Production Of Bioactive Peptides Research Articles

From bitter to delicious: properties and uses of microbial aminopeptidases.

Protein hydrolysates are easily digested and utilized by humans and animals, and are less likely to cause allergies. Protein hydrolysis caused by endopeptidases often leads to the exposure of hydrophobic amino acids at the ends of peptides, which consequently causes bitter taste. Microbial aminopeptidases remove the exposed hydrophobic amino acids at the ends of aminopeptides, which improves taste, allowing for easier production. This processe is attacking significant attention from industry and laboratories. Aminopeptidases selectively hydrolyze peptide bonds from the N-terminal of proteins or peptides to produce free amino acids. Aminopeptidases can be classified into leucine, lysine, methionine and proline aminopeptidases by hydrolyzed N-terminal residues; metallo-, serine- and cysteine- aminopeptidases by the reaction mechanisms; dipeptide and triphoptide enzymes by the released number of amino acid residues at the end of hydrolyzed peptides; or acidic, neutral and basic aminopeptidases by their optimal hydrolysis pH. Commercial aminopeptidases are generally produced by microbial fermentation, and are mainly applied in the debittering of protein hydrolysates, the deep hydrolysis of protein, and the production of condiments, cheese, and bioactive peptides, as well as for disease detection in the medical industry.

Ultrasonic-Assisted Extraction and Antioxidant Potential of Valuable Protein from Ulva rigida Macroalgae.

Ulva green macroalgae or sea lettuce are rich sources of protein with nutritional benefits that promote health as a future plant-based functional ingredient in the food industry. Alkaline pretreatment improved ultrasonic-assisted protein extraction from Ulva rigida biomass. Parameters affecting ultrasonic-assisted extraction of protein were type of solvent, biomass-solvent ratio, biomass preparation and extraction cycle. In vitro digestibility was evaluated from oven- and freeze-dried biomass. Results showed highest concentration and extraction yield of protein from U. rigida using alkaline rather than acid and distilled water. A high biomass-solvent ratio at 1:10 or 0.1 g mL-1 increased protein extraction. Higher alkaline concentration increased protein extraction. Highest protein extractability was 8.5% dry matter from freeze-dried U. rigida biomass, with highest protein extraction and antioxidant activity from extraction of U. rigida macroalgae at high alkaline concentrations. U. rigida macroalgae oven-dried biomass presented suitable human digestibility. Efficient pretreatment of U. rigida maximized protein hydrolysate and bioactive peptide production for wide-ranging applications.

Technological role and metabolic profile of two probiotic EPS-producing strains with potential application in yoghurt: Impact on rheology and release of bioactive peptides

Limosilactobacillus fermentum Lf2 (Lf2) and Bifidobacterium animalis INL1 (INL1) are two autochthonous probiotic strains that produce exopolysaccharides (EPS), and some of these molecules were associated with health-promoting properties. In the present work, stirred yoghurts supplemented with these bacteria (added before or after fermentation) were made, in parallel with yoghurt with purified EPS from Lf2. The rheological properties, water holding capacity, microstructure, metabolic activity (aminopeptidase activity, sugar and organic acid metabolism), and production of bioactive peptides (before and after in vitro digestion) were assessed, as well as the activities of six peptidases for each strain, the latter clearly showing different patterns. Yoghurts made with starter culture and Lf2 exhibited a major impact on the previously mentioned parameters. In conclusion, both EPS-producing microorganisms increased the release of bioactive metabolites in yoghurt; they also impacted on levels of organic acids and carbohydrates, rheological properties, and microstructure.

Impact of Pulsed Electric Fields and pH on Enzyme Inactivation and Bioactivities of Peptic Hydrolysates Produced from Bovine and Porcine Hemoglobin.

The production of bioactive peptides from hemoglobin via peptic hydrolysis is a promising alternative to valorizing slaughterhouse blood proteins. Nevertheless, it has some limitations such as low yield, high cost of enzymes, and the use of chemical reagents. The latter is aggravated by the pH increase to inactivate the enzyme, which can affect the bioactivity of the peptides. Thus, this study aimed to evaluate the effect of pulsed electric fields (PEF) on the pepsin inactivation and biological activities (antimicrobial and antioxidant) of hemoglobin hydrolysates. Bovine (Hb-B) and porcine (Hb-P) hemoglobin were hydrolyzed with pepsin for 3 h and treated with PEFs to inactivate the enzyme. The degree of hydrolysis (DH) did not show significant changes after PEF inactivation, whereas peptide population analysis showed some changes in PEF-treated hydrolysates over time, suggesting residual pepsin activity. PEF treatments showed no significant positive or negative impact on antimicrobial and antioxidant activities. Additionally, the impact of pH (3, 7, and 10) on bioactivity was studied. Higher pH fostered stronger anti-yeast activity and DPPH-scavenging capacity, whereas pH 7 fostered antifungal activity. Thus, the use of hemoglobin from the meat industry combined with PEF treatments could fit the circular economy concept since bioactive peptides can be produced more eco-efficiently and recycled to reduce the spoilage of meat products. Nevertheless, further studies on PEF conditions must be carried out to achieve complete inactivation of pepsin and the potential enhancement of peptides' bioactivity.

Evaluation of the antimicrobial attribute of bioactive peptides derived from colostrum whey fermented by Lactobacillus against diarrheagenic E. coli strains.

Colostrum known as “liquid gold” contains approximately 60–80% of whey proteins that can be a great source of bioactive peptide production. Therefore, this study aimed to perform a comparative antimicrobial evaluation of the bioactive peptide generated from L. rhamnosus C25, L. rhamnosus C6, and L. casei NCDC17 fermented colostrum whey. Peptide fractions 10 kDa, 5 kDa, and 3 kDa were isolated using their respective molecular weight cut-off membranes and antimicrobial activity was evaluated against diarrheagenic E. coli strains. The higher inhibition was shown by < 10 kDa peptide fractions from L. rhamnosus C25 fermented colostrum whey and the zone of inhibition was 15 ± 0.06 (E. coli MTCC 723), 17 ± 0.04 (E. coli MTCC 724), 18 ± 0.05 (E. coli MTCC 725), and 17 ± 0.02 (E. coli ATCC 25922). In addition, ST-1 and LT-1 genes of E. coli strains were also confirmed using PCR which is responsible for the diarrheagenic property. Further, the interaction of potent peptides against E. coli strains was also observed by scanning electron microscope. Hence, the significance of the present study emphasized that these bioactive peptides generated from fermented colostrum whey can be used as ingredients in functional food against diarrhoea.

Antioxidant and Metal-Chelating Activities of Bioactive Peptides from Ovotransferrin Produced by Enzyme Combinations

Peptides produced from food sources possess numerous bioactivities that make them useful in improving human health and preventing diseases. Although many studies related to egg protein hydrolysis are available, little work has been conducted on the production of bioactive peptides from apo-ovotransferrin (OTF) using two-step enzyme hydrolysis. The objectives of this study were to produce bioactive peptides from OTF using two enzymes and to determine their functional properties. Lipolyzed OTF was prepared at a concentration of 20 mg/mL and treated with protease (3 h at 55 °C), papain (3 h at 37 °C), elastase (24 h at 25 °C), and α-chymotrypsin (3 h at 37 °C) as the first enzyme treatment. The hydrolysates from the first step of hydrolysis were treated with the above enzymes in different combinations and incubated for 24 h at their optimum temperatures, followed by heat inactivation at the end of each treatment. Based on 15% SDS-PAGE results, the nine best enzyme combinations were selected for further analysis. Papain + protease (PapPro, 0.0075 ± 0.004 malondialdehyde (MDA) mg/kg), α-chymotrypsin + papain (ChyPap, 0.081 ± 0.003 MDA mg/kg), and elastase + α-chymotrypsin (ElaChy, 0.083 ± 0.015 MDA mg/kg) showed strong antioxidant activity. PapPro showed the highest Fe-chelating activity (5.40 ± 0.85%) but lacked Cu-chelating activity. In conclusion, PapPro, ChyPap, and ElaChy treatments of OTF produced peptides with strong antioxidant and Fe-chelating activities but lacked Cu-chelating activity. Thus, ovotransferrin hydrolysates produced using PapPro, ChyPap, and ElaChy treatments have the potential to reduce oxidative stress in the body.

Production, health-promoting properties and characterization of bioactive peptides from cereal and legume grains.

The search for bioactive components for the development of functional foods and nutraceuticals has received tremendous attention. This is due to the increasing awareness of their therapeutic potentials, such as antioxidant, anti-inflammatory, antihypertensive, anti-cancer properties, etc. Food proteins, well known for their nutritional importance and their roles in growth and development, are also sources of peptide sequences with bioactive properties and physiological implications. Cereal and legume grains are important staples that are processed and consumed in various forms worldwide. However, they have received little attention compared to other foods. This review therefore is geared towards surveying the literature for an appraisal of research conducted on bioactive peptides in cereal and legume grains in order to identify what the knowledge gaps are. Studies on bioactive peptides from cereal and legume grains are still quite limited when compared to other food items and most of the research already carried out have been done without identifying the sequence of the bioactive peptides. However, the reports on the antioxidative, anticancer/inflammatory, antihypertensive, antidiabetic properties show there is much prospect of obtaining potent bioactive peptides from cereal and legume grains which could be utilized in the development of functional foods and nutraceuticals.

Review and perspective on bioactive peptides: A roadmap for research, development, and future opportunities

Bioactive peptides (BPs) possess a broad spectrum of beneficial effects, such as antioxidant, antihypertensive, antidiabetic, anticancer, anti-inflammatory, antimicrobial, and anti-aging functions. Given their rapid developments, it is important to revisit our knowledge of BPs, including their production, bioactivity, bioaccessibility, commercial availability, and the latest work in structural bioinformatics. In this paper, recent advances in BP sources, production and characterization, bioactivities, and commercial availability are briefly reviewed; critical challenges, as well as corresponding perspectives, are highlighted. In silico approaches show a great potential to accelerate BP studies and warrant further research. An integrated and comprehensive workflow for future BP screening and evaluation is proposed. There is a great demand for in vivo experiments to further understand the mechanisms of BPs and promote their commercialization. This perspective paper will be a useful reference for both academic researchers and industry partners to comprehend current developments in BPs and to design future research that connects structural bioinformatics, advanced computation methods, and wet chemistry studies.

Bioactive peptides in fermented foods and their application: a critical review

Bioactive peptides are released during the production of fermented dairy, vegetables, fruits, legumes, fish, and meat products. The proteolytic specificity of lactic acid bacteria, Bacillus spp., yeasts, and mold, apart from their ability to synthesize bioactive peptides, plays an important role in the generation of specific bioactive peptides in traditional fermented foods. Controlled fermentation using defined starter strains has been explored for the development of bioactive peptides enriched novel fermented foods with potential functionality. Bioactive peptides enriched foods exert diverse health benefits, such as antioxidant, antihypertensive, antidiabetic, and immunomodulatory effects. Bioactive peptides can be used as alternatives to synthetic compounds due to negligible side effects and high valuation in the nutraceutical and functional food market. However, challenges associated with the identification, quantification, organoleptic properties, and bioavailability of bioactive peptides need to be addressed before exploiting the potential of bioactive peptides in the functional food industry. In the present review, we have discussed the production of bioactive peptides in diverse fermented foods. Structural and sequence specificity of peptides and their effect on the expression of distinct health beneficial effects have been described. The potential of utilizing these bioactive peptides for the development of novel functional fermented foods is discussed. Recent advances in peptide identification, quantification, debittering of peptides, and increasing peptide bioavailability have been explained.

Pea Protein-Derived Peptides Inhibit Hepatic Glucose Production via the Gluconeogenic Signaling in the AML-12 Cells.

Pea protein is considered to be a high quality dietary protein source, but also it is an ideal raw material for the production of bioactive peptides. Although the hypoglycemic effect of pea protein hydrolysate (PPH) has been previously reported, the underlying mechanisms, in particular its effect on the hepatic gluconeogenesis, remain to be elucidated. In the present study, we found that PPH suppressed glucose production in mouse liver cell-line AML-12 cells. Although both of the gluconeogenic and insulin signaling pathways in the AML-12 cells could be regulated by PPH, the suppression of glucose production was dependent on the inhibition of the cAMP response element-binding protein (CREB)-mediated signaling in the gluconeogenic pathway, but not the activation of insulin signaling. Findings from the present study have unveiled a novel role of PPH underlying its anti-diabetic activity, which could be helpful to accelerate the development of functional foods and nutraceuticals using PPH as a starting material.

Gene expression and methylation profiles show the involvement of POMC in primary hyperparathyroidsm

Primary hyperparathyroidism (PHPT) is mainly caused by parathyroid adenoma, which produces excess parathyroid hormones. Its pathogenic mechanisms have not yet been fully understood. To investigate the mechanism in the pathogenesis of PHPT, the transcriptome and genome-wide DNA methylation profiles of parathyroid adenoma were analyzed. The candidate genes that may be involved in the PHPT were verified via qRT-PCR, immunohistochemistry, western blot, and methylation-specific PCR. A total of 1650 differentially expressed genes and 2373 differentially methylated regions were identified. After the integration of its transcriptome and DNA methylation data, IL6, SYP, GNA01, and pro-opiomelanocortin (POMC) were the candidate genes that demonstrated a similar pattern between their mRNA expression and DNA methylation status. Of the 4 candidate genes, POMC, a pro-peptide which is processed to a range of bioactive peptide products like ACTH, was further confirmed to be expressed at low levels at both the mRNA and protein levels, which may be due to POMC promoter hypermethylation. Hypermethylation of the POMC promoter may contribute to its low expression, which may be involved in the pathogenesis of PHPT.

Effect of radio frequency, ultrasound, microwave-assisted papain, and alcalase hydrolysis on the structure, antioxidant activity, and peptidomic profile of Rosa roxburghii Tratt. seed protein.

Traditional enzymatic hydrolysis methods have defects such as low efficiency and poor bioactivity in the production of active peptides. In this study, radio frequency (RF) technology was innovatively used to assist the hydrolysis of Rosa roxburghii Tratt. seed protein (RTSP) by papain and alcalase. RF-assisted hydrolysis was compared with ultrasound-(US) and microwave (MW)-assisted techniques in terms of the degree of hydrolysis, structure, antioxidant properties, and changes in the peptidome of the hydrolysates to clarify the mechanism of functional change of physically-assisted hydrolysate. All three methods improved hydrolysis efficiency. The degree of hydrolysis (DH) of papain group increased from 6.38% to 7.97%, 9.97% and 8.37% after US-, MW- and RF-assisted hydrolysis, respectively, while the DH of alcalase-treated group increased from 21.13% to 25.66%, 26.03%, and 23.01%, respectively. The in vitro antioxidant capacity and intracellular antioxidant capacity of RTSP and its hydrolysates were measured and evaluated by fuzzy statistical evaluation, and MW-assisted alcalase hydrolysis had the highest in vitro and intracellular antioxidant activity scores of 0.713 and 0.820, respectively. Fourier transform infrared and amino acid composition analysis explained the enhanced antioxidant properties of the hydrolysates. Further peptide profiling showed the physical assistance led to an increase in the species and contents of small molecule antioxidant peptides compared to enzyme treatment alone. Pearson's linear correlation analysis showed that AY, LY, IY, PHW, SVL, LHL, YYV, VYY, and NHAV were significantly correlated with the antioxidant properties of hydrolysates. Our data suggested that physical assistance such as US, MW, and RF were effective to improve the efficiency of enzymatic hydrolysis and produce novel antioxidant peptides. PRACTICAL APPLICATION: In this study, it was found that electromagnetic wave-assisted enzymatic hydrolysis could improve the efficiency of hydrolysis and enhance the antioxidant activity of hydrolysates compared to unassisted means. Compared with MW treatment, RF has the comparable hydrolysis effect, but has the advantages of high penetration ability, good uniformity, and low energy consumption and has greater potential for the production of bioactive peptides.

Multivariate correlation of infrared fingerprints and molecular weight distributions with bioactivity of poultry by-product protein hydrolysates

• Processing conditions influence the bioactive properties of protein hydrolysates. • FTIR and SEC fingerprints are correlated with bioactivities of protein hydrolysates. • PLSR models predicted ACE-1 inhibition and DPPH radical scavenging activity. • FTIR-based models were observed to be more robust than SEC-based models. Characterization of protein hydrolysates is a vital step in developing peptide-based bioactive ingredients. Multivariate correlation of chemical fingerprints and bioactivity of poultry by-product protein hydrolysates is explored as a potential analytical strategy for characterization and quality control. Chemical fingerprints of sixty hydrolysates were acquired using Fourier-transform infrared spectroscopy (FTIR) and size exclusion chromatography (SEC). Bioactivities (2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging and angiotensin-1-converting enzyme (ACE-1) inhibition) were measured in vitro . Partial least squares regression models based on FTIR fingerprints or SEC chromatograms showed a better prediction performance for ACE-1 inhibition (coefficients of determination (R 2 ) = 0.91, root mean square error of prediction (RMSECV) = 2.8; R 2 = 0.85, RMSECV = 3.5, respectively) than for DPPH radical scavenging (R 2 = 0.74, RMSECV = 0.3; R 2 = 0.75, RMSECV = 0.3, respectively). Such models are promising tools for rapid prediction of bioactivities and as a quality control technology in production of bioactive peptides.

Regulated processing and secretion of a peptide precursor in cilia

Cilia are sensory and secretory organelles that both receive information from the environment and transmit signals. Cilia-derived vesicles (ectosomes), formed by outward budding of the ciliary membrane, carry enzymes and other bioactive products; this process represents an ancient mode of regulated secretion. Peptidergic intercellular communication controls a wide range of physiological and behavioral responses and occurs throughout eukaryotes. The Chlamydomonas reinhardtii genome encodes what appear to be numerous prepropeptides and enzymes homologous to those used to convert metazoan prepropeptides into bioactive peptide products. Since C. reinhardtii, a green alga, lack the dense core vesicles in which metazoan peptides are processed and stored, we explored the hypothesis that propeptide processing and secretion occur through the regulated release of ciliary ectosomes. A synthetic peptide (GATI-amide) that could be generated from a 91-kDa peptide precursor (proGATI) serves as a chemotactic modulator, attracting minus gametes while repelling plus gametes. Here we dissect the processing pathway that leads to formation of an amidated peptidergic sexual signal specifically on the ciliary ectosomes of plus gametes. Unlike metazoan propeptides, modeling studies identified stable domains in proGATI. Mass spectrometric analysis of a potential prohormone convertase and the amidated proGATI-derived products found in cilia and mating ectosomes link endoproteolytic cleavage to ectosome entry. Extensive posttranslational modification of proGATI confers stability to its amidated product. Analysis of this pathway affords insight into the evolution of peptidergic signaling; this will facilitate studies of the secretory functions of metazoan cilia.

Structural, functional, and anti-cancer properties of conjugates of quinoa protein isolate and olive leaf polyphenolic extract: Application in production of bread

Plant-based proteins are of growing interest in the food industry as an alternative to replace animal based ones, however, their functional properties are limited and research is needed in order to improve emulsifying, foaming, solubility properties. The objectives of the present study were to investigate the impacts of complexation between quinoa protein isolate (QPI) and different concentrations of olive leaf polyphenolic extract (OLE) (0.1 %, 0.2 %, 0.3 %, 0.4 %, and 0.5 %) on the structural changes, functional properties, and in-vitro gastric digestion of QPI. The cytotoxicity of the hydrolyzed QPI/OLE complex, in which proteins turn to bioactive peptides, was evaluated using human stomach cancer cell lines. Additionally, bread using optimum QPI/OLE complex was produced and textural, sensorial, and color properties were evaluated. Fluorescence quenching and surface hydrophobicity measurements showed that QPI and OLE were complexed mainly through hydrophobic interactions. SDS-PAGE revealed that the complexation between the protein and phenolic compounds was appropriate and also complexes were highly digestible in stomach-like conditions. Additionally, OLE could enhance solubility, foaming as well as emulsification properties of QPI significantly. The rate of lipid hydroperoxide formation in QPI/OLE samples containing greater amounts of OLE was also reduced significantly. QPI/OLE complexes also exhibited a large potential to scavenge free radicals. In-vitro digestion experiment showed that the addition of OLE to the QPI solution promoted the production of bioactive peptides. According to the anti-cancer results, hydrolyzed QPI/OLE complexes exhibited a greater cell survival reduction in comparison to the OLE alone. Analysis of produced bread also revealed that the hardness of samples decreased with addition of QPI/OLE complexes. This study demonstrated that QPI/OLE complex shows the potential to be developed by food industry as a tailor-made functional food with health benefits. • Hydrophobic interactions were the main interaction mechanism between QPI and OLE. • Addition of OLE improved the solubility of QPI, significantly. • Complexation with OLE promoted the production of bioactive peptides during digestion. • Digested QPI/OLE complex exhibited a greater human stomach cancer cell survival reduction in comparison to the OLE alone. • Bread with QPI/OLE complexes was made without negative changes in bread’s properties.

Protein Hydrolysates Derived from Animals and Plants-A Review of Production Methods and Antioxidant Activity.

There is currently considerable interest on the use of animal, plant, and fungal sources in the production of bioactive peptides, as evidenced by the substantial body of research on the topic. Such sources provide cheap and environmentally friendly material as it often includes waste and by-products. Enzymatic hydrolysis is considered an efficient method of obtaining peptides capable of antioxidant activity. Those properties have been proven in terms of radical-scavenging capacity using the DPPH (1,1-diphenyl-2-picrylhydrazyl) and ABTS (2,2-azinobis-(3-ethyl-benzothiazoline-6-sulphonic acid)), hydroxyl and superoxide radical methods. Additionally, the reducing power, ferrous ion-chelating (FIC), ferric reducing antioxidant power (FRAP), and the ability of the protein hydrolysates to inhibit lipid peroxidation have also been explored. The results collected in this review clearly indicate that the substrate properties, as well as the conditions under which the hydrolysis reaction is carried out, affect the final antioxidant potential of the obtained peptides. This is mainly due to the structural properties of the obtained compounds such as size or amino acid sequences.

SHTXTHHly, an extracellular secretion platform for the preparation of bioactive peptides and proteins in Escherichia coli

BackgroundIn previous work, we developed an E. coli extracellular secretion platform XTHHly based on the hemolysin A secretion system. It can produce bioactive peptides with simple purification procedures. However, the wider application of this platform is limited by poor secretion efficiency.ResultsIn this study, we first discovered a positive correlation between the isoelectric point (pI) value of the target protein and the secretion level of the XTHHly system. Given the extremely high secretion level of S tag, we fused it at the N-terminus and created a novel SHTXTHHly system. The SHTXTHHly system significantly increased the secretion levels of antimicrobial peptides (PEW300, LL37, and Aurein 1.2) with full bioactivities, suggesting its excellent capacity for secretory production of bioactive peptides. Furthermore, RGDS, IL-15, and alcohol dehydrogenase were successfully secreted, and their bioactivities were largely maintained in the fusion proteins, indicating the potential applications of the novel system for the rapid determination of protein bioactivities. Finally, using the SHTXTHHly system, we produced the monomeric Fc, which showed a high affinity for Fcγ Receptor I and mediated the antibody-dependent immunological effects of immune cells, demonstrating its potential applications in immunotherapies.ConclusionsThe SHTXTHHly system described here facilitates the secretory production of various types of proteins in E. coli. In comparison to previously reported expression systems, our work enlightens an efficient and cost-effective way to evaluate the bioactivities of target proteins or produce them.Graphical abstract

Exploring magnetic field treatment into solid-state fermentation of organic waste for improving structural and physiological properties of keratin peptides

This study systematically investigated the effects of a low-intensity magnetic field on the influence of keratinase activity, peptide yield, and structural and functional properties of peptides produced during solid-state fermentation (SSF) of mixed organic substrates (chicken feather powder and okara) using a mutant strain of Bacillus licheniformis. Initially, the magnetic field-assisted SSF (MSSF) conditions were optimized, which provided the optimized conditions as the number of treatments 3 at every 24 h (24, 48, and 72 h) with 4 h holding time at 120 Gs of magnetic intensity (mI). Under the optimum conditions, keratinase activity and peptide production increased by 10.31% and 13.77%, respectively. Further, in order to evaluate the influence of magnetic field treatment on the peptides, MSSF experiments were done under different mI conditions (40, 80, 120, and 160 Gs), followed by the evaluation of the structural changes of the extracted peptides. The structural analysis revealed that mI had a significant impact on the keratin surface. In contrast, secondary structure analysis confirmed the unfolding of the peptide with decreased α-keratin and increased β-keratin, thereby boosting the bioactive properties of the peptides. The highest hydroxyl free radical (.OH), 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging and Fe2+ chelating rates (56.55, 71.36, and 50.72%, respectively) were found at 120 Gs, which were insignificant with the results at 160 Gs. Therefore, MSSF has a positive effect on the proteolysis mechanism, which can increase bioactive peptide production from keratin.

Production of Bioactive Peptides from Sea Cucumber and Its Potential Health Benefits: A Comprehensive Review.

Bioactive peptides from food have been widely studied due to their potential applications as functional foods and pharmaceuticals. Sea cucumber, a traditional tonic food, is characterized by high protein and low fat, thereby substrates are being studied to release sea cucumber peptides (SCPs). Although recent studies have shown that SCPs have various bioactive functions, there is no literature reviewing the development status of SCPs. In this review, we summarized the production of SCPs, including their purification and identification, then mainly focused on the comprehensive potential health benefits of SCP in vivo and in vitro, and finally discussed the challenge facing the development of SCPs. We found that SCPs have well-documented health benefits due to their antioxidation, anti-diabetes, ACE inhibitory, immunomodulatory, anti-cancer, anti-fatigue, anti-aging, neuroprotection, micromineral-chelating, etc. However, the structure-activity relationships of SCPs and the functional molecular mechanisms underlying their regulation in vivo need further investigation. Research on the safety of SCP and its potential regulation mechanism will contribute to transferring these findings into commercial applications. Hopefully, this review could promote the development and application of SCPs in further investigation and commercialization.

Review on plant-derived bioactive peptides: biological activities, mechanism of action and utilizations in food development

Plant proteins are good alternative to animal sources in bioactive peptide production due to their safety, low-cost, rich resources and easy for large scale production. The bioactivities of the peptides derived from plant proteins including antihypertensive, hypocholesterolemic, immunomodulatory, antioxidant, antimicrobial, anti-diabetic, opiate and hepatoprotective effect are being increasingly recognized with regards to health promoting and disease prevention. In addition to bioactivities, the plant-derived bioactive peptides possess various functional properties including emulsifying and foaming properties, and water and oil retention capacities owning to the hydrophilic/lipophilic property, conformational flexibility and chain length of peptides. Hence, the plant-derived bioactive peptides are promising ingredients for the development of health-care and functional products. This review provides the research progress on the biological activities and functional properties of plant derived peptides. The mechanism of action and structure-activity relationships of the bioactive peptide were also described, when known. Furthermore, recent developments, major challenges and prospect in the application of the plant-derive bioactive peptides in the development of functional products are discussed and summarized. The objective of this review is to improve the understanding of plant-derive bioactive peptides, and provide some constructive inspirations for further research and industrial application in the food and medicine industry.