. [ABSTRACT FROM AUTHOR] more...