Encyclopedia
Please note this is a comparison between Version 2 by Wendy Huang and Version 1 by Tsun-Thai Chai.
Numerous bioactive peptides have been identified from edible insect species, including peptides that were enzymatically liberated from insect proteins and endogenous peptides that occur naturally in insects. The peptides exhibited diverse bioactivities, encompassing antioxidant, anti-angiotensin-converting enzyme, anti-dipeptidyl peptidase-IV, anti-glucosidase, anti-lipase, anti-lipoxygenase, anti-cyclooxygenase, anti-obesity, and hepatoprotective activities. Such findings point to their potential contribution to solving human health problems related to inflammation, free radical damage, diabetes, hypertension, and liver damage, among others. Bioactive peptides may have a positive impact on body functions and thus benefit human health. New information reporting their beneficial effects on the health of livestock and plants is also emerging. Bioactive peptides may be produced endogenously in humans, animals, and plants.
- antioxidant
- antimicrobial
- bioactivity
- entomophagy
- livestock
- nutraceutical
- peptide purification
- protein hydrolysate
- protein hydrolysate
1. Introduction
Bioactive peptides may have a positive impact on body functions and thus benefit human health [1,2][1][2]. New information reporting their beneficial effects on the health of livestock and plants is also emerging. Bioactive peptides may be produced endogenously in humans, animals, and plants. Furthermore, such peptides can also be released from protein sources by enzymatic hydrolysis or prepared by chemical synthesis [3,4][3][4]. While bioactive peptides identified from hydrolyzed food proteins often range between two and twenty amino acid residues, longer endogenous peptides that occur naturally in humans and animals have been discovered [5]. The composition and sequence of amino acids determine the activity of bioactive peptides [6]. Bioactive peptides play important roles in the cardiovascular, immune, nervous, digestive, and endocrine systems. They represent a new generation of bioactive regulators, displaying hormone or drug-like activities, and exhibiting antioxidant, anticancer, antithrombotic, antihypertensive, anti-obesity, anti-inflammatory, opioid, mineral binding, immunomodulatory, antiaging, and antimicrobial effects [7,8,9,10,11][7][8][9][10][11]. Bioactive peptides exhibit high specificity in terms of target tissues and consequently possess low or no toxicity. Importantly, they are effective at even relatively low concentrations, which is especially important in the treatment of chronic diseases [5].
2. Purification and Identification of Bioactive Peptides from Insect Protein Hydrolysates
In the past 10 years, enzymatic hydrolysis has been frequently adopted as a means of producing bioactive peptides from the proteins of edible insects. In such studies, silkworm pupae were relatively popular for the purpose of bioactive peptide discovery [29,30,31,32,33][12][13][14][15][16]. Figure 1 shows a general workflow employed by many studies in the discovery of bioactive peptides.
Figure 1.
General workflow commonly adopted by researchers in the discovery of bioactive peptides from insect protein hydrolysates.
Among the numerous commercially available proteases, alcalase, flavourzyme, and Promod 278P were found to effectively generate functional hydrolysate/peptides from edible insects, leading to the discovery of antioxidant, anti-angiotensin-converting enzyme (ACE), anti-dipeptidyl peptidase-IV (DPP-IV), anti-obesity and hepatoprotective peptides (Table 1). However, alcalase received the most attention as it produced more potent peptides [29,30,34][12][13][17]. This could be because alcalase exhibits both endo- and exo-protease activities, which allows a broad specificity in hydrolysis sites [29][12], thus providing relatively extensive hydrolysis of the insect proteins. Furthermore, some studies used multiple proteases to generate insect protein hydrolysates, either through sequential hydrolysis with different proteases or in vitro simulation of gastrointestinal digestion in which a combination of multiple gastrointestinal proteases was used. Such use of multiple proteases could improve the degree of hydrolysis and yield more low-molecular-weight peptides when compared to only using a single enzyme in the hydrolysis of insect proteins [31,32,33,35][14][15][16][18].
Table 1.
Examples of purification and identification methodologies used in the discovery of bioactive peptides from insect hydrolysates.
| Insect | Peptide Sequence (Validated Activity) | Enzymatic Hydrolysis | Peptide Purification Strategy | Peptide Identification | Reference |
|---|---|---|---|---|---|
| Larva of the Japanese rhinoceros beetle ( | Allomyrina dichotoma | ) | EIAQDFKTDL (Anti-obesity) AGLQFPVGR (Hepatoprotective) |
Promod 278P *, pepsin, trypsin, protease NP, pancreatin, alphalase NP, alkaline protease, alcalase, neutrase, protamex |
45,46][23][24][25]. As a result, the development of agents that reduce oxidative stress has piqued the interest of both academic research and the pharmaceutical industry. Many antioxidant peptides have been isolated from edible insects. Most of the examined edible insects’ antioxidant capacities were investigated primarily using 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays. The peptide FDPFPK is one of the most potent antioxidant peptides among those listed in Table 2. This synthetic peptide isolated from baked locusts (Schistocerca gregaria) showed strong ABTS•+ and DPPH• scavenging capacity with IC50 values of 0.08 and 0.35 mg/mL, respectively [47,48][26][27]. The antioxidant activity of Egyptian cotton leafworm hydrolysate produced by simulated gastrointestinal digestion (SGD) has been studied more thoroughly using cellular and in vivo antioxidant assays [49][28]. The in vivo Caenorhabditis elegans antioxidant model is regarded as an effective model organism for nutritional evaluation, including bioactive peptides. These nematodes have advantages over other in vivo models due to their short life span and, most notably, their high level of gene conservation relative to humans. Therefore, the antioxidant activity of Egyptian cotton leafworm hydrolysate, as measured by the in vivo Caenorhabditis elegans antioxidant model, could be regarded as promising and potentially translatable for human health applications.
Table 2.
Edible insects used for the generation of bioactive peptides and their potential applications in human health management.
| Insect | Peptide/Hydrolysate | Bioactivity * | Potential Application | References | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cricket ( | Gryllodes sigillatus | ) | IIAPPER |
|
|
|
Anti-hypertension, antidiabetic, weight control, antioxidant, and anti-inflammation | [47,48] | [26][27] | [36,37] | [19][20] | ||||||
| Larva of the white-spotted flower chafer ( | Protaetia brevitarsis | ) | SY, PF, YPY, WI (Anti-ACE) |
||||||||||||||
| LAPSTIK |
| Flavourzyme |
|
|
| [38] | [21] | ||||||||||
| Mealworm ( | Tenebrio molitor | ) | LPDQWDWR, APPDGGFWEWGD (Anti-DPP-IV) |
Flavourzyme *, alcalase, papain, trypsin | |||||||||||||
| VAPEEHPV |
|
|
| [39] | [22] | ||||||||||||
|
| Mealworm ( | Tenebrio molitor | ) | LE, AKKHKE (Hepatoprotective) |
Alcalase *, flavourzyme, neutrase | |||||||||||
| KVEGDLK |
|
|
| [34] | [17] | ||||||||||||
| Asian weaver ant larva and pupa mixture ( | Oecophylla smaragdina | ) | ||||||||||||||
| Mealworm ( | Tenebrio molitor | ) | FFGT, LSRVP (Anti-ACE) CTKKHKPNC (Antioxidant) |
SGD (Pepsin and trypsin) | NYVADGLG |
|
|
| [35] | [18] | |||||||
| Silkworm pupa ( | Bombyx mori | ) | AAEYPA, AKPGVY (Antioxidant) |
Alcalase *, papain, trypsin | |||||||||||||
| AAAPVAVAK |
|
|
|
| [30] | [13] | |||||||||||
| Silkworm pupa ( | Bombyx mori | ) | SWFVTPF, NDVLEF (Antioxidant) |
||||||||||||||
| YDDGSYKPH |
| Alcalase *, Prolyve, Flavourzyme, Brewers Clarex |
|
|
| [29] | [12] | ||||||||||
| Silkworm pupa ( | Bombyx mori | ) | FKGPACA, SVLGTGC (Antioxidant) |
||||||||||||||
| AGDDAPR |
| Acidic protease, followed by neutral protease |
|
|
| [33] | [16] | ||||||||||
| Silkworm pupa ( | Bombyx mori | ) | |||||||||||||||
| Locust | ASL (Anti-ACE) |
SGD (pepsin, trypsin, and α-chymotrypsin) | ( | Schistocerca gregaria | ) | GKDAVIV |
|
|
| [32] | [15] | ||||||
| Silkworm pupa ( | Bombyx mori | ) | GNPWM (Anti-ACE) |
Neutral protease | |||||||||||||
| AIGVGAIER |
|
|
| [31] | [14] |
* Enzyme generating the most active hydrolysate, which was selected for peptide purification. ACE: Angiotensin-I-converting enzyme, DPP-IV: Dipeptidyl peptidase-IV, GFC: Gel filtration chromatography, IEC: Ion exchange chromatography, LC: Liquid chromatography, MALDI: Matrix Assisted Laser Desorption/Ionization, MS: Mass spectrometry, MS-MS: Tandem mass spectrometry, RP-HPLC: Reversed-phase High-Performance Liquid Chromatography, SGD: Simulated gastrointestinal digestion, UF: Ultrafiltration.
3. Applications in Human Health Management
A wide variety of pathological conditions, including chronic obstructive pulmonary disease (COPD), diabetes complications, obesity, and cancer, have been linked to oxidative stress [44,
| FDPFPK | ||||||||||||||
| ||||||||||||||
| ||||||||||||||
| ||||||||||||||
| ||||||||||||||
| YETGNGIK |
| |||||||||||||
| Silkworm pupa ( | Bombyx mori | ) | AAEYPA |
| Antioxidant | [30] | [13] | |||||||
| AKPGVY |
| |||||||||||||
| Silkworm pupa ( | Bombyx mori | ) | SWFVTPF NDVLFF |
| Antioxidant | [29] | [12] | |||||||
| Silkworm pupa ( | Bombyx mori | ) | FKGPACA SVLGTGC |
| Antioxidant | [33] | [16] | |||||||
| Silkworm pupa ( | Bombyx mori | ) | ASL |
| Anti-hypertension | [32] | [15] | |||||||
| Silkworm pupa ( | Bombyx mori | ) | GNPWM WW |
| Anti-hypertension | [31] | [14] | |||||||
| Silkworm pupa ( | Bombyx mori | ) | PNPNTN |
| Immunomodulation | [52] | [29] | |||||||
| Asian weaver ant ( | Oecophylla smaragdina | ) | FFGT LSRVP |
| Anti-hypertension | [35] | [18] | |||||||
| CTKKHKPNC |
| Antioxidant | ||||||||||||
| Mealworm ( | Tenebrio molitor | ) | LPDQWDWR APPDGGFWEWGD |
| Antidiabetic | [39] | [22] | |||||||
| Larva of the Japanese rhinoceros beetle ( | Allomyrina dichotoma | ) | EIAQDFKTDL | In vivo model: HFD mouse model |
| In vitro model: 3T3-L1 cells |
| Anti-obesity, weight control | [37] | [20] | ||||
| Larva of the Japanese rhinoceros beetle ( | Allomyrina dichotoma | ) | AGLQFPVGR | In vivo model: HFD mouse model |
| Anti-obesity, weight control, hepatoprotective | [36] | [19] | ||||||
| Cotton leafworm ( | Spodoptera littoralis | ) | VF AVF |
In vivo model: SHR rat model |
| Anti-hypertensive | [53] | [30] | ||||||
| Egyptian cotton leafworm ( | Spodoptera littoralis | ) | SGD hydrolysate | In vivo model: Caenorhabditis elegans |
| Antioxidant | [49] | [28] | ||||||
| Cricket ( | Gryllodes sigillatus | ) | Cationic peptide fraction from sequential alcalase and SGD hydrolysates |
| Antidiabetic and anti-hypertension | [54] | [31] | |||||||
| Yellow mealworms ( | Tenebrio molitor | ) | RP-HPLC fraction of pepsin and trypsin hydrolysate |
| Antithrombotic | [55] | [32] | |||||||
| Mexican katydid ( | Pterophylla beltrani | ) | SGD hydrolysate |
| Anti-hypertension | [56] | [33] | |||||||
| <3 kDa fraction of SGD hydrolysate |
| Antidiabetic, Anti-hypertension, |
* All bioactivities were results obtained from in vitro models unless otherwise stated. AAPH: 2,2′-Azobis(2-amidinopropane) dihydrochloride, ABTS: 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), ACE: Angiotensin-converting enzyme, COX: Cyclooxygenase, DPPH: 2,2-Diphenyl-1-picrylhydrazyl, DPP-IV: Dipeptidyl peptidase IV, GPx: Glutathione peroxidase, GR: Glucocorticoid receptor, HDL: High-density lipoprotein cholesterol, HFD: High-fat diet, LDL: Low-density lipoprotein cholesterol, LOX: Lipoxygenases, ORAC: Oxygen radical antioxidant capacity, SGD: Simulated gastrointestinal digestion, SHR: Spontaneously hypertensive rat, SOD: Superoxide dismutase, TC: Total cholesterol, TG: Triglycerides, VLDL: Very low-density lipoprotein cholesterol.
4. Applications in Farm Animal Health Management
The beneficial bioactive properties of insect-derived peptides observed in humans and model organisms may also mediate advantageous health effects in livestock. In this context, the potential application of bioactive peptides with antimicrobial properties as alternatives to antibiotics has raised increasing interest [71,72][34][35]. In farm animals, the utilization of antibiotics is essential for animal health and welfare as well as food security [73][36]. The increasing application of antibiotics in livestock production systems represents, however, a major concern regarding the development of antimicrobial resistance that threatens both animal and human health and life [74,75][37][38]. Therefore, the importance of reducing the utilization of antibiotics in livestock production systems has been acknowledged in the Sustainable Development Goals [76][39]. Despite the available data on the antimicrobial effects of insect-derived bioactive peptides, studies in livestock mainly investigated the effects of bioactive peptides derived from sources other than insects [71,72][34][35]. Beneficial effects of AMPs from various sources on health and performance have been shown, e.g., in poultry [77,78][40][41] and pigs [79,80][42][43]. In general, the AMPs from insects comprise around 50 amino acids and are usually cationic [81,82][44][45]. The first AMP derived from insects is cecropin, which was isolated from the pupae of the giant silkmoth (Hyalophora cecropia) in 1980 [83][46]. To date, the only study that has investigated the effects of an insect-derived bioactive peptide on livestock physiology applied cecropin AD [84][47]. Even though the original peptides cecropin A and cecropin D were isolated from insect material (Hyalophora cecropia), the cecropin AD gene was expressed in Bacillus subtilis, cleaved and purified to obtain the chimeric target peptide (cecropin A(1–11)-D(12–37); KWKLFKKIEKV-GQRVRDAVISAGPAVATVAQATALAK) that was used for dietary supplementation. The cecropin AD was fed to 21-day-old, weaned piglets for 19 days at a 400 mg/kg diet. In comparison to the combination of two antibiotics (kitasamycin (100 mg/kg) and colistin sulfate (800 mg/kg)), no beneficial effects on growth performance were observed when supplementing cecropin AD. In contrast, after challenging the piglets with a single oral dose of 5 mL broth containing 109 colony-forming units/mL Escherichia coli K88, cecropin AD improved weight gain and feed efficiency along with reduced diarrhea incidence comparable to the antibiotic treatment. In addition, cecropin AD enhanced the ileal mucosa morphology and modulated the intestinal microbiota composition of the piglets. Different from the antibiotic combination, cecropin AD did not only increase the jejunal secretory immunoglobulins but also increased immunoglobulins and interleukins in serum, indicating a systemic immunomodulating effect of the peptide in weaned piglets. In soybean-meal fed turbot, dietary addition of cecropin AD from the previously described Bacillus subtilis expression system also positively modulated intestinal health and prevented the development of enteritis symptoms by shifting the intestinal microbiota towards an anti-inflammatory phenotype [85][48]. In addition to the antimicrobial properties of insect-derived peptides, bioactive peptides with antioxidant properties are also of interest to livestock nutrition. The continuous exposure of livestock animals to pathogenic microbes results in the activation of immune cells and, consequently, the production of reactive oxygen species. Excessive formation of reactive oxygen species can promote inflammatory processes and impair animal health and productivity. In this context, BSF protein hydrolysates were shown to possess antioxidant properties when compared to fish meal and chicken meal, potentially providing advantageous effects on animal health [97][49]. These results were obtained in vitro and thus require confirmation in vivo. Still, the antioxidant activity of insect proteins has been demonstrated upon ingestion by fish and chicken [98[50][51],99], suggesting that antioxidant peptides might be involved in mediating the observed effect.5. Applications in Plant Health Management
Evidence in the literature substantiates the efficacy of endogenous AMPs of insect origin in protecting against plant diseases. Plant diseases due to microbes and insects have led to an approximately 30% reduction in the yield of staple crops worldwide, with agricultural losses amounting to billions of dollars [100][52]. In view of the above, the effects of endogenous AMPs, specifically those from edible insects, are discussed below. In addition to the antimicrobial effects of cecropin observed in animals, as presented in the previous section, cecropin was also found to be functional against both phytopathogenic bacteria and fungi [101][53]. Other AMPs which can target plant pathogens with different modes of action, such as sarcotoxin, attacins, defensins, and metchnikowin, were isolated from various insects. However, these AMPs displayed broad-spectrum activities against more than one bacterium/fungus. AMPs with specific inhibition towards a single pathogen are more desirable [102][54]. The creation of transgenic plants expressing insect AMPs to resist bacterial and fungal infections is widely implemented in the agricultural sector. The gene coding for the apidaecins, AMPs from honeybees, was genetically engineered into the genome of the potato plant. The transgenic potato demonstrated resistance to infections from plant pathogens of the Erwinia genus and Agrobacterium species [103][55]. In addition, a tomato plant expressing cecropin was shown to resist wilt and spot diseases caused by the pathogenic bacteria Ralstonia solanacearum and Xanthomonas campestris, respectively [104][56]. The fusion of two or more AMPs to form chimeric AMPs prior to transformation into plants was reported to increase the potency of the recombinant peptides to overcome future infections [105,106][57][58]. Nevertheless, the production of foreign AMP genes within the host could interfere with the plant’s own gene expression system, which may indirectly affect the plant’s physiology and fitness [82][45]. There are also insect-derived neuropeptides that could confer plants with insecticidal properties against herbivorous insects. These neuropeptides generally modulate the insect’s behavior and physiology by interfering with the arthropod’s developmental processes, which include reproduction, energy metabolism, and growth [107][59]. The injection of the neuropeptide Allatostatin Manse-AST from the tobacco hornworm (Manduca sexta) into the larvae of the tomato moth (Lacanobia oleracea) led to reduced feeding, growth retardation, and a higher mortality rate of up to 80% [108][60]. This neuropeptide is made up of the sequence pEVRFRQCYFNPISCF-OH [109][61]; it can inhibit foregut peristalsis of insect larvae, producing the aforementioned insecticidal effects [108][60].References
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