Abstract
Bioactive peptides (BAPs) obtained from plants and microbes have been thoroughly explored and studied due to their prophylactic properties. The use of BAPs seems to be a promising substitute for several currently available antibiotics because of their antimicrobial properties against foodborne pathogens. BAPs have several other useful properties including antitumor, antihypertensive, antioxidant, antiobesity, and antidiabetic activities. Nowadays, scientists have attempted to recombinantly synthesize bioactive peptides to study their characteristics and potential uses, since BAPs are not found in large quantities in nature. Many pathogenic microorganisms including foodborne pathogens are becoming resistant to various antibiotics. To combat these pathogens, scientists are working to find novel, innovative, and safe antimicrobial agents. Plant- and microbe-based BAPs have demonstrated noteworthy antimicrobial activity against a wide range of pathogenic microorganisms, including foodborne pathogens. BAPs can kill pathogenic microorganisms by disrupting membrane integrity, inhibiting DNA and RNA synthesis, preventing protein synthesis, blocking protein activity, or interacting with certain intracellular targets. In addition, the positive effect of BAP consumption extends to gut microbiota modulation and affects the equilibrium of reactive oxygen species in the gut. This article discusses recombinant BAPs, BAPs generated from plants and microbes, and their antimicrobial applications and modes of action for controlling foodborne pathogens.
1. Introduction
Bioactive peptides have been thoroughly researched for their health advantages and possible applications as nutraceuticals and functional food ingredients [1]. Emerging antibiotic resistance (ABR) related to foodborne illnesses harms both human and animal populations as well as the economy and human health suffers greatly from bacterial resistance which prompts food to deteriorate and causes health problems. Finding antibiotic substitutes that can reduce health risks and the consequences of numerous foodborne illnesses is now vital [2]. If BAPs are employed as food additives or preventative measures, they exhibit potential as safe food supplements with a variety of health benefits and BAPs are less likely than antibiotics to cause bacteria to evolve resistance [3].
BAPs are often embedded in the structure of large proteins and are cleaved to become active. They consist of short amino acid (aa) sequences (2–20 aa) that provide beneficial health facilities, such as, in the form of controlling foodborne pathogens [4]. They can be derived from microbes, plants, and animal tissues. In addition, food processing (cooking, fermentation, and ripening) or microbial enzyme maturation may produce BAPs. Products including milk, cheese, yogurt, sausage, eggs, soybeans, soy milk, chia, rice bran, peas, flaxseed, mushrooms, and cauliflower are considered richer sources of BAPs [5]. Many classes of BAPs are currently available for purchase chemically or recombinantly [6].
There are a variety of plant-derived BAPs such as puroindolines, lipid transfer proteins, thionins (α/β, γ), glycine-rich peptides, hevein-like peptides, plant defensins, and knottin-like peptides. Numerous classes of stems, roots, seeds, flowers, and leaves have all been found to contain BAPs and they show activity against both phytopathogens and bacteria that are harmful to humans [7]. Microbes also produce a large variety of biologically active peptides such as pediocins, nisin, enterocin, propionicin, gramicidin, endolysins, and apicidin. These peptides are derived from viruses, bacteria, and fungi. They protect organisms from invasive bacteria, viruses, protozoa, and fungi by disrupting the membrane or metabolic processes [8].
Peptides can regulate a number of vital physiological functions such as hormones. Their positive health impacts include cardiovascular disease reduction, immunomodulatory, antihypertensive effects, mineral binding, chelating action, and anticoagulant, antioxidative, and antimicrobial properties. Besides, they are in charge of the flavor of the food as well as preventing the activity of enzymes that cause diseases to develop [8]. Some BAPs through their antimicrobial activity protect mammals from various foodborne pathogens as well as their direct impact on the shelf life of prepared foods has made them highly desirable in this industry [9]. These peptides can change the biological processes of pathogens, such as the growth of cells and the formation of cell membranes. They are thought to work by opening up channels or pores in bacterial membranes, which prevent anabolic processes, and alter gene expression and signal transmission while encouraging angiogenesis [10]. Another immunomodulatory result, that may halt the spread of foodborne illnesses caused by the foodborne pathogen, Listeria monocytogenes can lead to severe listeriosis and develop resistance to antibiotics [11]. Therefore, as an antimicrobial peptide, BAP can kill pathogens through a variety of actions such as interrupting membrane integrity, hindering DNA and RNA synthesis, preventing protein synthesis, and acting on particular intracellular targets [12, 13]. Besides, the positive effect of BAP by consuming it also includes gut microbiota regulation. Recent research has linked the prevention and treatment of neurodegenerative illnesses such as Parkinson’s disease, Alzheimer’s disease, and dementia to gut microbiome modifications supported by BAPs [14, 15].
Food safety and human health are seriously compromised by foodborne pathogens. They are responsible for various life-threatening diseases in humans. Moreover, a large number of these foodborne bacteria are developing antibiotic resistance on a daily basis [11]. Therefore, it is essential to develop safe and effective antimicrobial agents to control these foodborne pathogens (e.g., viruses, bacteria, and parasites) for food safety as well as to protect human health. Bioactive antimicrobial peptides could be a good option for the development of novel antimicrobial agents against foodborne pathogenic microorganisms such as Escherichia coli, Salmonella, Listeria, Cyclospora, Campylobacter, and Shigella. The naturally derived BAPs possess significant antiviral activity against the hepatitis virus along with other viruses as these BAPs can inhibit viral entry into the host cells and interfere with host-specific interactions. From this perspective, this review highlights currently known plant- and microbes-derived bioactive BAPs as well as recombinant BAPs with their mechanisms of action for controlling foodborne pathogens and their prospects.
2. BAPs from Different Sources
2.1. Plant-Derived BAPs
Plants produce a large variety of biologically active peptides such as thionins (α/β, γ), puroindolines, lipid transfer proteins, plant defensins, glycine-rich peptides, hevein-like peptides, knottin-like peptides, and homologs of MBP-1, which work against bacterial and fungal pathogens (Table 1). There are five types of thionins: grain endosperms that contain purothionins, which are type I thionins; α-hordothionin and β-hordothionin are type II thionins that are found in Pyrularia pubera leaves and nuts; ligatoxin A and viscotoxins are examples of type III thionins; and crambin and hellothionin D peptides belong to groups IV and V, respectively [7, 13, 16]. Plant defensins are small, cysteine-rich, cationic antimicrobial peptides containing conserved 3D structures comprising one α-helix and three antiparallel β-strands. γ-Hordothionin is a member of plant defensins and Ah-AMP1, Ct-AMP1, Rs-AFP1, PhD1, and Hs-AFp1 are examples of plant defensins [7, 45]. Most plant defensins fall into one of the three categories based on the quantity and location of cysteine residues inside the molecules: hevein-type, knottin-type, and thionin-type [50].
2.2. Microbe-Derived BAPs
Microbe-derived BAPs are found in viruses, bacteria, and fungi. These peptides are classified based on their sources, structural characteristics, amino-acid-rich content, and activities. Viral BAPs are phage proteins containing virion-associated peptidoglycan hydrolases, depolymerases, lysins, and holins called enzybiotics. Phage-tail complexes and phage-encoded lytic factors are two types of phage BAPs. Bacterial BAPs are produced by both Gram-positive and Gram-negative bacteria. Gram-positive bacterial BAPs are classified as ribosomally-produced BAPs known as bacteriocin and nonribosomally or enzymatically-produced BAPs [8]. There are two types of bacteriocins: lantibiotics and nonlantibiotics (lantibiotics contain unnatural amino acid lanthionine) [68]. Gram-negative bacterial bacteriocins are grouped into colicins, microcins, colicin-like bacteriocins, and phage-tail-like bacteriocins. Defensins and peptaibol are the two types of fungal BAPs. Peptaibol contains the name in combination with peptide, α-aminoisobutyrate, and amino alcohols. Microbe-derived BAPs and their potential antimicrobial applications are shown in Table 2.
2.3. Recombinant BAPs
Once the peptide sequence is revealed, it can be synthesized chemically or by utilizing recombinant DNA technologies. Hydrolysis by enzymes is a simple production process, but it takes time and requires sophisticated purifying methods. Furthermore, the yield of natural proteins is restricted by their extremely low BAP content. Even though chemical synthesis is the most mature technology for peptide production, the necessity of toxic reagents for their chemical production and lack of specificity are severe drawbacks. On the other hand, recombinant DNA technology uses fewer chemicals and makes the synthesis of these proteins simpler with high yield and purity without any environmental impact [113, 114].
According to multiple studies, recombinant production of BAPs can be categorized into two classes, depending on bioactive peptide gene expression in a particular expression system, either in vivo or in vitro [6]. In the in vivo expression method, the targeted peptide gene is linked to another known carrier protein gene to make the purification simple and to be able to produce a mass amount of the necessary peptide. For instance, ecallantide and desirudin peptides are expressed in yeast [115, 116]. On the other hand, the in vitro expression method, which is a cell-independent system, has the benefit of rapid production of the desired outcome though it is not cost-effective [117]. However, the recent focused method is the engineering of BAPs, due to peptide flexibility and effectiveness. For example, engineered insulin plays a crucial role in type II diabetes with a longer effect than own insulin [118].
One study investigated the recombinant synthesis of the BAP, GIISHR (Gly-Ile-Ile-Ser-His-Arg) with notable antioxidant activity from the muscle of the flawless smooth-hound (Mustelus griseus) [119]. Antioxidant peptides isolated from spotless smooth-hound exhibited good scavenging activities and protected H2O2-induced HepG2 cells from oxidative stress by increasing the levels of catalase, superoxide dismutase, glutathione peroxidase, and glutathione reductase along with decreasing the content of malonaldehyde [4]. The peptide had a strong ability to neutralize hydroxyl, ABTS (2,2′-Azino-bis-(3-ethylbenzotiazoline-6-sulfonic acid)), and superoxide radicals [119]. At the beginning, the strain as host such as E. coli needs to be selected and then the expression vector is designed. Tricine-SDS-PAGE and western blot analysis are employed to assess the amount of expression of the recombinant protein [120], which is followed by trypsin digestion and purification of the peptide [121]. Then, the purified peptide was analyzed by liquid chromatography and their activity was tested by different assays [4].
An antagonistic peptide, Turgincin A is recombinantly produced by the Pichia pastoris strain. This recombinant peptide prevents the growth of all bacteria in the pork meat while preserving the meat’s color [21]. Another recent recombinant fusion peptide, CpsA-CpsC-L-ACAN consists of three parts: CpsAo CpsC, the enzymes that produce Streptococcus agalactiae capsules, serine, and glycine, a linker, and ACAN, an anticancer component. As a result, this peptide shows good antimicrobial performance against E. coli and Staphylococcus aureus [22].
3. Antimicrobial Applications of BAPs against Foodborne Pathogens
Both the health of people and the economy are at stake due to the rise in the frequency of foodborne diseases. The presence of harmful bacteria, viruses, fungi, parasites, and toxins in food that is contaminated has been linked to more than 200 various diseases [122]. Due to this, the application of preservatives is required in a wide variety of foods to ensure safety while preserving the product’s quality and sensory qualities. In addition, as it was already indicated, efforts are continually made to find natural antimicrobials in order to keep up with the customer demand [123]. In this case, the application of BAPs becomes necessary.
Plant-derived BAPs having antimicrobial properties have been identified and described in a wide range of structural and functional ways up to this point. From a library of cDNA derived from Mexican avocado fruits, PaDef was found and isolated. It is a peptide with defensin-like properties. As PaDef exhibits antibacterial properties against S. aureus and E. coli, it can be used to heal foodborne infections [124]. In a different investigation, four closely similar cysteine-rich peptides with antifungal and antibacterial properties were extracted and described from the grain of Impatiens species balsamina [125]. In addition, these cysteine-rich peptides showed high activity against enteric pathogens such as S. aureus, E. coli, and Salmonella yet showed no cytotoxicity toward human cells. Plants have also been found to contain 2S albumin proteins, another family of AMPs. Pa-AFP-1 was discovered to effectively suppress the growth of filamentous fungi, including Trichoderma harzianum, Colletotrichum gloeosporioides, Aspergillus fumigatus, and Fusarium oxysporum, which were isolated from passion fruit [126, 127]. The next compound is CaThi, an isolated and described thionin-like peptide from chili. According to reports, CaThi is effective against a variety of pathogenic bacteria, including Candida albicans, F. solani, C. tropicalis, and S. cerevisiae [128, 129].
The main enzyme for photorespiration and photosynthesis in plants as well as in other living things is known as ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), which is also the most prevalent protein in the world. RuBisCO is a desirable and long-term resource for BAPs [130]. RuBisCO 407 large subunit-derived peptides ELAAAC (f454-459), and MDN (472-474), as well as the original hydrolysate and portions generated by hydrolyzing RuBisCO with pepsin, all exhibited antimicrobial activity against Gram-positive (L. innocua, Micrococcus luteus, and Bacillus subtilis) and Gram-negative (E. coli) microorganisms [131]. Unquestionably, a revolutionary method for producing BAPs with a variety of positive health effects involves the fermentation by microorganisms of protein from different sources. The BAPs produced by microbial fermentation can be further purified without hydrolysis, and it is less expensive than using enzymes [8].
Gram-positive lactic acid bacteria (LAB) are the source of a wide range of bioactive substances, such as fatty acids, hydrogen peroxide, short-chain peptides, and fatty acids. The importance of LAB in the food and beverage business extends far beyond the manufacture of fermented foods because many of these substances have a bioprotective action against infections and degrading agents [132, 133]. Lactiplantibacillus plantarum, a LAB that is known to produce antimicrobial peptides, has been examined in various investigations to determine whether it has the capacity to inhibit significant foodborne pathogens [134–136]. Research also showed that L. plantarum, cell-free supernatant, and isolated bacteriocins from this strain enhance direct inhibition. In addition, it has been noted that BAPs produced from L. plantarum have the properties of proteolyzing milk proteins [137–139]. S. aureus, L. monocytogenes, E. coli, and S. Typhimurium are only a few of the Gram-positive and Gram-negative foodborne pathogenic organisms that have been found to be inhibited by L. plantarum fermented camel’s milk [137, 140, 141]. In addition, a significant amount of low-molecular-weight antimicrobial peptides were found among which 32 of these peptides came from milk proteins in the most effective fraction [138]. Lactobacillus casei ATCC 334 producing BAP-P1, P2, and P4 in the fermented fat kenaf grain had a strong antibacterial action against S. Typhimurium, E. coli, Pseudomonas aeruginosa, S. aureus, and other microorganisms [142]. Bioactive antimicrobial peptides also exhibit antivirulence property activity against foodborne pathogens at subinhibitory concentrations. Various BAPs have bactericidal effects on biofilm formation and can eradicate infections in animal models [143].
Nanoantimicrobials are frequently utilized to treat bacterial infections directly. Nanoantimicrobials, also known as nanoantibiotics, are nanoparticles exhibiting antimicrobial activity or enhancing the activity of encapsulated antimicrobial agents. Chitosan nanoparticles and peptides, known as CNMs, are outstanding new antibacterial medications that are a promising alternative to antibiotics for use against harmful bacteria. By using a digestive epithelial cell framework, the role of CNMs was assessed in the prevention of E. coli O157 infection. CNMs exhibited good bactericidal effects against E. coli O157, according to antibacterial activity testing [144].
Both Gram-positive and Gram-negative bacteria, including, E. coli, L. monocytogenes, S. aureus, P. aeruginosa, and S. enterica were inhibited by the antibacterial activity of BAPs generated by Bifidobacterium lactis BB-12 and Lactobacillus acidophilus LA-5 in milk model medium and their combination cultures [145]. Figure 1 shows the antimicrobial applications of bioactive peptides.
The primary biotechnological tool for producing Brewer’s or Baker’s biomasses, which are mostly used in the production of fermented foods and beverages, is Saccharomyces cerevisiae. The S. cerevisiae precursor proteins enolase II and glyceraldehyde-3-phosphate dehydrogenase are notable because they released BAPs having antimicrobial properties with the highest scores. In particular, protein-sealing antibacterial peptides that exhibit broad-spectrum activity and may prevent cytotoxicity while also reducing the emergence of microbial resistance ought to be considered a reliable and year-round source for next-generation bioactive substances. S. cerevisiae biomass is a food-grade product that is sold and consumed globally [146].
4. Mode of Action of BAPs against Foodborne Pathogens
Nomura’s 1967 identified two mode of actions of biopeptides [147]. One method showed how bacteria might attach to peptides, creating pores or holes in their cell walls. Another method proposed how contact strength damages the chemical and biological structures of afflicted cells [148]. The interaction of peptides with sensitive cells can occur in two ways: (1) cell wall receptors bind to the peptide molecules and it does not affect the physiological makeup of cells or (2) the impacted cells suffer biological and chemical harm [149]. The interaction between positively charged BAPs and the mannan of fungi, lipoteichoic acid of Gram-positive bacteria, and LPS of Gram-negative bacteria is characterized by a significant affinity [150]. Figures 2 and 3 show the possible antimicrobial mechanisms of BAPs.
4.1. Alteration of Outer Membrane Permeability
BAPs can enter the membrane and perform intracellular functions or permeate the membrane and cause intracellular contents to leak [147, 150]. The interaction of peptides with cell walls is primarily influenced by conformational change and the peptide-lipid ratio [151–154]. In an aqueous solution, alpha-helical peptides attach to the negatively-charged lipid membrane and change its disorganized structure. The stability of disulfide bond bridges in β-sheet peptides is attributed to their lack of conformational changes during interaction with the plasma membrane [155]. The peptide-lipid ratio is another important factor since low values lead peptides to be located parallel to the bacterial cell membrane [156, 157].
Some speculative models of membrane-cavity formation have been put forth, including the barrel-stave, toroidal-pore, carpet, and aggregate models (Figure 2) [147]. In the barrel-stave model, when more peptide binds to the membrane, aggregation and conformational modification take place, leading to a shift in the local phospholipid head groups and thinning of the membrane [68]. During penetration into the phospholipid bilayer, the hydrophilic sections of the peptide helixes face inside, whereas the hydrophobic portions of the β-sheet and α-helical peptides are near the cell membrane phospholipid. The core lumen is formed by paralleling many helical molecules [155]. Unlike the barrel-stave model, the toroidal-pore model involves peptide helices penetrating the cell membrane and interacting with lipids to construct the toroidal-pore complexes. High quantities of locally-gathered peptides cause lipid molecules to bend, which allows both the lipid head groups and peptides anchored inside the core of the lipid to move [68]. While the electrostatic impact of peptides and anionic membrane is essential in the carpet model, significant peptide concentrations must be present to produce micelles and damage the microbial membrane [155]. While the concentration of peptide crosses the threshold, clusters of peptides coat the membrane and break it like a surfactant. In the hydrophobic core of the membrane, neither channel development nor peptide insertion takes place. This action is strong enough to cause cell death by partial or total lysis of the cell membrane [147].
According to the aggregation model, lipids and peptides are compelled to assemble a micelle of the peptide-lipid complex when peptides attach to the anionic cytoplasmic membrane [158]. In comparison to the carpet concept, peptides, lipids, and water in cellular channels allow ions and subcellular components to flow. Cell death results from leakage. These channels might also assist in the transfer of peptides into the cytoplasm, where they can function. This mechanism explains why peptides can act on intracellular substances in addition to the cytoplasmic membrane, which is their primary target [159]. Unlike cationic peptides, the mechanisms underlying anionic peptides are still unknown. Maximin H5’s antimicrobial effect against S. aureus has been believed to underlie membrane dissolution [160]. Other reported modes of action also include membrane destruction. For instance, clavanin A embraces the α-helical peptide membrane permeation mode in neutral pH [161]. However, it causes cell death in slightly acidic pH by acting on membrane proteins that keep a constant pH gradient. An essential step for disrupting microbial surfaces is the LPS anchored in the bacterial pathogen’s outer membrane [162]. The vital role of the synchronized opening movements of the LPS transport (Lpt) β-taco domain and β-barrel of the LPS transport protein has been shown to facilitate the insertion of LPS into the bacterial surface. Since thanatin stabilizes the β-taco domain, LPS cannot be transported to the cell surface [162].
4.1.1. Alteration of the Intracellular Mechanism of Action
Buforin II, a BAP, containing 21 amino acids, displays antibacterial action against a variety of microorganisms [163]. It shares the same sequence as a piece of the protein called histone H2A, which directly engages nucleic acids [163]. Previous studies have shown that buforin II has the capacity to bind to DNA and RNA, as well as penetrate lipid vesicles in vitro, hence potentially affecting the permeability of the membrane [163]. PR-39, a BAP, isolated from the small intestine of pigs and high in proline and arginine, was discovered to quickly permeate the outer membrane of E. coli [164]. After entering the cytoplasm, PR-39 interferes with the synthesis of proteins, leading to the breakdown of proteins essential for the synthesis of DNA. Consequently, this disruption impairs the process of DNA synthesis. Usually, the proline-enriched BAPs attach to ribosomes and obstruct protein production [165].
According to reports, peptides stop a bacterial intracellular enzyme from working. The bacterium heat shock protein DnaK, which was isolated from protein lysates of E. coli and shown to be selectively bound by pyrrhocoricin, was demonstrated by the Otvos’ group [166]. The same team went on to show in a subsequent investigation that pyrrhocoricin prevented DnaK from acting as an ATPase [167]. It was first discovered that human neutrophil peptide-1 could enter both the inner and outer membranes of E. coli and inhibit the making of the bacteria’s DNA, RNA, and proteins [168]. The deadly event, it should be noted, seems to be inner membrane permeabilization. The enzymatic activities of D-Ala-D-Ala ligase and alanine racemase are essential for the biosynthesis of D-Ala-D-Ala dipeptide, a key component of lipid II, that serves as a precursor molecule in the formation of peptidoglycan. The antibacterial activity of bacteria may be restricted by cycloserine via the inhibition of D-Ala-D-Ala ligase and alanine racemase [169].
As BAPs exhibit antibacterial activity by membrane or nonmembrane-mediated action either by increasing membrane permeability or pore formation leading to the leakage of intracellular contents, or penetration into the membrane to exert intracellular actions without targeting specific molecules/pathways, it is unlikely to develop bacterial resistance to BAPs [147, 150]. The maximal H5 engages in interactions with bacteria through its N-terminal helical peptide, while the aspartate residues primarily serve a minimal function. As a result of their separation from the membrane surface, they play an important structural role. The hydrogen bonds created during the acetylation of the N- and C-terminal ends of the peptide are what stabilize its -helix structure [170]. Despite cell membrane disintegration and intracellular efflux, the anionic peptide Xlasp-p1 displays wide antibacterial activity against Gram-positive and Gram-negative bacteria [171].
A milk-derived peptide (AMP SSSEESII from -casein) has been shown in many studies to be able to prevent the development of M. luteus, L. innocua, E. coli, and S. enteritidis. In casein, a different bioactive peptide called IKHQGLPQE reduced the number of harmful microorganisms that are often prevalent in newborn formula [172]. B. subtilis, S. aureus, S. pneumoniae, E. coli, P. aeruginosa, S. dysenteriae, and S. typhimurium have all been reported to be strongly inhibited by the GLSRLFTALK peptide [173]. Mackerel byproducts E. coli and Listeria innocua were both suppressed by SIFIQRFTT [174]. Antioxidant activities [175] and immunomodulation [176] can make BAPs better alternatives for antibiotics [172]. Several haemoglobin-derived peptides possess cytotoxic properties against S. Enteritidis, S. saprophyticus, S. simulants, B. cereus, E. coli, M. luteus, E. faecalis, L. innocua, and S. sonnei. [177, 178].
5. Conclusions and Future Prospects
Several studies have demonstrated the significance of BAPs and their applicability in the pharmacological and pharmaceutical fields. They may also be used in crop development and cosmetology, though to a lesser level [179–183]. These bioactivities, especially the antibacterial potential, can be advantageous to the agri-food sector. This business is constantly in need of the creation of effective and secure substitutes for preservatives and food additives. As a result of the advent of antibiotic resistance, the abuse of antibiotics in livestock farming is additionally a significant worldwide public health issue. Researchers are trying to develop unique, safe, and efficient antimicrobial agents [184–188]. The use of BAPs with antimicrobial capacity appears to be a favorable strategy for concerns relating to both food safety and animal growth promotion [189–191]. With demonstrated action against significant bacteria such as B. subtilis, L. monocytogenes, E. coli, V. parahaemolyticus, P. aeruginosa, S. aureus, K. pneumoniae, and S. enterica, the use of BAPs produced from dietary proteins against foodborne pathogens has a lot of potential. When evaluating the application of BAPs having antimicrobial properties, BAPs as food additives or drugs, it is important to keep in mind that the majority of studies have been conducted in vitro, and further research is required to assess the in vivo combinations and how they interact with food substrates [192]. Another problem is that BAPs may lose their bioactivity as a result of interactions with other food matrix constituents, food manufacturing, or the intestinal environment. Therefore, when developing functional foods containing these peptides, it is necessary to assess the impact of food manufacturing conditions on the biological activity as well as the availability of these peptides. In addition, it is necessary to examine how these peptides interact with other ingredients once they have been added to the food matrix. It is possible to consider the controlled delivery systems such as microparticulate, nanoemulsion, and nanostructured lipid carriers or chemical changes such as the cyclization of the structures of BAPs that are vulnerable to digestive enzymes or thermal treatment [184]. The feasibility of using controlled delivery methods, such as microparticulate, nanoemulsion, and nanostructured lipid carriers, or implementing chemical modifications, such as cyclization of bioactive peptide structures, to protect against the effects of digestive enzymes or heat treatment may be contemplated [193]. BAPs are intriguing compounds with a wide range of uses because of their antioxidant, anticancer, antihypertensive, antihyperpigmentation, anti-inflammatory, antidiabetic, intestine-modulating, hypocholesterolemic, and antibiotic properties, along with others. BAPs can modulate the composition of gut microbiota facilitating the proliferation of those with antiobesity effects that exert antiobesity effects by controlling the energy balance of the host and food intake along with suppressing the growth of proobesity gut bacteria. Future studies should therefore concentrate on encouraging the commercial manufacturing of stable, plant- and microbe-based BAPs that may be used in a variety of food matrices without impairing food quality or bioavailability along with controlling foodborne pathogens. Opportunities and difficulties are constantly interconnected, and sufficient scientific evidence supports the idea that BAPs produced from plant materials and microbial sources may exhibit a variety of biological and functional features, highlighting their enormous potential in the food industry as well as for controlling the emergence of foodborne pathogens in the future.
Data Availability
No data were used to support the study.
Conflicts of Interest
The authors declare that they have no conflicts of interest.
Authors’ Contributions
Anowar Khasru Parvez and Md. Amdadul Huq contributed equally as the first author of this manuscript.