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Wong, F.; Chai, T. Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors. Encyclopedia. Available online: (accessed on 25 June 2024).
Wong F, Chai T. Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors. Encyclopedia. Available at: Accessed June 25, 2024.
Wong, Fai-Chu, Tsun-Thai Chai. "Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors" Encyclopedia, (accessed June 25, 2024).
Wong, F., & Chai, T. (2023, July 13). Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors. In Encyclopedia.
Wong, Fai-Chu and Tsun-Thai Chai. "Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors." Encyclopedia. Web. 13 July, 2023.
Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors

Lipoxygenases are non-heme iron-containing enzymes that catalyze the oxidation of polyunsaturated fatty acids, resulting in the production of lipid hydroperoxides, which are precursors of inflammatory lipid mediators. These enzymes are widely distributed in humans, other eukaryotes, and cyanobacteria. Lipoxygenases hold promise as therapeutic targets for several human diseases, including cancer and inflammation-related disorders. Inhibitors of lipoxygenase have potential applications in pharmaceuticals, cosmetics, and food. Bioactive peptides are short amino acid sequences embedded within parent proteins, which can be released by enzymatic hydrolysis, microbial fermentation, and gastrointestinal digestion. A wide variety of bioactivities have been documented for protein hydrolysates and peptides derived from different biological sources. 

anti-lipoxygenase peptide enzymatic hydrolysis inflammation lipoxygenase inhibitory activity

1. Introduction

Bioactive peptides are short fragments ranging between 2 and 20 residues that are initially encrypted in an inactive state in a parent protein. Such fragments exhibit their bioactivities after they are released from the parent protein [1][2][3]. To date, a large number of bioactive peptides that are capable of modulating biological functions of the human body and those that can tackle the activity of pathogenic organisms have been documented [4]. Such peptides can exert their effects in a variety of ways, including the inhibition of enzymes associated with metabolic syndrome and inflammation [5][6][7][8], the disruption of protein–protein interactions, the regulation of gene and protein expression, and the modulation of cellular signaling pathways [9][10]. Bioactive peptides could be released from dietary proteins during in vivo gastrointestinal (GI) digestion. They can also be generated from other protein-rich samples by means of enzymatic proteolysis and microbial fermentation [1][2][3][11]. The raw materials that have been documented as sources of bioactive peptides are diverse and numerous [12]. They range from edible materials, such as seafood [2][13], edible insects [14], spices [15], seeds [16], and traditional medicine [17], to non-edible marine organisms, such as the barrel sponge (Xestospongia testudinaria) [18]. Additionally, agricultural by-products, such as poultry feathers [19], fish scales [20], and corn silk [21], are also sources of bioactive peptides.
“Protein hydrolysate” refers to the product of the hydrolytic action of protease(s) on a complex proteinaceous sample or a pure protein sample. Protein hydrolysates are essentially a mixture of free amino acids, peptides, and possibly even partially degraded proteins. Protein hydrolysates are generally regarded as a crude peptide mixture. Owing to the crude nature of a protein hydrolysate, peptides of opposite bioactivity, such as prooxidant peptides vs. antioxidant peptides, may co-exist in the same hydrolysate [22][23]. The presence of non-bioactive peptides or low availability of the bioactive peptides of interest may lead to the detection of poor bioactivity. Protein hydrolysates often serve as the initial raw material for bioactivity testing and subsequently, as the sources from which bioactive peptides can be isolated and identified, facilitated by a series of bioassay- or chemical assay-guided fractionation steps [1][2][3].

2. Lipoxygenases (LOX)

There are six arachidonate LOXs in humans, including 5-LOX, 12-LOX, and 15-LOX. The genes encoding these enzymes, their tissue distribution. The nomenclature of LOX enzymes corresponds to the position of the carbon in the fatty acid that the enzyme oxygenates. For example, human 5-LOX oxygenates carbon 5 on arachidonic acid, converting it to 5-hydroperoxyeicosatetraenoic acid (5-HPETE) [24][25]. It is understood that 5-HPETE may serve as a precursor in the production of proinflammatory lipid mediators in human cells [26]. LOX enzymes have been implicated in the pathogenesis of human diseases, including several cancers, chronic liver disease, atherosclerosis, and asthma [26][27]. Consequently, inhibition of LOX is considered an important strategy for disease prevention and treatment, and LOX inhibitors have attracted considerable attention from the medical community [25][26]. LOX is responsible for many inflammatory skin problems, such as the redness, rashes, or edema characteristic of many skin diseases. Therefore, LOX inhibitors are considered to have skin care or cosmetic applications [28][29][30]. On the other hand, the products of undesired LOX reactions can affect the quality of food. Legumes, which are rich in fatty acids, are particularly susceptible to LOX-associated food spoilage. The action of LOX on unsaturated fatty acids can lead to rancidity, accompanied by the development of off-flavors and odors in legumes and legume-based products. In addition, LOX activity can also affect the color, aroma, and flavor of oil and oil-containing foods during processing and storage [24]. In short, LOX inhibition not only provides a valuable approach to the prevention and treatment of human diseases, but the control of LOX activity is also relevant to the food industry.

3. Production of Anti-LOX Protein Hydrolysates and Peptides

The production of anti-LOX protein hydrolysates and bioactive peptides from various biological sources, including edible plant proteins (proso millet and chia seeds) [31][32], edible animal proteins (insects and milk) [33][34], velvet antler blood [17], and agricultural wastes (e.g., poultry feathers and fish scales) [19][35], has been documented. Protein hydrolysis, facilitated primarily by enzymatic hydrolysis and less commonly by microbial degradation, has been used to liberate anti-LOX peptides from biological samples. Enzymatic hydrolysis in the form of simulated GI digestion, as mediated by the action of pepsin and pancreatin, has been employed to generate anti-LOX protein hydrolysates and peptides from velvet antler blood [17] and chia seed proteins [32]. In comparison, the simulated GI digestion experiments performed on insect proteins [33] and millet grain protein fractions [31] were more representative of human GI digestion because they also simulated oral digestion by using α-amylase in artificial saliva, in addition to simulating gastric digestion with pepsin, and intestinal digestion with pancreatin and bile extract. Simulated GI digestion is an interesting experimental approach because it may reveal the potential benefit of dietary proteins in terms of their ability to release GI-resistant anti-LOX peptides after oral ingestion. GI resistance does not imply GI absorption or uptake. However, GI-resistant anti-LOX peptides remain valuable because they are not susceptible to further degradation, reducing the risk of losing their bioactivity before intestinal absorption can occur. In contrast to the common approach of hydrolyzing protein samples with commercially available proteases, Kshetri and coworkers [19] used locally isolated keratinolytic bacteria, namely Streptomyces tanashiensis-RCM-SSR-6 and Bacillus sp. RCM-SSR-102 [36][37], to perform microbial hydrolysis of chicken feather waste.
When preparing anti-LOX protein hydrolysates, some researchers prepared protein isolates or fractions from their samples prior to protein hydrolysis [31][32][33], while others did not [19]. Focusing on three insect species (mealworms, locusts, and crickets), Zielińska and coworkers [33] compared the anti-LOX activities of hydrolysates prepared from whole insects and insect protein isolates. They found that hydrolysates of insect proteins (IC50 = 0.65–0.89 mg/mL) exhibited a stronger anti-LOX activity than the hydrolysates of whole insects (IC50 = 1.30–3.14 mg/mL). Thus, both groups of hydrolysates exerted anti-LOX activity, although the use of insect protein isolates as raw material led to stronger anti-LOX activity [33]
Some researchers use sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to monitor the extent of protein sample hydrolysis and to estimate the molecular weight distribution of the major proteins/peptides in the hydrolyzed samples [17][19][38]. To monitor the extent of protein hydrolysis, specifically the percentage of cleaved peptide bonds, Grancieri and coworkers [32] analyzed the degree of hydrolysis (DH) of chia seed protein fractions after simulated GI digestion. The scholars found that the DH of protein hydrolysates did not correlate closely with their anti-LOX activity [32]. This suggests that although DH is useful for monitoring the extent or effectiveness of proteolysis, it is not a reliable indicator of the anti-LOX activity of protein hydrolysates.
The strategy employed by Ding and coworkers [16] for isolating and identifying anti-LOX peptides from velvet antler blood hydrolysate is typical of how numerous other bioactive peptides were discovered in the literature [1][2][3]. Briefly, the scholars used a combination of non-chromatographic (membrane ultrafiltration) and chromatographic (gel filtration chromatography) methods to fractionate the hydrolysate, guided by an in vitro anti-LOX assay. The desired gel filtration chromatography fraction was finally subjected to liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis to identify the peptide sequences present in the fraction. Ding and coworkers [17] identified 219 peptides from a gel filtration chromatographic fraction of velvet antler blood hydrolysate. Synthesis of all 219 peptides for in vitro activity validation would be costly and laborious. Therefore, the scholars used in silico screening tools to narrow down the entire set of putative bioactive peptides to eight candidates before synthesizing and testing them for in vitro anti-LOX activity [17].
In bioactive peptide discovery, peptide synthesis is the next logical step after the peptide sequence identification. Such a step is crucial because the final purified active fraction isolated by researchers often comprise multiple peptide sequences, some of which may not exert the desired bioactivity.
In the context of peptide identification, discrepancies between theoretically expected fragments from a hydrolyzed protein and those actually detected from the hydrolysate have been reported. For example, in the search for anti-LOX peptides from β-casein tryptic digest, Rival and coworkers [38] identified a missed cleavage peptide segment (VKEAMAPK). In addition, the scholars found a peptide sequence resulting from an unexpected cleavage of the Ser-Lys peptide bond in β-casein by trypsin. 

4. Potency and Modes of Action

 Figure 1 depicts a graphical summary of the modes of action proposed for the 18 anti-LOX peptides.
Figure 1. Summary of modes of action of 18 anti-LOX peptides.
Eight anti-LOX peptides ranging from three to nine residues were identified from velvet antler blood hydrolysate [17]. The eight peptides were individually less potent (<12% anti-LOX activity) than diclofenac sodium (approximately 85% activity), a commonly prescribed nonsteroidal anti-inflammatory drug that exhibits anti-LOX activity [39]. The peptides were only tested at a single sample concentration (1 mg/mL) and IC50 values were not reported. The peptides FSAL and LFP, exhibiting approximately 12 and 10% activity, respectively, were the strongest among the eight peptides.
Ding and coworkers [17] also reported that the eight peptides all showed weaker anti-LOX activity than the gel filtration chromatographic fraction GF-2 (26%) from which they were isolated. Therefore, the anti-LOX activity of partially purified peptide fraction GF-2 may have resulted from synergism between multiple peptides present in the fraction. GF-2 apparently holds more potential as an anti-LOX agent when compared to the eight individual peptides. Thus, GF-2 may be a more promising and likely more economical anti-LOX ingredient for functional food and cosmeceutical applications. 
Four anti-LOX peptides of 7–8 residues were identified from a tryptic digest of β-casein [38][40]. Rival and coworkers [40] hypothesized that these four peptides inhibit LOX by acting as the preferred targets for carbon-centered radicals formed prior to the introduction of oxygen in LOX-catalyzed reactions. Their experimental data ruled out the possibility that the peptides acted as LOX inhibitors by forming enzyme-inhibitor complexes or by iron chelation [40]. Comparing the relative potency between the anti-LOX peptides derived from β-casein [40] and velvet antler blood [17] is challenging because the two studies used distinctly different LOX inhibition assays (spectrophotometric vs. rate of oxygen consumption) and due to the lack of an identical reference compound in their assays. 
Grancieri and coworkers [32] identified three putative anti-LOX peptides (HYGGPPGGCR, SPKDLALPPGALPPVQ, and TGPSPTAGPPAPGGGTH) from chia seed proteins subjected to simulated GI digestion (pepsin + pancreatin). In the study, anti-LOX capacity was expressed as ascorbic acid equivalents, and IC50 values were not reported. While all samples tested exhibited anti-LOX activity, hydrolysates of chia globulin, prolamin, and glutenin fractions were similarly potent, being stronger than the hydrolysate of total chia protein. Nonetheless, the scholars did not proceed to synthesize the peptide sequences to verify their anti-LOX activity. The anti-LOX potential of the three peptides was predicted only based on their interactions with LOX in molecular docking simulation. The three peptides exhibited relatively negative binding free energies and lower inhibition constants (Ki) when compared to the pharmacological control Simvastatin, suggesting the potential of the peptides as LOX inhibitors [32]. Wet-lab validation of the anti-LOX activity of the three peptides is warranted in the future.


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