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Baindara, P.;  Mandal, S.M. Plant-Derived Antimicrobial Peptides. Encyclopedia. Available online: https://encyclopedia.pub/entry/26725 (accessed on 21 December 2024).
Baindara P,  Mandal SM. Plant-Derived Antimicrobial Peptides. Encyclopedia. Available at: https://encyclopedia.pub/entry/26725. Accessed December 21, 2024.
Baindara, Piyush, Santi M. Mandal. "Plant-Derived Antimicrobial Peptides" Encyclopedia, https://encyclopedia.pub/entry/26725 (accessed December 21, 2024).
Baindara, P., & Mandal, S.M. (2022, August 31). Plant-Derived Antimicrobial Peptides. In Encyclopedia. https://encyclopedia.pub/entry/26725
Baindara, Piyush and Santi M. Mandal. "Plant-Derived Antimicrobial Peptides." Encyclopedia. Web. 31 August, 2022.
Plant-Derived Antimicrobial Peptides
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This entry is adapted from the peer-reviewed paper 10.3390/foods11162415

Food spoilage is a widespread issue brought on by the undesired growth of microbes in food products. Thousands of tons of usable food or food products are wasted every day due to rotting in different parts of the world. Several food preservation techniques are employed to prevent food from rotting, including the use of natural or manufactured chemicals or substances; however, the issue persists. One strategy for halting food deterioration is the use of plant-derived antimicrobial peptides (AMPs), which have been investigated for possible bioactivities against a range of human, plant, and food pathogens. The food industry may be able to benefit from the development of synthetic AMPs, produced from plants that have higher bioactivity, better stability, and decreased cytotoxicity as a means of food preservation.

plant antimicrobial peptides food preservatives food spoilage

1. Introduction

Food waste caused by microorganisms such as bacteria, fungi, and yeast is on the rise globally in the modern era. The Food and Agriculture Organization (FAO) defines food loss and waste as a “decrease in quality and quantity of food along with the food supply chain.” One-third of the worldwide food supply generated for human consumption, or 1.3 billion tonnes per year, is wasted, according to the World Food Program (WFP). According to a study, food spoiling caused by spoilage bacteria results in a loss of 25% of the food produced globally [1]. Food spoilage is a complex process in which microorganisms play a major role. The process of food spoilage includes the growth and reproduction of microorganisms along with physical, chemical, and enzymatic reactions with food via different processes including, lipid oxidation, proteolysis, starch aging, and postharvest respiration in vegetables, where enzymes such as polyphenol oxidase, pectinase, and lipases are playing important roles [2][3]. The growth of microorganisms during food spoilage depends on the type of substrate available in the food along with water, sugar, salt, oxygen, and nutrient content [4].
Food loss and wastage are still issues despite the adoption of food preservatives and preservation techniques such as cold storage, improved packaging, ionization, and chemical and natural food additives [5]. Chemical food preservatives are extensively used worldwide because of their low cost and straightforward manufacturing procedure. Food preservatives play a crucial part in the fight against food degradation. However, the inappropriate use or prolonged consumption of chemical preservatives including sodium benzoate, sodium nitrate, sodium nitrite, and benzoic acid has been linked to significant health problems [6][7]. Facts about the adverse effects of using chemical preservatives in food result in the development of concern in modern consumer behavior and an increased interest in natural biological preservatives. Essential oils, organic acids, chitosan, plant extracts, and bioactive AMPs from animals, bacteria, and plants are the major interesting alternatives to chemical food preservatives. Research on natural food preservatives has already shown that they may be more effective than chemical food preservatives [8][9]. It is interesting to note that some naturally occurring AMPs and their synthetic analogs have already been employed as food preservatives in the food industry [10].

2. Different Classes of Plant-Derived AMPs

2.1. Defensins

Defensins are universal in the kingdom of plants and are present in all life forms. Defensins are brief peptides that range in size from less than 45 amino acids in length to a molecular weight of about 5 kDa [11][12][13]. Plant defensins are very basic, and the formation of disulfide linkages has been linked to 8–10 cysteine residues [14]. Plant defensins are kept together by four disulfide linkages and have a distinct, three-dimensional structure. According to their 3D structure, plant defensins have a parallel, triple-stranded β-sheet and α-helix [15][16]. Due to their antibacterial and antifungal capabilities, defensins are produced by plants during their reproductive, storage, and stress responses and serve to protect them [17][18].

2.2. 2S Albumins

The term 2S albumin comes from the sedimentation coefficient of the protein. These are storage proteins that are necessary for plant development and growth. Notably, 2S albumins are made up of a large 18–20 kDa precursor peptide that is post-translationally modified through proteolytic cleavage to yield small active peptide fragments [19]. Finally, the processed AMP accumulates in storage vacuoles inside seeds, leaves, and vegetative tissues such as tubercles and has a low molecular weight that ranges from 4 to 9 kDa. Importantly, 2S albumins have been discovered to exhibit antibacterial and antifungal properties [20].

2.3. Glycine-Rich Proteins (GRPs)

GRPs are storage proteins found in the xylem, hypocotyls, stems, and petioles of plants [21]. They are frequently characterized by several glycine-containing motifs and an overall 70% of glycine percentage in the protein. Plants use GRPs to defend themselves against abiotic and biotic stress through their antifungal and antibacterial properties [22].

2.4. Lipid Transfer Proteins (LTPs)

LTPs are lipid carriers that bind monomeric lipid units in a hydrophobic pocket and play essential roles in lipid transfer across donor and acceptor membranes [23]. They are small proteins with a molecular weight of less than 10 kDa. Like defensins, LTPs are cysteine-rich and have four to five α-helices with four disulfide linkages. Several disulfide connections give LTPs their high degree of stability and resistance to heat denaturation [24][25]. Due to their antibacterial qualities, LTPs are recognized to be essential for plant survival and play significant roles in plant breeding [26].

2.5. Snakins

Snakins are low-molecular-weight peptides with 12 cysteine residues that are involved in disulfide bond formation and are highly conserved plant AMPs [27]. They are known to have potent antibacterial and antifungal properties against a variety of plant diseases, as well as being involved in plant development and growth [28].

2.6. Thionins

Thionins are small peptides consisting of 45–48 amino acids with 3–4 disulfide bonds and about 5 kDa of molecular weight. Thionins are usually found in higher plants and are reported to have potent antibacterial and antifungal activities [29].

2.7. Cyclotides

Cyclotides are small cysteine-rich AMPs isolated from plants. They have three characteristic disulfide bonds and usually contain 28–37 amino acids. They are known as cyclotides because of their head-to-tail cyclized peptide bone [30]. Cyclotides have a variety of biological effects, including antibacterial, antifungal, insecticidal, and anticancer effects [31].

2.8. Napins

Napins are low-molecular-weight plant AMPs, with a molecular weight of less than 15 kDa, while two polypeptide chains are linked by disulfide bonds. Like defensins and other plant AMPs, napins are also cysteine-rich peptides [32]. Napins are seed storage proteins with high water solubility [33]. They are reported to have antibacterial, antifungal, and trypsin-inhibiting properties in addition to their role in plant growth and development [34].

3. Antagonistic Effects of Plant-Derived AMPs against Foodborne Pathogens

Plant AMPs could be a potential alternative for biopreservation applications in the food industry. They can be used for the development of high-yielding genetically modified crops with enhanced resistance against plant and foodborne pathogens. Plant AMPs have already been suggested as potential drug sources for human infectious diseases caused by bacteria, viruses, and parasites, and for the treatment of different types of cancers [35][36][37]. Although the use of plant AMPs in a clinical setting requires further in-depth experimental studies, they are suitable potential options for use in the food industry as food preservatives against foodborne pathogens. In the natural environment, plants experience different weather and drought conditions, and therefore, their immune system is developed to efficiently fight against various pathogens, where AMPs play essential roles in their protection [38].
It is interesting to note that using plants and the products in which they are utilized, such as natural medicines and cosmetics, has long been linked to improving human health. Additionally, a number of the pharmaceuticals today are derived from plants [39]. Furthermore, the numerous antibacterial qualities of AMPs generated from plants suggest their potential use in agricultural production [40]. Additionally, the promising antifungal and antibacterial properties of AMPs generated from various plant components have the potential to be developed for biotechnological uses in the food business, such as food preservatives [41][42].
To date, various plant-derived AMPs have been isolated and characterized with enormous structural and functional diversity. PaDef was discovered and extracted from a cDNA library obtained from Mexican avocado fruit. It is a peptide that resembles a defensin. PaDef can be utilized to treat foodborne infections because it has antibacterial action against Escherichia coli and Staphylococcus aureus [43]. Another defensin, J1, was discovered in a cDNA library of bell pepper fruit and demonstrated potent antifungal activity against the Colletotrichum gloeosporioides-induced anthracnose disease of transgenic bell pepper [44][45]. Similar to this, Rs-AFP1 and Rs-AFP2, two defensins isolated from radish seeds, have potent antifungal action [46].
Further, these two defensins were chemically synthesized and reported to have anti-yeast activity against food spoilage yeast Zygosaccharomyces bailii in different beverages [47]. In another study, four closely related cysteine-rich peptides were isolated and characterized from the seeds of Impatiens balsamina (Balsam), showing antifungal and antibacterial activities [48]. Interestingly, these cysteine-rich peptides did not show any cytotoxicity against human cells while exhibiting strong activity against enteric foodborne pathogens including S. aureus, E. coli, Salmonella enterica, Pseudomonas aeruginosa, and Bacillus cereus [49]. Plant-derived AMPs can also be used for the protection of stored grains in warehouses, as reported in a study where a defensin, Cp-thionin-II, isolated from cowpea seeds, was confirmed to protect stored wheat grains from fungal spoilage caused by Fusarium culmorum [50]. MsDef1 and MtDef4 are plant defensins isolated from Medicago sativa, and M. truncatula showed inhibitory activity against F. graminearum, a fungal plant pathogen that caused fusarium head blight of wheat and barley [51].
Another class of AMPs identified in plants is 2S albumin proteins. Pa-AFP-1 is isolated from passion fruit and has been found to efficiently inhibit the development of filamentous fungi, C. gloeosporioides, Trichoderma harzianum, F. oxysporum, and Aspergillus fumigatus [20][52]. CW-1 is another 2S albumin protein, isolated and characterized from Malwa perviflora (Cheeseweed), that is reported to have antifungal activity against F. graminearum [53].
Pg-AMP1 is a glycine-rich peptide that is isolated from guava seeds and has been shown to have potent antibacterial properties against Klebsiella species and Proteus species [54]. A class of plant AMPs called lipid transfer proteins is effective against bacteria, yeast, and fungi. The lipid transfer protein Ca-LTP1, which is isolated from chili pepper seeds, has high antifungal action against C. lindemunthianum and C. tropicalis and may be employed as a food preservative [55].
Another lipid transfer protein identified from sunflower seeds is called Ha-AP10. Ha-AP10 demonstrates strong inhibitory action against the germination of spores of pathogenic fungal pathogens F. solani, indicating its potential use in the food business [56]. Next, a mung bean nsLTP, isolated from mung bean sprouts, has been reported for its potential antifungal activities against various fungi, including F. solani, F. oxysporum, Pythium aphanidermatum, and Sclerotium rolfsii, as well as its antibacterial activity against S. aureus.
Snakin-Z is identified and isolated from Jujube fruits and exhibits potential antibacterial and antifungal activities against S. aureus and Phomopsis azadirachtae, respectively. Interestingly, snakin-Z does not exhibit any cytotoxicity against RBCs and is suggested as a potential plant AMP for therapeutic or food preservation applications [57]. MsSN1 is a snakin-1, isolated and characterized from M. sativa, that exhibits antibacterial and antifungal activity against multiple foodborne pathogens [58].
Next, CaThi is a thionin-like peptide characterized and isolated from chili. CaThi is reported to have antimicrobial, anti-yeast, and antifungal properties against various pathogenic bacteria, including S. cerevisiae, Candida albicans, C. tropicalis, and F. solani [59][60]. Another plant thionin is isolated from the wheat endosperm material that showed antibacterial activities against Corynebacterium michiganense and Xanthomonas campestris, which are known plant pathogens of tomatoes and peppers [61][62]. Another study reported a potent antifungal thionin named thionin 2.4, secreted from Arabidopsis thaliana, which showed antifungal properties against F. graminearum, a serious crop fungal pathogen [63]. TuAMP1 and TuAMP2 are thionin-like peptides that are isolated and characterized from the bulbs of Tulipa gesneriana (Tulip) and exhibit diverse antifungal activity against Agrobacterium rhizogenes, A. radiobacter, Clavibacter michiganensis, Curtobacterium flaccumfaciens, F. oxysporum, and Geotrichum candidum [64].
Cycloviolacin O2 and Cycloviolacin O8 are cyclotides isolated and characterized from Viola odorata, which showed potential antibacterial activity against various pathogenic bacteria [65][66]. Additionally, parigidin-br1, a cyclotide isolated from Palicourea rigida, is reported to have potent insecticidal activity against neonate larvae of Lepidoptera (Diatraea saccharalis), a sugarcane insect [67]. This suggests that plant-derived AMPs can also be developed as biopesticides for direct applications in food crops.
An α-hairpin-like peptide, LuffinP1, isolated and characterized from the seed of Luffa cylindrica (Sponge gourd), showed potential protein translational inhibitory activity [68]. Bleogen pB1 is a hevein-like peptide isolated from Cactus fruits and has been reported to have potent inhibitory activity against C. albicans and C. tropicalis [69]. Next, two hevein-like peptides, EAFP1 and EAP1, isolated and characterized from the bark of Eucommia ulmoides, exhibit broad inhibitory activity against eight pathogenic fungi from cotton, wheat, potato, tomato, and tobacco [70]. Another hevein-like peptide, Ee-CBP, was purified and characterized from the bark of Euonymus europaeus and showed broad-spectrum antifungal activity against various plant pathogenic fungi [71]. SmAMP3 is a novel hevein-like peptide that is isolated from leaves of Stellaria media and has been reported to have potent inhibitory activity against plant pathogenic fungi [72].
Napins are another class of plant AMPs that show promising results to be used as food preservatives. Em2-F18 is a napin-like peptide isolated and characterized from the seed of Jambu fruits, confirmed to have potential antibacterial activities against foodborne pathogens, such as S. aureus and S. enteritidis [73]. Another napin, Tn-AFP1, was identified from the Water chestnut and found to have antifungal activity against F. oxysporum, Mycosphaerella arachidicola, and Physalospora piricola through its inhibition of fungal mycelial growth [74]. Mandal et al. identified and characterized two other napin-like peptides, Cn-AMP1 and Cn-AMP2, from green coconut, which were found to exhibit potent antifungal activity against C. tropicalis [75].
Knottin-type peptides are another class of plant-derived AMPs that show strong antifungal properties against foodborne pathogens. PAFP-S is a knottin-like peptide isolated from the seeds of Phytolacca Americana and exhibits antifungal activities against F. oxysporum and Pyricularia oryzae, which are common crop pathogens of legumes, rice, and barley [76]. Mj-AMP1 and Mj-AMP2 are other knottins isolated from the seeds of Mirabilis jalapa and exhibit potential antifungal activity against major pathogenic fungal species, including F. oxysporum, which causes significant loss to crops [77]. Many unclassified plant AMPs, in addition to the known classes of plant AMPs, have the potential to be used in the food sector. A plant AMP called Cn-AMP3 was discovered in coconut water and demonstrated promising antibacterial properties against various bacterial species [78]. The aforementioned examples collectively show the potential of plant-derived AMPs against several plant diseases and foodborne pathogens, which can be further developed as food preservatives in the future food industry to prevent food spoiling or loss.

4. Applications of Plant-Derived AMPs in the Food Industry

Plant-derived AMPs have been proven to possess strong antibacterial capabilities against bacteria, yeast, and fungi, pointing to the possibility of using them in the future to create food preservatives for the food industry. However, natural plant AMPs have several disadvantages that prevent their usage in culinary applications. The main drawbacks of natural plant AMPs include poor chemical stability, astringent flavor, short-term effectiveness, and cytotoxicity. Despite all the negative aspects, plant AMPs can be altered or enhanced for use as food preservatives through chemical synthesis and the addition of delivery techniques such as encapsulation, nanoparticles, or edible packaging [41][79]. With recent developments in technology and scientific advancement, some of the natural plant AMPs have been modified and used in the food industry with improved efficacy. In a recent study, glycinin basic polypeptides (GBPs) were isolated from soybean and found to have strong antifungal properties against A. niger and Penicillium sp. by inhibiting fungal mycelial growth, spore germination, and plasma membrane disruption via inhibition of ergosterol synthesis. By improving the sensory qualities of fresh, wet noodles, this GBP intriguingly demonstrated possible food preservation characteristics and has been proposed as a potential tool for extending the shelf life of starchy foods [80]. Ning et al. demonstrated the effects of soybean GPB’s preservation properties on the Scomberomorus niphonius surimi (Japanese Spanish Mackerel). In a 24-day experiment, it was proven that GBP enhanced texture and prevented microbiological growth, extending the overall shelf life of surimi when stored [81].
Another study aiming at the evaluation of food preservative capacities of legumes (pea, lentil, and fava bean flours) reported the potent antifungal activity of this native flour mixture against multiple species of Aspergillus and Penicillium. Further, purification confirmed the presence of nine native peptides in the legume flour mixture. A purified blend of these nine peptide mixtures was used to make bread under pilot plant conditions, which showed a longer shelf-life in comparison to the control bread [82]. In another study, the same group found the antifungal activity of pea hydrolysate against P. roqueforti and found the mixture of active components as a blend of pea defensins, lipid transfer proteins, and other peptides. They synthesized the identified peptides and found that this mixture is efficiently able to enhance the shelf-life of bread up to the storage period of 21 days [83]. Low-molecular-weight peptides that have the ability to extend the shelf life of starchy foods and exhibit antifungal action were also discovered to be produced during the fermentation of plant products. Palm kernel cake is fermented via solid-state Lacto-fermentation by using Lactobacillus casei. The generated fermentation product was identified as a mixture of peptides produced by Palm kernels and bacteria. The peptide mixture was reported to have antifungal activity against Aspergillus sp., Fusarium sp., and Penicillium sp. while also found to enhance the shelf-life of whole wheat bread slices for a storage period of 10 days [84].
Another method for producing plant-derived AMPs on a large scale is recombinant expression. Huang et. al. confirmed the recombinant expression and production of Ac-AMP2, a plant AMPs, originally produced by Amaranthus caudatus (an annual flowering plant), and MiAMP1, a highly basic protein from the nut kernel of Macadamia integrifolia. The recombinant strains of Pichia pastoris (GS115/Ac-AMP2 and GS115/MiAMP1) expressing these peptides showed potential post-harvest food preservation properties in pears infected with the fungal pathogen P. expansum [85].
Another method for preserving food during lengthy storage is to use food preservation films coated with AMPs. By using several encapsulation techniques such as liposomes, emulsions, biopolymer particles, nanofibers, and nanofilms, plant AMPs can be employed in active food packaging [10]. A recent study created and tested double-layered furcellaran/gelatin hydrolysate films containing the Ala-Tyr peptide for the preservation of frozen fish. No bacterial growth or oxidation was seen throughout the lengthy four-month storage period at −18 °C [86].

References

  1. Bondi, M.; Messi, P.; Halami, P.M.; Papadopoulou, C.; De Niederhausern, S. Emerging microbial concerns in food safety and new control measures. Biomed Res. Int. 2014, 2014, 251512.
  2. Poghossian, A.; Geissler, H.; Schöning, M.J. Rapid methods and sensors for milk quality monitoring and spoilage detection. Biosens. Bioelectron. 2019, 140, 111272.
  3. Sevindik, M.; Uysal, I. Food spoilage and Microorganisms. Turk. J. Agric. Food Sci. Technol. 2021, 9, 1921–1924.
  4. Doyle, M.P.; Diez-Gonzalez, F.; Hill, C. Food Microbiology: Fundamentals and Frontiers; ASM Press: Washington, DC, USA, 2019; ISBN 9781683670476.
  5. Varzakas, T.; Tsarouhas, P. Advances in food processing (Food preservation, food safety, quality and manufacturing processes). Appl. Sci. 2021, 11, 5417.
  6. Sweis, I.E.; Cressey, B.C. Potential role of the common food additive manufactured citric acid in eliciting significant inflammatory reactions contributing to serious disease states: A series of four case reports. Toxicol. Rep. 2018, 5, 808–812.
  7. AL-Mamun, M.; Chowdhury, T.; Biswas, B.; Absar, N. Food Poisoning and Intoxication: A Global Leading Concern for Human Health. In Food Safety and Preservation; Elsevier: Amsterdam, The Netherlands, 2018; pp. 307–352.
  8. Silveira, R.F.; Roque-Borda, C.A.; Vicente, E.F. Antimicrobial peptides as a feed additive alternative to animal production, food safety and public health implications: An overview. Anim. Nutr. 2021, 7, 896–904.
  9. Baptista, R.C.; Horita, C.N.; Sant’Ana, A.S. Natural products with preservative properties for enhancing the microbiological safety and extending the shelf-life of seafood: A review. Food Res. Int. 2020, 127, 108762.
  10. Liu, Y.; Sameen, D.E.; Ahmed, S.; Dai, J.; Qin, W. Antimicrobial peptides and their application in food packaging. Trends Food Sci. Technol. 2021, 112, 471–483.
  11. Baindara, P.; Gautam, A.; Raghava, G.P.S.; Korpole, S. Anticancer properties of a defensin like class IId bacteriocin Laterosporulin10. Sci. Rep. 2017, 7, 46541.
  12. Baindara, P.; Nayudu, N.; Korpole, S. Whole genome mining reveals a diverse repertoire of lanthionine synthetases and lanthipeptides among the genus Paenibacillus. J. Appl. Microbiol. 2020, 128, 473–490.
  13. Baindara, P.; Kapoor, A.; Korpole, S.; Grover, V. Cysteine-rich low molecular weight antimicrobial peptides from Brevibacillus and related genera for biotechnological applications. World J. Microbiol. Biotechnol. 2017, 33, 124.
  14. Thomma, B.P.H.J.; Cammue, B.P.A.; Thevissen, K. Plant defensins. Planta 2002, 216, 193–202.
  15. Meindre, F.; Lelie, D.; Loth, K.; Mith, O.; Aucagne, V.; Berthomieu, P.; Marquès, L.; Delmas, A.F.; Landon, C.; Paquet, F. The nuclear magnetic resonance solution structure of the synthetic AhPDF1.1b plant defensin evidences the structural feature within the γ-Motif. Biochemistry 2014, 53, 7745–7754.
  16. Francisco, A.G.C.; Georgina, E. Structural Motifs in Class I and Class II Plant Defensins for Phospholipid Interactions:Intriguing Role of Ligand Binding and Modes of Action. J. Plant Physiol. Pathol. 2017, 5, 1000159.
  17. Contreras, G.; Shirdel, I.; Braun, M.S.; Wink, M. Defensins: Transcriptional regulation and function beyond antimicrobial activity. Dev. Comp. Immunol. 2020, 104, 103556.
  18. Sathoff, A.E.; Velivelli, S.; Shah, D.M.; Samac, D.A. Plant defensin peptides have antifungal and antibacterial activity against human and plant pathogens. Phytopathology 2019, 109, 402–408.
  19. Ericson, M.L.; Rodin, J.; Lenman, M.; Glimelius, K.; Josefsson, L.G.; Rask, L. Structure of the rapeseed 1.7 S storage protein, napin, and its precursor. J. Biol. Chem. 1986, 261, 14576–14581.
  20. Ribeiro, S.M.; Almeida, R.G.; Pereira, C.A.A.; Moreira, J.S.; Pinto, M.F.S.; Oliveira, A.C.; Vasconcelos, I.M.; Oliveira, J.T.A.; Santos, M.O.; Dias, S.C.; et al. Identification of a Passiflora alata Curtis dimeric peptide showing identity with 2S albumins. Peptides 2011, 32, 868–874.
  21. Souza Cândido, E.; Pinto, M.F.S.; Pelegrini, P.B.; Lima, T.B.; Silva, O.N.; Pogue, R.; Grossi de Sá, M.F.; Franco, O.L. Plant storage proteins with antimicrobial activity: Novel insights into plant defense mechanisms. FASEB J. 2011, 25, 3290–3305.
  22. Czolpinska, M.; Rurek, M. Plant glycine-rich proteins in stress response: An emerging, still prospective story. Front. Plant Sci. 2018, 9, 302.
  23. De Carvalho, A.O.; Gomes, V.M. Role of plant lipid transfer proteins in plant cell physiology-A concise review. Peptides 2007, 28, 1144–1153.
  24. Molina, A.; Segura, A.; García-Olmedo, F. Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Lett. 1993, 316, 119–122.
  25. Nazeer, M.; Waheed, H.; Saeed, M.; Ali, S.Y.; Choudhary, M.I.; Ul-Haq, Z.; Ahmed, A. Purification and Characterization of a Nonspecific Lipid Transfer Protein 1 (nsLTP1) from Ajwain (Trachyspermum ammi) Seeds. Sci. Rep. 2019, 9, 4148.
  26. Salminen, T.A.; Blomqvist, K.; Edqvist, J. Lipid transfer proteins: Classification, nomenclature, structure, and function. Planta 2016, 244, 971–997.
  27. Mansour, S.C.; Pena, O.M.; Hancock, R.E.W. Host defense peptides: Front-line immunomodulators. Trends Immunol. 2014, 35, 443–450.
  28. Su, T.; Han, M.; Cao, D.; Xu, M. Molecular and biological properties of snakins: The foremost cysteine-rich plant host Defense peptides. J. Fungi 2020, 6, 220.
  29. Höng, K.; Austerlitz, T.; Bohlmann, T.; Bohlmann, H. The thionin family of antimicrobial peptides. PLoS ONE 2021, 16, e0254549.
  30. Craik, D.J.; Daly, N.L.; Bond, T.; Waine, C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J. Mol. Biol. 1999, 294, 1327–1336.
  31. Grover, T.; Mishra, R.; Bushra; Gulati, P.; Mohanty, A. An insight into biological activities of native cyclotides for potential applications in agriculture and pharmaceutics. Peptides 2021, 135, 170430.
  32. Byczyńska, A.; Barciszewski, J. The biosynthesis, structure and properties of napin—The storage protein from rape seeds. J. Plant Physiol. 1999, 154, 417–425.
  33. Shewry, P.R.; Napier, J.A.; Tatham, A.S. Seed storage proteins: Structures and biosynthesis. Plant Cell 1995, 7, 945–956.
  34. Mignone, G.; Shwaiki, L.N.; Arendt, E.K.; Coffey, A. Isolation of the mustard Napin protein Allergen Sin a 1 and characterisation of its antifungal activity. Biochem. Biophys. Rep. 2022, 29, 101208.
  35. Hancock, R.E.W. Cationic antimicrobial peptides: Towards clinical applications. Expert Opin. Investig. Drugs 2000, 9, 1723–1729.
  36. Zhang, Q.Y.; Yan, Z.B.; Meng, Y.M.; Hong, X.Y.; Shao, G.; Ma, J.J.; Cheng, X.R.; Liu, J.; Kang, J.; Fu, C.Y. Antimicrobial peptides: Mechanism of action, activity and clinical potential. Mil. Med. Res. 2021, 8, 48.
  37. Guzmán-Rodríguez, J.J.; Ochoa-Zarzosa, A.; López-Gómez, R.; López-Meza, J.E. Plant antimicrobial peptides as potential anticancer agents. Biomed Res. Int. 2015, 2015, 735087.
  38. Lacerda, A.F.; Vasconcelos, É.A.R.; Pelegrini, P.B.; Grossi de Sa, M.F. Antifungal defensins and their role in plant defense. Front. Microbiol. 2014, 5, 116.
  39. Clark, A.M. Natural products as a resource for new drugs. Pharm. Res. 1996, 13, 1133–1141.
  40. Nor, Y.A.; Johari, F.; Ariffin, F.N.K.; Mohd Ali, A.M.; Khairudin, N.H. Antimicrobial applications in agriculture: A review. J. Pure Appl. Microbiol. 2018, 12, 1829–1838.
  41. Shwaiki, L.N.; Lynch, K.M.; Arendt, E.K. Future of antimicrobial peptides derived from plants in food application – A focus on synthetic peptides. Trends Food Sci. Technol. 2021, 112, 312–324.
  42. Meneguetti, B.T.; dos Machado, L.S.; Oshiro, K.G.N.; Nogueira, M.L.; Carvalho, C.M.E.; Franco, O.L. Antimicrobial peptides from fruits and their potential use as biotechnological Tools-A review and outlook. Front. Microbiol. 2017, 7, 2136.
  43. Guzmán-Rodríguez, J.J.; López-Gómez, R.; Suárez-Rodríguez, L.M.; Salgado-Garciglia, R.; Rodríguez-Zapata, L.C.; Ochoa-Zarzosa, A.; López-Meza, J.E. Antibacterial activity of defensin PaDef from avocado fruit (Persea americana var. drymifolia) expressed in endothelial cells against Escherichia coli and Staphylococcus aureus. Biomed. Res. Int. 2013, 2013, 986273.
  44. Meyer, B.; Houlné, G.; Pozueta-Romero, J.; Schantz, M.L.; Schantz, R. Fruit-specific expression of a defensin-type gene family in bell pepper: Upregulation during ripening and upon wounding. Plant Physiol. 1996, 112, 615–622.
  45. Seo, H.H.; Park, S.; Park, S.; Oh, B.J.; Back, K.; Han, O.; Kim, J.I.; Kim, Y.S. Overexpression of a defensin enhances resistance to a fruit-specific anthracnose fungus in pepper. PLoS ONE 2014, 9, e97936.
  46. Terras, F.R.G.; Schoofs, H.M.E.; De Bolle, M.F.C.; Van Leuven, F.; Rees, S.B.; Vanderleyden, J.; Cammue, B.P.A.; Broekaert, W.F. Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J. Biol. Chem. 1992, 267, 15301–15309.
  47. Shwaiki, L.N.; Arendt, E.K.; Lynch, K.M. Anti-yeast activity and characterisation of synthetic radish peptides Rs-AFP1 and Rs-AFP2 against food spoilage yeast: Synthetic radish peptides against food spoilage yeast. Food Control 2020, 113, 107178.
  48. Tailor, R.H.; Acland, D.P.; Attenborough, S.; Cammue, B.P.A.; Evans, I.J.; Osborn, R.W.; Ray, J.A.; Rees, S.B.; Broekaert, W.F. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein. J. Biol. Chem. 1997, 272, 24480–24487.
  49. Wu, W.H.; Di, R.; Matthews, K.R. Activity of the plant-derived peptide Ib-AMP1 and the control of enteric foodborne pathogens. Food Control 2013, 33, 142–147.
  50. Schmidt, M.; Arendt, E.K.; Thery, T.L.C. Isolation and characterisation of the antifungal activity of the cowpea defensin Cp-thionin II. Food Microbiol. 2019, 82, 504–514.
  51. Sagaram, U.S.; Pandurangi, R.; Kaur, J.; Smith, T.J.; Shah, D.M. Structure-activity determinants in antifungal plant defensins msdef1 and mtdef4 with different modes of action against fusarium graminearum. PLoS ONE 2011, 6, e18550.
  52. Pelegrini, P.B.; Noronha, E.F.; Muniz, M.A.R.; Vasconcelos, I.M.; Chiarello, M.D.; Oliveira, J.T.A.; Franco, O.L. An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins. Biochim. Biophys. Acta Proteins Proteom. 2006, 1764, 1141–1146.
  53. Wang, X.; Bunkers, G.J. Potent heterologous antifungal proteins from cheeseweed (Malva parviflora). Biochem. Biophys. Res. Commun. 2000, 279, 669–673.
  54. Pelegrini, P.B.; Murad, A.M.; Silva, L.P.; dos Santos, R.C.P.; Costa, F.T.; Tagliari, P.D.; Bloch, C.; Noronha, E.F.; Miller, R.N.G.; Franco, O.L. Identification of a novel storage glycine-rich peptide from guava (Psidium guajava) seeds with activity against Gram-negative bacteria. Peptides 2008, 29, 1271–1279.
  55. Diz, M.S.; Carvalho, A.O.; Ribeiro, S.F.F.; Da Cunha, M.; Beltramini, L.; Rodrigues, R.; Nascimento, V.V.; Machado, O.L.T.; Gomes, V.M. Characterisation, immunolocalisation and antifungal activity of a lipid transfer protein from chili pepper (Capsicum annuum) seeds with novel α-amylase inhibitory properties. Physiol. Plant. 2011, 142, 233–246.
  56. Regente, M.C.; De la Canal, L. Purification, characterization and antifungal properties of a lipid-transfer protein from sunflower (Helianthus annuus) seeds. Physiol. Plant. 2000, 110, 158–163.
  57. Daneshmand, F.; Zare-Zardini, H.; Ebrahimi, L. Investigation of the antimicrobial activities of Snakin-Z, a new cationic peptide derived from Zizyphus jujuba fruits. Nat. Prod. Res. 2013, 27, 2292–2296.
  58. García, A.N.; Ayub, N.D.; Fox, A.R.; Gómez, M.C.; Diéguez, M.J.; Pagano, E.M.; Berini, C.A.; Muschietti, J.P.; Soto, G. Alfalfa snakin-1 prevents fungal colonization and probably coevolved with rhizobia. BMC Plant Biol. 2014, 14, 248.
  59. Taveira, G.B.; Da Motta, O.V.; Machado, O.L.T.; Rodrigues, R.; Carvalho, A.O.; Teixeira-Ferreira, A.; Perales, J.; Vasconcelos, I.M.; Gomes, V.M. Thionin-like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts. Biopolym. Pept. Sci. Sect. 2014, 102, 30–39.
  60. Taveira, G.B.; Mello, É.O.; Carvalho, A.O.; Regente, M.; Pinedo, M.; de La Canal, L.; Rodrigues, R.; Gomes, V.M. Antimicrobial activity and mechanism of action of a thionin-like peptide from Capsicum annuum fruits and combinatorial treatment with fluconazole against Fusarium solani. Biopolymers 2017, 108, e23008.
  61. Mak, A.S.; Jones, B.L. The amino acid sequence of wheat β purothionin. Can. J. Biochem. 1976, 54, 835–842.
  62. Fernandez de Caleya, R.; Gonzalez-Pascual, B.; García-Olmedo, F.; Carbonero, P. Susceptibility of phytopathogenic bacteria to wheat purothionins in vitro. Appl. Microbiol. 1972, 23, 998–1000.
  63. Asano, T.; Miwa, A.; Maeda, K.; Kimura, M.; Nishiuchi, T. The Secreted Antifungal Protein Thionin 2.4 in Arabidopsis thaliana Suppresses the Toxicity of a Fungal Fruit Body Lectin from Fusarium graminearum. PLoS Pathog. 2013, 9, e1003581.
  64. Fujimura, M.; Ideguchi, M.; Minami, Y.; Watanabe, K.; Tadera, K. Purification, characterization, and sequencing of novel antimicrobial peptides, Tu-AMP 1 and Tu-AMP 2, from bulbs of tulip (Tulipa gesneriana L.). Biosci. Biotechnol. Biochem. 2004, 68, 571–577.
  65. Zarrabi, M.; Dalirfardouei, R.; Sepehrizade, Z.; Kermanshahi, R.K. Comparison of the antimicrobial effects of semipurified cyclotides from Iranian Viola odorata against some of plant and human pathogenic bacteria. J. Appl. Microbiol. 2013, 115, 367–375.
  66. Pränting, M.; Lööv, C.; Burman, R.; Göransson, U.; Andersson, D.I. The cyclotide cycloviolacin O2 from Viola odorata has potent bactericidal activity against Gram-negative bacteria. J. Antimicrob. Chemother. 2010, 65, 1964–1971.
  67. Pinto, M.F.S.; Fensterseifer, I.C.M.; Migliolo, L.; Sousa, D.A.; De Capdville, G.; Arboleda-valencia, J.W.; Colgrave, M.L.; Craik, D.J.; Magalhães, B.S.; Dias, S.C.; et al. Identification and Structural Characterization of Novel Cyclotide with Activity against an Insect Pest of Sugar Cane. J. Biol. Chem. 2012, 287, 134–147.
  68. Li, F.; Yang, X.X.; Xia, H.C.; Zeng, R.; Hu, W.G.; Li, Z.; Zhang, Z.C. Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica. Peptides 2003, 24, 799–805.
  69. Loo, S.; Kam, A.; Xiao, T.; Tam, J.P. Bleogens: Cactus-derived anti-candida cysteine-rich peptides with three different precursor arrangements. Front. Plant Sci. 2017, 8, 2162.
  70. Huang, R.H.; Xiang, Y.; Liu, X.Z.; Zhang, Y.; Hu, Z.; Wang, D.C. Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv. FEBS Lett. 2002, 521, 87–90.
  71. Van Den Bergh, K.P.B.; Proost, P.; Van Damme, J.; Coosemans, J.; Van Damme, E.J.M.; Peumans, W.J. Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.). FEBS Lett. 2002, 530, 181–185.
  72. Rogozhin, E.A.; Slezina, M.P.; Slavokhotova, A.A.; Istomina, E.A.; Korostyleva, T.V.; Smirnov, A.N.; Grishin, E.V.; Egorov, T.A.; Odintsova, T.I. A novel antifungal peptide from leaves of the weed Stellaria media L. Biochimie 2015, 116, 125–132.
  73. da Silva Dantas, C.C.; de Souza, E.L.; Cardoso, J.D.; de Lima, L.A.; de Sousa Oliveira, K.; Migliolo, L.; Dias, S.C.; Franco, O.L.; Magnani, M. Identification of a Napin-Like Peptide from Eugenia malaccensis L. Seeds with Inhibitory Activity Toward Staphylococcus aureus and Salmonella enteritidis. Protein J. 2014, 33, 549–556.
  74. Wang, H.X.; Ng, T.B. An antifungal peptide from the coconut. Peptides 2005, 26, 2392–2396.
  75. Mandal, S.M.; Migliolo, L.; Franco, O.L.; Ghosh, A.K. Identification of an antifungal peptide from Trapa natans fruits with inhibitory effects on Candida tropicalis biofilm formation. Peptides 2011, 32, 1741–1747.
  76. Shao, F.; Hu, Z.; Xiong, Y.M.; Huang, Q.Z.; Chun-Guang, W.; Zhu, R.H.; Wang, D.C. A new antifungal peptide from the seeds of Phytolacca americana: Characterization, amino acid sequence and cDNA cloning. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1999, 1430, 262–268.
  77. Cammue, B.P.A.; De Bolle, M.F.C.; Terras, F.R.G.; Proost, P.; Van Damme, J.; Rees, S.B.; Vanderleyden, J.; Broekaert, W.F. Isolation and characterization of a novel class of plant antimicrobial peptides from Mirabilis jalapa L. seeds. J. Biol. Chem. 1992, 267, 2228–2233.
  78. Mandal, S.M.; Dey, S.; Mandal, M.; Sarkar, S.; Maria-Neto, S.; Franco, O.L. Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water. Peptides 2009, 30, 633–637.
  79. Zhang, S.; Luo, L.; Sun, X.; Ma, A. Bioactive Peptides: A Promising Alternative to Chemical Preservatives for Food Preservation. J. Agric. Food Chem. 2021, 69, 12369–12384.
  80. Hou, J.; Li, Y.Q.; Wang, Z.S.; Sun, G.J.; Mo, H.Z. Applicative effect of glycinin basic polypeptide in fresh wet noodles and antifungal characteristics. LWT Food Sci. Technol. 2017, 83, 267–274.
  81. Ning, H.Q.; Wang, Z.S.; Li, Y.Q.; Tian, W.L.; Sun, G.J.; Mo, H.Z. Effects of glycinin basic polypeptide on the textural and physicochemical properties of Scomberomorus niphonius surimi. LWT 2019, 114, 108328.
  82. Rizzello, C.G.; Verni, M.; Bordignon, S.; Gramaglia, V.; Gobbetti, M. Hydrolysate from a mixture of legume flours with antifungal activity as an ingredient for prolonging the shelf-life of wheat bread. Food Microbiol. 2017, 64, 72–82.
  83. Rizzello, C.G.; Lavecchia, A.; Gramaglia, V.; Gobbetti, M. Long-term fungal inhibition by Pisum sativum flour hydrolysate during storage of wheat flour bread. Appl. Environ. Microbiol. 2015, 81, 4195–4206.
  84. Mohamad Asri, N.; Muhialdin, B.J.; Zarei, M.; Saari, N. Low molecular weight peptides generated from palm kernel cake via solid state lacto-fermentation extend the shelf life of bread. LWT 2020, 134, 110206.
  85. Huang, Y.; Gao, L.; Lin, M.; Yu, T. Recombinant expression of antimicrobial peptides in Pichia pastoris: A strategy to inhibit the Penicillium expansum in pears. Postharvest Biol. Technol. 2021, 171, 111298.
  86. Jamróz, E.; Kulawik, P.; Tkaczewska, J.; Guzik, P.; Zając, M.; Juszczak, L.; Krzyściak, P.; Turek, K. The effects of active double-layered furcellaran/gelatin hydrolysate film system with Ala-Tyr peptide on fresh Atlantic mackerel stored at −18 °C. Food Chem. 2021, 338, 127867.
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Subjects: Biotechnology & Applied Microbiology
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Piyush Baindara
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Santi M. Mandal
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