Production Of Bioactive Peptides Research Articles

Production of wheat gluten bioactive peptides by Biarum carduchcorum extract

Production of wheat gluten bioactive peptides by Biarum carduchcorum extract

Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.

The production of bioactive peptides from animal-based raw materials highly depends on enzymatic hydrolysis. Porcine placenta is an underutilized biomass in Thailand's pig farms, yet it is still a source of proteins and beneficial compounds. Porcine placenta could be used as a protein substrate for the production of enzymatic hydrolysate, which could be employed as a functional food ingredient in the future. The goal of this study was to enzymatically produce porcine placenta hydrolysates (PPH) using three commercial enzymes (Alcalase, Flavouzyme, and papain) and evaluate their in vitro antioxidant and antibacterial activity. The degree of hydrolysis (DH) increased as the enzyme load and hydrolysis time increased, but the DH was governed by the enzyme class. The maximum DH was found after using 10% enzyme for 20 min of hydrolysis (36.60%, 31.40%, and 29.81% for Alcalase, Flavouzyme, and papain). Depending on the enzyme type and DH, peptides of various sizes (0.40-323.56 kDa) were detected in all PPH. PPH created with Alcalase had an excellent reducing capacity and metal chelating ability (p < 0.05), whereas PPH made with Flavourzyme and Papain had higher DPPH• and ABTS•+ inhibitory activities (p < 0.05). Papain-derived PPH also had a strong antibacterial effect against Staphylococcus aureus and Escherichia coli, with clear zone values of 17.20 mm and 14.00 mm, respectively (p < 0.05). When PPH was transported via a gastrointestinal tract model system, its antioxidative characteristics were altered. PPH's properties and bioactivities were thus influenced by the enzyme type, enzyme concentration, and hydrolysis time used. Therefore, PPH produced from porcine placenta can be categorized as an antioxidant and antibacterial alternative.

Assessment of Bioavailability after In Vitro Digestion and First Pass Metabolism of Bioactive Peptides from Collagen Hydrolysates.

Collagen hydrolysates (CHs) are composed of bioactive peptides (BAPs), which possess health enhancing properties. There is a knowledge gap regarding the bioavailability of these BAPs that involves intestinal transport and hepatic first pass effects. A simulated gastrointestinal model was used to generate digesta from two CHs (CH-GL and CH-OPT), which were applied to a novel transwell co-culture of human intestinal epithelium cell line-6 (HIEC-6) and hepatic (HepG2) cells to simulate in vivo conditions of absorption and first pass metabolism. Peptide transport, hepatic first pass effects, and bioavailability were determined by measuring BAPs (Gly-Pro, Hyp-Gly, Ala-Hyp, Pro-Hyp, Gly-Pro-Hyp) using an innovative capillary electrophoresis method. All peptides were transported across the intestinal cell layer to varying degrees with both CHs; however, Gly-Pro-Hyp was transported only with CH-GL, but not CH-OPT. Notable hepatic production was observed for Ala-Hyp with both CH treatments, and for Pro-Hyp and Gly-Pro with CH-GL only. All peptides were bioavailable (>10%), except for Gly-Pro-Hyp after CH-OPT. Overall, a high degree of transport and hepatic first pass effects on CH-derived BAPs were observed. Further research is needed to explore the hepatic mechanisms related to the production of BAPs and the bifunctional effects of the bioavailable BAPs noted in this study.

Exploring potentials of antioxidative, anti-inflammatory activities and production of bioactive peptides in lactic fermented camel milk

Camel milk has nutritional and medicinal benefits for the human hosts. The antioxidant activities (ABTS assay, superoxide and hydroxyl free radical assay) in camel milk fermented with Lactobacillus plantarum KGL3A were evaluated. At 48 h (37 °C), the superoxide scavenging activity of free radicals (52.26%), ABTS (62.19%), and hydroxyl scavenging activity of free radicals (61.52%) were measured. The optimal growth conditions for maximal peptide development via proteolytic activity (OPA method) (inoculation rate and incubation time) were determined, and the highest peptide (7.84 mg/ml) was reported at 37 °C for 48 h. Lower molecular weight fermented camel milk peptides decreased the production of proinflammatory cytokines by the lipopolysaccharide treated murine macrophages. Protein profiles had been examined using 2D and SDS-PAGE with a water-soluble extract from fermented camel milk. All 2D spots were trypsin digested and analyzed in RPLC/MS. RP-HPLC was used to analyze 3 kDa and 10 kDa permeates, and RPLC/MS was used to detect peptides. Peakview analysts' tools were used to calculate the raw masses of LC/MS. Most of the new peptides in the Swissport and PIR databases were derived from fermented camel milk protein sequences. Searches in the BIOPEP database confirmed the new antioxidant peptides.

Ekşi Maya Fermantasyonu ile Üretilen Ekmeklerdeki Biyoaktif Bileşenlerin In Vitro Biyoerişilebilirliği ve Sağlık Üzerine Etkileri

Sourdough bread is a traditional product, which is produced by mixing wheat, rye or other grain flours with water and lactic acid fermentation. The supposed mechanisms for the effect of foods produced by sourdough fermentation on health were probiotic effect of microorganisms, production of bioactive peptides and organic acids (acetic acid, butyrate, propionic acid), decreased amount of anti-nutrients (phytic acid, etc.), digestibility of starch and protein, increased bioaccessibility of phenolic compounds and bioavailability of minerals, degradation of gluten, new product to celiac patients. It was reported to have effects on nutrition, such as product development. In this review, the effect of sourdough fermentation on the ingredients in bread, in vitro bioaccessibility and health benefits are examined.

Changes of antioxidative activities and peptidomic patterns of Auxenochlorella pyrenoidosa protein hydrolysates: Effects of enzymatic hydrolysis and decoloration processes

Enzymatic hydrolysis and decoloration are indispensable processes for the production of biological peptides from microalgae materials. Herein, this study aimed to investigate the effects of enzymatic hydrolysis and activated carbon decoloration on antioxidative activities and peptidomic patterns of microalgae protein hydrolysates based on a peptidomic approach. Protein hydrolysates with different hydrolysis time (2–16 h) showed significantly different antioxidative activities based on DPPH and ABTS assays. Regarding the peptidomic pattern, principal component analysis (PCA) models revealed that hydrolysates were classified into discriminable clusters depending on the hydrolysis and decoloration processes. Protein hydrolysates contained many aromatic amino acid containing peptides, such as GDSLYPG, SADPETF, FPALN, FPGDY, and LTDWV, contributing to the classification of PCA models. Activated carbon decoloration at the concentration of 5 mg/mL significantly increased the color lightness by 38.20%, reduced antioxidative activities by 29.78% and 33.59% based on DPPH and ABTS methods, and reduced relative abundances of peptides, especially aromatic amino acid containing peptides. Fifteen selected peptides showed strong ABTS radical scavenging abilities and ten of these peptides were correlated with the antioxidative properties of hydrolysates. The monitoring of dynamic production processes at a molecular scale would contribute to the production and quality control of bioactive peptides from Auxenochlorella pyrenoidosa.

Antivibriosis and cytotoxicity of Actinobacteria associated with red seaweed Gelidiella acerosa

Vibriosis causes a problem in aquaculture and human health. The antibiotic resistance and the limited availability of antimicrobial agents are the driving force for searching for new antivibrio compounds from natural products. Herein, we evaluated ten marine Actinobacteria isolated from red seaweed Gelidiella acerosa for antivibriosis, cytotoxicity and secondary metabolites genes in the way to find a new antivibrio agent. Five Actinobacteria isolates exhibited activity against Vibrio alginolyticus and Vibrio parahaemolyticus with MIC ranging from 0.625 to 5 µg/µl. All isolates displayed no cytotoxicity against Vero cell line except for isolate DR-2R-115–8. All isolates harbour nrps gene, which might indicate that these isolates have great potential in the production of bioactive peptides while none of the isolates showed the presence of pks I, II and hmgcr genes. Identification of ten isolates of marine Actinobacteria associated with red algae was classified into four genera of Brevibacterium, Nocardiopsis, Allokutzneria and Brachybacterium. Our study revealed that the marine Actinobacteria associated with red algae Gelidiella acerosa were promising sources for controlling vibriosis.

ANTIOXIDANT ACTIVITY OF BIOACTIVE PEPTIDE DERIVED FROM PEKIN DUCK FEET GELATIN HYDROLYSATE

Malaysia is one of the main producers of duck meat globally with increasing demands. Increasing in duck production will also increase the number of duck by-products such as skin, feet and bones. Pekin duck (Anas platyrhyncos domestica) is one of the famous duck breeds. Gelatin that was extracted from Pekin duck feet has shown a potential raw material for the production of bioactive peptide that can involve in various functions of the organism physiologically for example antioxidant effects. Pekin Duck feet gelatin was hydrolyzed by using five commercial enzymes (Alcalase, Esperase, Flavourzyme, Neutrase and Protamex) to identify radical scavenging potencies of derived bioactive peptides. All the five enzymes were studied under three different enzyme-substrate ratio (1:10, 1:15, 1:20) with every enzyme optimum pH and temperature. Scavenging activities studied included DPPH radical scavenging activity and ABTS radical scavenging activity. In DPPH radical scavenging activity, all the five enzymes showed the highest percentage of radical scavenging activity at (1:20) enzyme-substrate ratio condition. Among the five enzymes studied, gelatin hydrolyzed with Protamex showed the highest activity (54.83%), followed by Alcalase (53.12%), Esperase (49.81%), Flavourzyme (49.32%) and lastly Neutrase (47.49%) at sample concentration 4.5 mg/ml. The half-maximal inhibitory concentration (IC50) value of the bioactive peptide for ABTS radical scavenging activity was measured. Alcalase has produced the duck feet gelatin hydrolysate that has the lowest IC50 value against ABTS radical scavenging activity with value (0.45%) followed by Esperase (0.54%), Neutrase (0.57%), Protamex (0.60%) and lastly Flavourzyme (0.74%).

Application of preliminary high-pressure processing for improving bioactive characteristics and reducing antigenicity of whey protein hydrolysates.

This study investigated the use of Novo Pro-D® (NPD) and Ficin (FC) as alternative proteases for the production of bioactive peptides with reduced allergenicity from whey protein concentrate (WPC). In addition, the use of high hydrostatic pressure processing as pre-treatment of WPC and its impact on the final characteristics of hydrolysates were also evaluated. NPD treatments generated hydrolysates with a 98% reduction of soluble proteins, greater in vitro antioxidant capacity, and less immunoreactivity when compared to FC ones. However, pre-treatment was an essential tool to improve WPC hydrolysis when FC was used, resulting in hydrolysates with less soluble proteins, enhanced antioxidant capacity, and less allergenicity compared with conventional hydrolysis. As for NPD, the pre-treatment of WPC improved the in vitro antioxidant capacity and resulted in a 100% reduction in immunoreactivity to β-lactoglobulin in a shorter processing time. Importantly, bioactive peptides generated by FC displayed an improved ability to induce in vitro arterial relaxation, compared with those obtained from NPD process. Therefore, this study provides innovative evidence regarding how the proteases used for production of whey hydrolysates can improve its biological effects, and discloses the use of high hydrostatic pressure combined with enzymatic hydrolysis as a promising alternative to produce hydrolysates with improved properties.

Bioactivities generated from meat proteins by enzymatic hydrolysis and the Maillard reaction

Bioactive peptides are released from meat proteins by enzymatic hydrolysis (i.e., gastrointestinal digestion, aging/storage, fermentation, and protease treatment). Such peptides attribute physiological functions to meat and meat products and are promising food ingredients for developing functional foods. Meat by-products (e.g., blood and collagen) are also good sources for generating bioactive peptides, since they are produced in large quantities and are rich in proteins. Although protein-derived bioactive peptides are attractive ingredients, their changes by the Maillard reaction during processing, cooking, and storage should be investigated. This article briefly reviews the production of bioactive peptides from meat and meat by-products. Such diverse peptides affects circulatory, nervous, alimentary, and immune systems. Then, the bioactivities of Maillard reaction products (MRPs) generated from protein hydrolysates are discussed. Special attention is paid to bioactivities of 2,5-dimethyl-4-hydroxy-3(2H)-furanone (DMHF) inhalation. As such activities, we have evaluated the impact of DMHF on blood pressure, moods, brainwaves, and dietary intake. Our efforts for understanding various aspects and implication of peptides and MRPs from meat proteins would open new avenues in the meat and food industry.

Impact of conductivity on the performances of electro-acidification and enzymatic hydrolysis phases of bovine hemoglobin by electrodialysis with bipolar membranes for the production of bioactive peptides

Production of bioactive peptides from slaughterhouse wastes with a final low salt content by electrodialysis with bipolar membranes (EDBM) has recently been demonstrated as an innovative and efficient technology. However, a limitation in the electro-acidification process was noticed due to membrane fouling. In this context, the aim of the present work was to identify process conditions that could reduce peptide fouling in EDBM. Hence, two different conductivity levels (0.9 mS/cm and 4.5 mS/cm) were investigated in bipolar/monopolar (anionic and cationic) configuration and compared to conventional hydrolysis in the same conductivity conditions as well as a conventional hydrolysis using a buffer solution. The impact of such conductivity levels was studied during EDBM especially on membrane fouling and hydrolysis parameters: 1) kinetics of the enzymatic mechanism, 2) degree of hydrolysis and 3) peptide population. The results showed the same enzymatic mechanism “one-by-one” for all the conditions but a slower enzymatic kinetics for EDBM-0.9 mS/cm. EDBM-0.9 mS/cm allowed the production of bioactive peptides but with fouling formation on MCP while EDBM-4.5 mS/cm allowed the production of bioactive peptides without any fouling. Finally, optimizing certain conditions for further studies would lead to a promising green process to substitute synthetic additives used to protect food by antimicrobial peptides from blood slaughterhouses.

Functional dairy products as a source of bioactive peptides and probiotics: current trends and future prospectives.

Milk is an incredibly healthy food world-wide. However, the 'lactase deficient' individuals cannot digest milk's carbohydrate lactose. A large part of the world population is depriving of highly beneficial milk proteins like casein, lactoalbumin, lactoglobulin, etc. due to lactose intolerance. Production of functional foods and bioactive peptides from milk with natural antioxidants and the addition of probiotics could be the best alternative to extend the use of milk functionalities. Among different probiotics, the lactic acid bacteria (LAB) like Lactobacillus delbrueckii sub sp. bulgaricus, Streptococcus thermophilus and some species of Bifidobacteria and their metabolites (paraprobiotics and postbiotics) have been given more preference to add in milk-derived functional foods. These species are generally considered as heat-tolerant, highly proteolytic, and peptidolytic towards milk proteins and they liberate smaller molecules of bioactive peptides during fermentation and other processes that stimulate the enzyme lactase to help people in digestion of milk carbohydrate lactose. Moreover, the incorporation of natural antioxidants in yoghurt and other dairy products prevents the rancidity of milk fat. The level of bioactive peptides produced in milk-derived functional foods can be determined by capillary zone electrophoresis, mass spectrometry, fractionation, and other modern assessment techniques. Commercial production of functional probiotic products with bioactive peptides could significantly contribute to reduce milk spoilage, enhance health benefits as well as the growth of the agro-processing industry.

Pepsin Hydrolysis of Orange By-Products for the Production of Bioactive Peptides with Gastrointestinal Resistant Properties

Recently, the use of bioactive compounds in improving human health has received more attention. The aim of the present study was to hydrolyze orange seed proteins using pepsin enzyme to obtain bioactive peptides as well as to study the stability of such activity after simulated gastrointestinal digestion conditions. The method was optimized using different enzyme concentrations from 1% to 3%, hydrolysis times between 2 and 5 h, and an optimal temperature of 33 °C. Biological activities including α-glucosidase inhibition, α-amylase inhibition, Angiotensin I-Converting Enzyme (ACEI) inhibition, ferric reducing antioxidant power, and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity were evaluated. According to the results, a significant higher value of the biological activity (p < 0.05) was observed using an enzyme ratio of 0.03 E/S and hydrolysis time of 3.5 h. After size-exclusion chromatography separation, fractions 45–49 and 50–54 showed the highest biological roles such as antioxidant, ACEI inhibitory, and hypoglycemic. Fractions with the highest biological activity were purified using RP-HPLC and analyzed using nano-liquid chromatography and mass spectrometry. The results obtained after simulated gastrointestinal digestion indicated that peptide fractions obtained after chromatographic separation significantly maintain their activity.

Seaweed Proteins as a Source of Bioactive Peptides.

Seaweeds have received great attention as a vegetarian and sustainable marine source of protein, which does not need irrigation, arable land, and fertilization. Besides, seaweeds are considered as an untapped resource for discovering bioactive compounds with health benefits where bioactive peptides have shown outstanding potential. This review provides a detailed overview of available scientific knowledge on production methods, bioactivity and application of peptides from seaweed proteins. The emphasis is on the effects from seaweed varieties and peptide production conditions on the bioactivity of the peptides and their potential health benefits. Bioactive properties of seaweed peptides, including antioxidant, antihypertensive, antidiabetic, anti-inflammatory, anticancer activities and other potential health benefits, have been discussed. It also covers current challenges and required future research and innovations for the successful application of seaweeds proteins as a sustainable source of bioactive peptides. Effects from seasonal variation of seaweed composition on the bioactivity of their peptides, difficulties in the extraction of proteins from seaweed complex structure, scalability and reproducibility of the developed methods for the production of bioactive peptides, the safety of the peptides are examples of highlighted challenges. Further studies on the bioavailability of the seaweed bioactive peptides and validation of the results in animal models and human trials are needed before their application as functional foods or pharmaceutical ingredients.

Continuous production of tempe-based bioactive peptides using an automated enzymatic membrane reactor

The utilization of bioactive peptides from food-grade raw materials has received increasing interest, especially for the production of functional foods. Within this study, a combination of fermentation and in vitro papain hydrolysis was devised to produce bioactive peptides exhibiting antioxidant property and angiotensin I-converting enzyme (AICE) inhibitory activity. The utilization of an automated membrane reactor system developed in this study could facilitate the continuous hydrolysis of tempe flour-rich in protein under constant flux, thus constant residence time operation. The optimum operating conditions were: [E]/[S] = 10% (w/v) and τ = 9 h. With a 10-kDa membrane filtration, the resulted antioxidant capacity and AICE inhibition were 0.033 mg AEAC/mL and 50.9%, respectively. Further separation of permeate with a 2-kDa membrane cut-off leveled off the antioxidant capacity but increased the AICE inhibitory activity (i.e., Reduction of IC50 of ~40%). By this, the obtained IC50 for AICE was 0.08 mg protein/mL, and this value was comparable with the IC50 values reported in the literature. Industrial relevanceThe production of bioactive peptides from soybean through a combination of fermentation and in vitro enzymatic hydrolysis is limitedly reported. In this work, fermented soybean (tempe) was further hydrolyzed continuously using an automated membrane reactor. The hydrolysis under optimum operating conditions could increase the antioxidant activity and AICE inhibition of permeate. This work is expected to increase the commercialization of tempe-based food products by using safer technological approaches (i.e., fermentation and membrane technology).

Distribution of Important Probiotic Genes and Identification of the Biogenic Amines Produced by Lactobacillus acidophilus PNW3.

The genome of Lactobacillus acidophilus PNW3 was assessed for probiotic and safety potentials. The genome was completely sequenced, assembled using SPAdes, and thereafter annotated with NCBI prokaryotic genome annotation pipeline (PGAP) and rapid annotation using subsystem technology (RAST). Further downstream assessment was determined using appropriate bioinformatics tools. The production of biogenic amines was confirmed through HPLC analysis and the evolutionary trend of the strain was determined through the Codon Tree pipeline. The strain was predicted as a non-human pathogen. A plethora of encoding genes for lactic acids and bioactive peptides production, adhesion molecules, resistance to the harsh gut environmental conditions, and improvement of the host metabolism, which are putative for important probiotic functionalities, were located at different loci within the genome. A bacteriocin predicted to be helveticin J was identified as one of the secondary metabolites. The maximum zone of inhibition exhibited by the crude bacteriocin against STEC E. coli O177 was 21.7 ± 0.58 mm and 24.3 ± 1.15 mm after partial purification (250 µg/mL). Three coding sequences were identified for insertion sequences and one for the CRISPR-Cas fragment. The protein-encoding sequence for Ornithine decarboxylase was found within the genome. L. acidophilus PNW3 presents important features categorizing it as a viable and safe probiotic candidate, though further safety investigations are necessary. The application of probiotics in livestock-keeping would ensure improved public health and food security.

Optimisation of bovine β-lactoglobulin hydrolysis using cardosins from dried flowers of Cynara cardunculus

Bovine whey protein was hydrolysed using cardosins A and B purified from dried flowers of Cynara cardunculus by combining diafiltration, anion-exchange chromatography and ultrafiltration. The proteolysis experiments were performed using different whey protein concentrations and enzyme/substrate (E/S) ratios. Complete hydrolysis of the main whey proteins, β-Lactoglobulin (β-Lg) and α-lactalbumin (α-La), was achieved after 4 h, at E/S ratios of 1/150 U/mg, regardless the initial protein concentration. In previous reports, the authors suggested that cardosins could not hydrolyse β-lactoblogulin. However, our promising results open up new possibilities to further explore the action of cardosins on whey proteins for the production of bioactive peptides.

Bioactive peptides and proteases: characteristics, applications and the simultaneous production in solid-state fermentation

Bioactive peptides are compounds hydrolysed from an inactive parental protein that has beneficial effects on health, such as reduction of blood pressure, antioxidant activity, reduction of problems caused by diabetes, anticancer action, among others. These compounds can be obtained by the hydrolysis of proteins by enzymes, as the proteases, which are produced by microorganisms through solid-state fermentation. Solid-state fermentation (SSF) has been widely used to produce enzymes and other biocompounds due to advantages as simplicity, the possibility of using residues as substrates, allowing the reduction of environmental pollution, the addition of value to these residues, and lower costs in the process. SSF also allows the simultaneous production of proteases and bioactive peptides, optimising the process and reducing antinutritional compounds, such as allergens. This work aimed to review the literature on the production of proteases and bioactive peptides through solid-state fermentation, including the simultaneous production of these compounds, since the fermented medium can benefit from the hydrolysis capacity of the enzymes produced by microorganisms. Normally, obtaining these compounds has been studied in an isolated way and not concomitantly in a single bioprocess, being this the main differential of our review.

Peptidomic analysis of antioxidant peptides from porcine liver hydrolysates using SWATH-MS

There is a growing interest in the production and identification of bioactive peptides as health-promoting agents. A relevant method to produce biopeptides is enzymatic hydrolysis from protein-rich meat by-products. Pork liver proved to be a good source of protein (18.54%) with a low-fat content (3.38%). After hydrolysis at different times (4,6,8 and 10 h) with Alcalase, relevant amino acids such as hydrophobic (leucine, valine and isoleucine) and aromatic (tyrosine and phenylalanine) involved in antioxidant capacity were strongly increased. For the peptidomic analysis, a novel technique called sequential window acquisition of all theoretical mass spectra (SWATH-MS) was used. Regarding the effect of hydrolysis time, PCA demonstrated a great differentiation among the peptidomic pattern. Fifty-one peptides were correlated with antioxidant activity measured by DPPH, ABTS, FRAP and ORAC assays. SWATH-MS allowed the identification and quantification of six peptides from trypsinogen, ferritin, keratin, carboxylic ester hydrolase and globin domain-containing protein as potential antioxidant compounds. SignificanceThe pork liver tissue contains a substantial amount of proteins whose enzymatic hydrolysis might generate antioxidant peptides. The bioactive peptides from pork liver would contribute to harnessing by-products of the swine industry as well as added-value products will be produced. The antioxidant activity of the mixtures revealed potential antioxidant peptides which could be used in the development of nutraceutical and functional food products.

Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development.

Bioactive peptides (BPs) are specific protein fragments that exert various beneficial effects on human bodies and ultimately influence health, depending on their structural properties and amino acid composition and sequences. By offering promising solutions to solve diverse health issues, the production, characterization, and applications of food-derived BPs have drawn great interest in the current literature and are of particular interest to the food and pharmaceutical industries. The microbial fermentation of protein from various sources is indubitably a novel way to produce BPs with numerous beneficial health effects. Apart from its lower cost as compared to enzymes, the BPs produced from microbial fermentation can be purified without further hydrolysis. Despite these features, current literature shows dearth of information on the BPs produced from food via microbial fermentation. Hence, there is a strong necessity to explore the BPs obtained from food fermentation for the development of commercial nutraceuticals and functional foods. As such, this review focuses on the production of BPs from different food sources, including the extensively studied milk and milk products, with emphasis on microbial fermentation. The structure-activity (antihypertensive, antioxidant, antimicrobial, opiate-like, anti-inflammatory, anticancer/antiproliferative, antithrombotic, hypolipidemic, hypocholesterolemic, and mineral binding) relationship, potential applications, future development, and challenges of BPs obtained from food fermentation are also discussed.