Protein Hydrolysates Research Articles

Bioactivities of black soldier fly larvae protein hydrolysate

One of the potential insects for feed and food sources is the Black Soldier Fly (BSF) (Hermetia illucens). The BSF originated in South America and has now spread to many tropical countries. The BSF larvae (BSFL) had attracted much attention due to their good nutrient content and were recently reported as having useful bioactivities. BSFL has been widely used as feed and has been found to reduce bad smells associated with the growth of pathogenic microbes. The high protein content in BSFL is advantageous in the production of bioactive peptides. This research aimed to extract and hydrolyze the protein from BSFL with protease enzyme to produce protein hydrolysate or peptides with antioxidant and antibacterial activities. The antioxidant activity was measured using DPPH and FRAP, while the antibacterial was analyzed using the agar well diffusion method. BSFL was hydrolyzed with bromelain extracted from pineapple or commercial enzyme (Enzyplex). The IC50 shown by protein hydrolysate was 9.43±0.84% (v/v) or 0.72 mg/mL. The FRAP value was 521.21±264.53 µM for BSFL protein without enzyme addition, 792.14±291.02 for BSFL with the addition of bromelain, and 5,352.114±861.99 µM for BSFL with the addition of Enzyplex. The addition of bromelain increased the FRAP value 1.2 times, while the addition of Enzyplex increased the FRAP value 10.2 times. The antibacterial activity indicated that protein hydrolysate with phosphate buffer pH 8 at 50℃ and 24 hrs incubation showed the highest antibacterial activity to the lowest are Vibrio cholerae, Bacillus cereus and Staphylococcus aureus, respectively. The results suggest that BSFL has antibacterial and antioxidant bioactivities using bromelain extracted from pineapple and Enzyplex, a commercial enzyme that contains protease, lipase and amylase. Using Enzyplex as an enzyme to hydrolyze BFSL shows a very high antioxidant capacity compared to bromelain as an enzyme. This suggests that more protein and other macromolecules contribute to the antioxidant capacity. Using bromelain as an enzyme to hydrolyze BSFL, shows that BSFL peptide has higher antibacterial activity in gramnegative bacteria.

Effect of the addition of protein hydrolysates from grape seed meal residue to red wines in warm regions in the stabilization stage

The effect of adding protein hydrolysates from defatted grape seed meals, a residue of the grape pomace industry, on the improvement of color stabilization of Syrah wines in warm climates was evaluated. Factors such as the type of raw material, the hydrolysis time, and the doses of protein hydrolysate were assessed. Hydrolysates were added to the wines at the stabilization stage and scrutinized over five months focusing on the polyphenolic composition, copigmentation and polymerization, as well as color by differential tristimulus colorimetry. The addition of 3 g/L protein hydrolysates from 1-h hydrolysis depicted a color stabilization effect, leading to higher values of chroma (C*ab), phenolic compounds (benzoic acids and flavan-3-ols), and copigmentation, although assuming a slightly more aged-related tonality. These data obtained provide an interesting insight, not reported so far, on the use of this oenological alternative to avoid common color losses of red wines elaborated in warm climate.

Structural and sensory characteristics of ultrasonic assisted wet-heating Maillard reaction products of Giant salamander protein hydrolysates.

Chinese giant salamander protein hydrolysates (CGSPH) are beneficial to human health as a result of their high content of amino acids and peptides. However, the formation of bitter peptides in protein hydrolysates (PHs) would hinder their application in food industry. The ultrasound assisted wet-heating Maillard reaction (MR) is an effective way to improve the flavor of PHs. Thus, the effect of ultrasonic assisted wet-heating MR on the structure and flavor of CGSPH was investigated in the present study. The results indicated that the ultrasound assisted wet-heating MR products (MRPs) exhibited a higher degree of graft and more significant changes in the secondary and tertiary structures of CGSPH compared to traditional wet-heating MRPs. Moreover, ultrasound assisted wet-heating MR could significantly increase the content of small molecule peptides and reduce the content of free amino acids of CGSPH, which resulted in more significant changes in flavor characteristics. The changed in flavor properties after MR (especially ultrasound assisted wet-heating MRPs) were mainly manifested by a significant reduction in bitterness, as well as a significant increase in the content of aromatic aldehyde ester compounds such as furan-2-carbaldehyde, butanal, benzaldehyde, furfural, etc. CONCLUSIONS: Ultrasound assisted wet-heating MR between CGSPH and xylose could be a promising way to improve the sensory characteristics of CGSPH. © 2024 Society of Chemical Industry.

Isolation, identification, and chelation mechanism of ferrous-chelating peptide from peanut protein hydrolysate.

Peanut peptides can chelate iron but their chelation mechanism remains unclear. The purpose of this study is to separate peanut ferrous-chelating peptides and explore the chelation mechanism of peanut peptides with iron. Peanut peptide component F-122, which had a higher chelation rate, was separated using ultrafiltration, gel filtration chromatography, and ion exchange chromatography, achieving a ferrous chelation rate of 90.7%. Six peptide segments were screened and their amino acid sequences were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Spectral analysis confirmed that the chelation between peanut peptides and ferrous ions occurred and a new substance was formed. Molecular docking simulation indicated that the amino acids in peanut peptides involved in the chelating reaction were glutamic acid, arginine, glycine, threonine, phenylalanine, and lysine. The binding sites included the main chain oxygen atom, side chain oxygen atom, and carboxyl oxygen atom of amino acid. The isolated peanut peptide had a higher ferrous-chelation rate. The chelating mechanism of peanut peptide with ferrous ion was elucidated. This study provides a theoretical basis for the development of new peptide-ferrous preparations. © 2024 Society of Chemical Industry.

Characterization and molecular docking of tetrapeptides with cellular antioxidant and ACE inhibitory properties from cricket (Acheta domesticus) protein hydrolysate

Wide-ranging bioactivities of enzymatically digested insect protein to produce peptides have been targeted for functional food development. In this study, fractionated peptides obtained from cricket (Acheta domesticus) protein hydrolysate by alcalase digestion were identified and evaluated for their bioactivities. Peptide fractions F44, F45, and F46, isolated through size exclusion chromatography, demonstrated strong cytoprotective effects on SH-SY5Y and HepG2 cells exposed to H2O2. This was evidenced by a 2-fold decrease in reactive oxygen species (ROS) accumulation in the cells and a 3-fold upregulation of genes encoding antioxidant enzymes. The F45 peptide fractions also showed chemical antioxidant activities ranging from approximately 290 to 393 mg trolox/g peptide, measured by DPPH, ABTS, and FRAP assays. Furthermore, F45 demonstrated the highest angiotensin-converting enzyme I (ACE) inhibitory activity, 57.93 %. F45 induced higher levels of Nrf2, SOD1, SOD2, CAT, GSR, and GPx4 gene expression in SH-SY5Y and HepG2 cells compared to cells treated with H2O2 and no peptides (p < 0.05). Cells treated with H2O2 and F45 exhibited significantly increased antioxidant enzyme activity, including SOD, CAT, GSR, and GPx (p < 0.05). The F45B fraction from F45 was sequenced to obtain FVEG and FYDQ tetrapeptides. Molecular docking analysis revealed their high binding affinity to cellular antioxidant enzymes (SOD, CAT, GSR, GPx1, and GPx4), an antioxidant-related protein (Keap1), and ACE. These results suggest that the novel tetrapeptides from Acheta domesticus demonstrate important biological activities, establishing them as significant cellular antioxidant activities and a potential source of antihypertensive peptides.

Bioactivity of hydrolysates obtained from buffalo caseinate using macambira (Bromelia laciniosa L.) proteases

Bromelain refers to a set of proteases with the ability to break peptide bonds, presenting several industrial applications. The present work aimed to obtain and evaluate protein hydrolysates from buffalo casein after the action of bromelain extracted from macambira (Bromelia laciniosa). Proteolytic activity was determined using azocasein as substrate. Total protein was determined using the Lowry method. The enzyme extract was partially purified and protein hydrolysates were obtained from buffalo caseinate through experimental design. It was found that bromelain promoted hydrolysis that varied between 14.47 and 19.43% and only the caseinate concentration was significant in the experimental field studied. All hydrolysates showed antioxidant activity by two methods used. The hydrolysates obtained did not show antimicrobial activity against the microorganisms tested. The bromelain obtained has the potential to obtain protein hydrolysates, with antioxidant activity, which can, after further studies, be added to functional foods.

Enhancing Abiotic Stress Tolerance in Fruit Trees Using Microbial Biostimulants

Global climate change has significantly reduced the yield of many crops due to various abiotic stressors. These stressors include water-related issues such as drought and flooding, thermal changes like extremely low and high temperatures, salinity, and adverse soil pH conditions including alkalinity and acidity. Biostimulants have emerged as promising and effective tools for mitigating the damage caused by these abiotic stressors in plants, ultimately enhancing both the quantity and quality of crops. Biostimulants are naturally derived substances that include humic acid, protein hydrolysates, nitrogenous compounds, seaweed extracts, beneficial bacteria, and molds. Even at low concentrations, biostimulants play a critical role in activating important plant enzymes, inducing antioxidant defenses, improving water relations and photosynthetic activity, stimulating hormone-like activities (particularly auxins, gibberellins, and cytokinins), and modulating root system development. This review discusses the physiological effects of microbial biostimulants on the quality and productivity of fruit crops, as well as their experimental applications.

QPH-FR: A Novel Quinoa Peptide Enhances Chemosensitivity by Targeting Leucine-Rich Repeat-Containing G Protein-Coupled Receptor 5 in Colorectal Cancer.

Chemoresistance is one of the difficulties in the treatment of colorectal cancer (CRC), and the enhanced stemness of tumor cells is the underlying contributing factor. Leucine-rich repeat-containing G-protein-coupled receptor 5 (LGR5) is a classical marker of CRC stem cells and can be an important potential target for CRC chemotherapy. Quinoa, a protein-rich plant, offers potential as a source of high-quality active peptides. Novelly, the study obtained quinoa protein hydrolysate (QPH) from whole quinoa grains by simulated digestion. In vivo experiments revealed that the tumor volume in the 5-FU+QPH group decreased from 145.90 ± 13.35 to 94.49 ± 13.05 mm3 in the 5-FU group, suggesting that QPH enhances the chemosensitivity of CRC. Further, the most effective peptide QPH-FR from 631 peptides in QPH was screened by activity prediction, molecular docking, and experimental validation. Mechanistically, QPH-FR competitively suppressed the formation of the LGR5/RSPO1 complex by binding to LGR5, causing RNF43/ZNRF3 to ubiquitinate the FZD receptor, thereby suppressing the Wnt/β-catenin signaling pathway and exerting stemness inhibition. In summary, the study proposes that a novel peptide QPH-FR from quinoa elucidates the mechanism by which QPH-FR targets LGR5 to enhance chemosensitivity, providing theoretical support for the development of chemotherapeutic adjuvant drugs based on plant peptides.

Application of Protein Hydrolysate Improved the Productivity of Soybean under Greenhouse Cultivation

Protein hydrolysates are plant biostimulants containing amino acids, oligopeptides, and peptides in their composition. When supplied to plants, protein hydrolysates (HPs) have been identified to improve nitrogen metabolism, enhance the activity of antioxidant enzymes, boost plant defense response to stresses, and positively impact the quantity and quality of products. Soybean is a crucial global commodity, with nitrogen being the primary nutrient for crop development as it directly affects productivity. This study aimed to evaluate the effect of an HP-based biostimulant on the N metabolism in nodulated soybean plants and their productivity. A greenhouse experiment was conducted to test two modes of application of the 0.20% HP-based biostimulant. Soybean plants, growing in pots, were treated with 0.20% HP either via seed treatment or foliar application (at growth stages V3 and V5). Activities of enzymes and compounds related to N metabolism, gene expression, and productivity components were analyzed. It was observed that the mode of application did not significantly influence the results. The application of HPs increased the concentration of nitrate, amino acids, and ureides in soybean leaves. It also positively altered the expression of genes such as nitrate reductase, urease, and asparagine. Additionally, it enhanced productivity, resulting in plants with a greater number and weight of pods and grains. Therefore, it is possible to consider HPs as a stimulator for increasing soybean productivity, even under non-stressing conditions.

Enriching NPK Mineral Fertilizer with Plant-Stimulating Peptides Increases Soilless Tomato Production, Grower Profit, and Environmental Sustainability.

The need to increase agricultural production to feed a steadily growing population may clash with the more environmentally friendly but less efficient production methods required. Therefore, it is important to try to reduce the use of chemical inputs without compromising production. In this scenario, natural biostimulants have become one of the most sought-after and researched technologies. In the present study, the results of a greenhouse experiment on hydroponic tomatoes (Solanum lycopersicum L.) are presented, which involved comparing the use of ordinary NPK fertilizer (Cerbero®) with the use of NPK fertilizers enriched with 0.5% protein hydrolysate of plant origin (Cerbero Green®) at both standard (100%) and reduced (70%) fertilization rates. The results highlight how the use of Cerbero Green® fertilizers improves the production performance of tomatoes. More specifically, they show that the use of Cerbero Green® leads to higher marketable yields, especially under reducing fertilizer use, ensuring a positive net change in profit for the grower. In addition, carbon footprint analysis has revealed that the use of Cerbero Green® reduces the environmental impact of hydroponic tomato growing practices by up to 8%. The observed higher yield of hydroponically grown tomatoes even with reduced fertilization rates underlines once again the key role of natural biostimulants in increasing both the economic and environmental sustainability of horticultural production.

Assessment of the impact of whey protein hydrolysate on myofibrillar proteins in surimi during repeated freeze–thaw cycles: Quality enhancement and antifreeze potential

The quality of surimi, widely used in processed seafood, is compromised by freeze–thaw cycles, leading to protein denaturation and oxidative degradation. The objective of this study is to explore the effects of adding natural whey peptide hydrolysate (WPH) on the myofibrillar proteins of repeatedly freeze–thawed surimi. Results indicated surimi treated with 15% WPH exhibited only a 128% increase in surface hydrophobicity and a maximum peroxide value of 7.84 μg/kg, significantly lower than the control group. Additionally, salt-soluble protein content, emulsification activity, and stability decreased with the increase in freeze–thaw cycles. With a 15% WPH offering the most significant protective effect, evidenced by reductions of only 25.02%, 42.52% and 37.02% in salt-soluble protein content, emulsification activity, and stability, respectively. These outcomes demonstrate that WPH effectively reduces protein denaturation during repeated freeze–thaw processes. Future research should explore the molecular mechanisms underlying WPH's protective effects and evaluate their applicability in other food systems.

Soy protein hydrolysates induce menaquinone-7 biosynthesis by enhancing the biofilm formation of Bacillus subtilis natto

Menaquinone-7 (MK-7) is a form of vitamin K2 with health-beneficial effects. A novel fermentation strategy based on combining soy protein hydrolysates (SPHs) with biofilm-based fermentation was investigated to enhance menaquinone-7 (MK-7) biosynthesis by Bacillus subtilis natto. Results showed the SPHs increased MK-7 yield by 199.4% in two-stage aeration fermentation as compared to the SP-based medium in submerged fermentation, which was related to the formation of robust biofilm with wrinkles and the enhancement of cell viability. Moreover, there was a significant correlation between key genes related to MK-7 and biofilm synthesis, and the quorum sensing (QS) related genes, Spo0A and SinR, were downregulated by 0.64-fold and 0.39-fold respectively, which promoted biofilm matrix synthesis. Meanwhile, SPHs also enhanced the MK-7 precursor, isoprene side chain, supply, and MK-7 assembly efficiency. Improved fermentation performances of bacterial cells during fermentation were attributed to abundant oligopeptides (Mw < 1 kDa) and moderate amino acids, particularly Arg, Asp, and Phe in SPHs. All these results revealed that SPHs were a potential and superior nitrogen source for MK-7 production by Bacillus subtilis natto.

Novel ACE inhibitory peptides from enzymatic hydrolysate of Channa punctata protein: In vitro and In silico assay of structure-activity relationship

Channa punctata flesh meat is well known for its ethnomedicinal values. The objective of this study was to isolate and identify peptides having Angiotensin-Converting Enzyme (ACE) inhibitory potential from the Channa punctata fish protein hydrolysates (FPH) and to investigate the inhibitory mechanism by docking study. ACE inhibitory potential of the ultrafiltrate of C. punctata 240 min protein hydrolysates was analysed. The PrAHyd240 (<3 kDa) had the strongest ACE inhibitory potential as it has the lowest IC50 value i.e., 66.08 μg/ml. To identify the ACE inhibitory peptides, PrAHyd240 (<3 kDa) was evaluated by LC ESI mass spectrometer. The amino acid residues of 3 peptides within the intensity count 100–250 were determined by de novo sequencing.The docking analysis reveals that the peptides were deeply buried in the active site of ACE. Thr 5 of ISISTSGGSFR, Val 3 of SLVNLGGSK, and Val 6, Ala 7 of SISISVAR form highly stable metal coordination bonds with the Zn cofactor present in the binding site of ACE. Similar to captopril, the peptide SISISVAR interacted with the amino acids His 353 and His 513 of the binding sites of ACE via H-bond interactions. The MD simulation study reveals that the peptides ISISTSGGSFR, SLVNLGGSK, and SISISVAR interacted with the Zn+ ion via H-bond with 100% occupancy respectively. The above study reveals that Channa punctata protein hydrolysate is a rich source of ACE inhibitory peptides and the isolated peptides ISISTSGGSFR, SLVNLGGSK, and SISISVAR are potential ingredients in the preparation of functional foods.

Valorisation of Tenebrio molitor beetles: enzymes-based bioprocessing to obtain a highly digestible protein hydrolysate

Abstract The biological valorisation of edible insects is an eco-saving approach that may increase their use for food and feeding purposes. Beetles of T. molitor are a direct waste of insect farms since their protein have a low digestibility. Currently, the degree of hydrolysis achieved with biological treatments are much lower than with chemical treatments. This work focused on the enzymatic hydrolysis of protein from T. molitor beetles using proteases. The obtained protein hydrolysate was evaluated regarding the digestibility and functional properties. Higher hydrolysis degree (HD; 47%) was obtained using a protease from Aspergillus oryzae, which efficiently separated protein from chitin. A full factorial design determined that a liquid:solid ratio (LSR) of 15 and an enzyme load of 3200 U/g increase HD up to 78%. The protein hydrolysate showed higher digestibility (77.3%) compared to beetles’ meal before (17.8%) and after defatting (25.7%). The protein hydrolysate showed a high antioxidant activity (462.1 ± 7.48 μmol TE/g DW), it was highly soluble at pH ranging between 3 and 9 and showed an emulsification activity and stability of 53.6% and 82.2%, respectively. Therefore, this bioprocess improved the use of beetles, obtaining protein with greater digestibility to be used as food.

Isolation, Characterization, and Functional Properties of Antioxidant Peptides from Mulberry Leaf Enzymatic Hydrolysates.

Recent evidence suggests that mulberry leaves have good antioxidant activity. However, what the antioxidant ingredient is and how the ingredient works are still not well understood. In this study, we enzymatically hydrolyze mulberry leaf proteins (MLPs) using neutral protease and find that the mulberry leaf protein hydrolysates (MLPHs) have stronger antioxidant activity compared to MLPs. We separate the core antioxidant components in MLPHs by ion-exchange columns and molecular sieves and identify 798 antioxidant peptides by LC-MS/MS. Through bioinformatics analysis and biochemical assays, we screen two previously unreported peptides, P6 and P7, with excellent antioxidant activities. P6 and P7 not only significantly reduce ROS in cells but also improve the activities of the antioxidant enzymes SOD and CAT. In addition, both peptides are found to exert protective effects against H2O2-induced chromatin damage and cell apoptosis. Collectively, these results provide support for the application of mulberry leaf peptides as antioxidants in the medical, food and livestock industries.

Production of plant protein from seeds and cake of industrial hemp: Overview of processing methods for food industry

Industrial hemp (Cannabis sativa L.) is a multifunctional raw material with a wide spectrum of applications. A huge interest in hemp has arisen in the food industry comparatively recently. Seeds and cake of hemp have the high protein content (20.00-38.70% and 27.90-40.70%, respectively), which makes them a promising raw material for production of concentrates, isolates, and hydrolysates for the food industry. Hemp cake is distinguished by the high content of fiber (17.41-60.38%) and can be used as a prebiotic component of food. In terms of the amino acid content, the amino acid composition of hemp exceeds the corresponding indicators of the reference protein recommended by WHO. The content of lysine is the only indicator, in which hemp protein is inferior to the “ideal” protein. Digestibility of protein of hulled hemp seeds is in a range from 90.8% to 97.5%, which is comparable to digestibility of casein. Digestibility of hemp isolate is 88-91%, which is 21.9% higher than that of soy protein isolate. Peptides and amino acids contained in hydrolysates of hemp protein can show the high biological activity. Hydrolysates attract interest among researchers not only because of their bioactivity but also because of their high digestibility and nutritional value. Targeted proteolysis is a tool that facilitates an improvement in the functional-technological properties of protein. Seeds and cake are a promising raw material for using in food technologies to produce vegetable oil, dietary fiber, protein preparations and functional products. The aim of this paper is to analyze the main methods for industrial hemp processing and promising directions of using protein products from waste of hemp oil production in the food industry.

Functional improvement and characterization of protein hydrolysates prepared by the fermentation of irradiated tilapia skin

Gamma irradiation (γ-irradiation) sterilizes and modifies proteins. This study aimed to enhance the performance of protein hydrolysates of fermented tilapia fish skin using irradiation. The results showed that γ-irradiation could effectively kill harmful microorganisms in fish skin at 6 kGy. Irradiation at 1–6 kGy dose disintegrated the internal structure of fish skin proteins, thus increasing the degree of hydrolysis after fermentation by Bacillus subtilis L4; however, irradiation at 9–12 kGy caused cross-linking and aggregation of fish skin proteins. The solubility, and water and oil holding capacity of the protein hydrolysates were significantly improved compared to those of the non-irradiated sample. The maximum emulsifying activity (164.61±16.28 m2/g), foaming activity (91.13±2.30 mL), and surface hydrophobicity index (5766.43±770.56) were observed in the protein hydrolysates fermented from fish skin irradiated at 12 kGy. The antioxidant activity of the protein hydrolysates increased with increasing irradiation doses. This suggested that the functional properties and antioxidant activity of protein hydrolysates from fish skin fermentation can be improved by appropriate irradiation pretreatment, providing a feasible method for improving the utilization and quality of proteins in fishery waste.

Whey protein hydrolysate intervention ameliorates memory deficits in APP/PS1 mice: Unveiling gut microbe–short‐chain fatty acid–brain axis

AbstractThe intricate causes of Alzheimer's disease (AD) hinder effective, lasting treatment. Although the dietary modulation of the brain–gut axis was explored for AD therapy, the exact mechanism remains unclear. This study suggested that 140 days of the whey protein hydrolysate (WPH) intake could attenuate the AD pathologic symptoms in APP/PS1 transgenic mice via a bidirectional action of the gut microbe–SCFA (short‐chain fatty acid)–brain axis. Behavioral tests demonstrated that high‐dose WPH (WPH‐H, 100 mg/kg body weight [bw]) improved passive and recognition memory in mice. Furthermore, WPH‐H significantly reduced amyloid beta 1–42 (Aβ1–42) levels in serum (p &lt; .05) and brain (p &lt; .001) while enhancing serum superoxide dismutase (SOD) activity (p &lt; .01). Brain acetylcholinesterase (p &lt; .01) activity and pro‐inflammatory factors in serum were also reduced. Notably, WPH‐H remodeled gut microbiota composition by increasing Dubosiella and decreasing Bacteroides and norank_f__Ruminococcaceae while stimulating SCFA production. Proteomics indicated that WPH enhanced neurotoxic Aβ autophagy, synaptogenesis, neurotransmitter delivery, and antioxidative stress response via regulated protein expression. Correlation analysis revealed strong links between modified gut microbiota, elevated SCFA levels, and hippocampal protein up‐regulation (Atg4b, Nsfl1c, Tcf20, Nr2f1, and Trappc9) and down‐regulation (Krt1). Overall, the amelioration of memory deficits in APP/PS1 mice through WPH‐H consumption can be attributed to the interconnected interactions among gut microbes, SCFAs, and brain. Our study illuminated the intricate interplay between nutrition, gut health, and memory function, emphasizing WPH's potential in alleviating AD symptoms.

Comparative analysis of rice bran and sesame protein hydrolysates in inhibiting foodborne pathogens: efficacy against Escherichia coliO157:H7 and Listeria monocytogenes

SummaryThis study explores the antibacterial potential of hydrolysates derived from rice bran protein (RBP) and sesame protein (SP) against Escherichia coli O157:H7 and Listeria monocytogenes. RBP and SP were hydrolysed by protease from Bacillus licheniformis (labelled as RBPH‐B and SPH‐B) and α‐chymotrypsin (denoted as RBPH‐C and SPH‐C), and subsequently fractionated into four molecular weight (MW) categories: F1 (&gt;100 kDa), F2 (10–100 kDa), F3 (1–10 kDa), and F4 (&lt;1 kDa). The antibacterial activities of these hydrolysates and their fractions were systematically evaluated. The results indicated that RBPH‐B and RBPH‐C, along with their fractions, exhibited notable efficacy against L. monocytogenes. Conversely, both SPH‐B, SPH‐C, and their fractions showed pronounced antibacterial activities against both pathogens. Notably, lower MW fractions (SPH‐B, SPH‐B‐F2, and SPH‐B‐F3) demonstrated superior antibacterial properties, effectively reducing bacterial populations to below detection limits (≥6 log CFU mL−1) at a concentration of 100 mg mL−1. Further analysis revealed that SPH‐B‐F3 markedly reduced the reaction time required to inhibit or eliminate E. coli O157:H7 and L. monocytogenes, with comparable times of 6 and 4 h, respectively. These findings highlight the potential application of specific SPH‐B fractions as antibacterial agents in the food industry.

Protein hydrolysates of millets: an effective therapeutic to wide range of diseases

PurposeMillets are underused crops that have the potential to withstand harsh environmental conditions. Recent research has proved immense nutritional benefits associated with millets which have increased their utilization to some extent but yet their sole potential is left to be exploited. Different millet varieties have exceptional nutritional and nutraceutical properties which can ameliorate even the deadly conditions of cancers. They have significant protein composition ranging from 10% to 12% which possess effective bioactive potential. Protein hydrolysates containing bioactive peptides have been evaluated for their therapeutic effects against a variety of diseases. This review aims to discuss the bioactive potential of different millet protein hydrolysates to encourage research for development of effective natural therapeutics.Design/methodology/approachThe present article elaborates on effective studies on the therapeutic effects of millet protein hydrolysates.FindingsSeveral effective millet peptides have been reported for their therapeutic effect against different diseases and their antioxidant, anti-inflammatory, anticancer, antimicrobial and antidiabetic effects have been investigated.Originality/valueThis review focuses on millet bioactive peptides and their significance in treating variety of diseases. Thus, will further encourage research to explore the novel therapeutic effects of millet proteins hydrolysates which can eventually result in the development of natural and safe therapeutics.