Peanut Peptides Research Articles

In Silico Identification of Peanut Peptides Suitable for Allergy Immunotherapy in HLA-DRB1*03:01-Restricted Patients.

Peanut allergy, a prevalent and potentially severe condition affecting millions worldwide, has been linked to specific human leukocyte antigens (HLAs), suggesting increased susceptibility. Employing an immunoinformatic strategy, we developed a "logo model" based on amino acid frequencies in the peptide binding core and used it to predict peptides originating from 28 known peanut allergens binding to HLA-DRB1*03:01, one of the susceptibility alleles. These peptides hold promise for immunotherapy in HLA-DRB1*03:01 carriers, offering reduced allergenicity compared to whole proteins. By targeting essential epitopes, immunotherapy can modulate immune responses with minimal risk of severe reactions. This precise approach could induce immune tolerance with fewer adverse effects, presenting a safer and more effective treatment for peanut allergy and other allergic conditions.

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.

Enhanced Gut Microbiome Capacity for Amino Acid Metabolism is associated with Peanut Oral Immunotherapy Failure.

Peanut Oral Immunotherapy (POIT) holds promise for remission of peanut allergy, though treatment is protracted and successful in only a subset of patients. Because the gut microbiome is linked to food allergy, we sought to identify fecal microbial predictors of POIT efficacy and to develop mechanistic insights into treatment response. Longitudinal functional analysis of the fecal microbiome of children (n=79) undergoing POIT in a first double-blind, placebo-controlled clinical trial, identified five microbial-derived bile acids enriched in fecal samples prior to POIT initiation that predicted treatment efficacy (AUC 0.71). Failure to induce disease remission was associated with a distinct fecal microbiome with enhanced capacity for bile acid deconjugation, amino acid metabolism, and increased peanut peptide degradation in vitro . Thus, microbiome mechanisms of POIT failure appear to include depletion of immunomodulatory secondary bile and amino acids and the antigenic peanut peptides necessary to promote peanut allergy desensitization and remission.

Potential of Marine Bacterial Metalloprotease A69 in the Preparation of Peanut Peptides with Angiotensin-Converting Enzyme (ACE)-Inhibitory and Antioxidant Properties.

Marine bacterial proteases have rarely been used to produce bioactive peptides, although many have been reported. This study aims to evaluate the potential of the marine bacterial metalloprotease A69 from recombinant Bacillus subtilis in the preparation of peanut peptides (PPs) with antioxidant activity and angiotensin-converting enzyme (ACE)-inhibitory activity. Based on the optimization of the hydrolysis parameters of protease A69, a process for PPs preparation was set up in which the peanut protein was hydrolyzed by A69 at 3000 U g-1 and 60 °C, pH 7.0 for 4 h. The prepared PPs exhibited a high content of peptides with molecular weights lower than 1000 Da (>80%) and 3000 Da (>95%) and contained 17 kinds of amino acids. Moreover, the PPs displayed elevated scavenging of hydroxyl radical and 1,1-diphenyl-2-picryl-hydrazyl radical, with IC50 values of 1.50 mg mL-1 and 1.66 mg mL-1, respectively, indicating the good antioxidant activity of the PPs. The PPs also showed remarkable ACE-inhibitory activity, with an IC50 value of 0.71 mg mL-1. By liquid chromatography mass spectrometry analysis, the sequences of 19 ACE inhibitory peptides and 15 antioxidant peptides were identified from the PPs. These results indicate that the prepared PPs have a good nutritional value, as well as good antioxidant and antihypertensive effects, and that the marine bacterial metalloprotease A69 has promising potential in relation to the preparation of bioactive peptides from peanut protein.

A combined in vitro and in silico study of the inhibitory mechanism of angiotensin-converting enzyme with peanut peptides

Food-derived peptides with low molecular weight, high bioavailability, and good absorptivity have been exploited as angiotensin-converting enzyme (ACE) inhibitors. In the present study, in-vitro inhibition kinetics of peanut peptides, in silico screening, validation of ACE inhibitory activity, molecular dynamics (MD) simulations, and HUVEC cells were performed to systematically identify the inhibitory mechanism of ACE interacting with peanut peptides. The results indicate that FPHPP, FPHY, and FPHFD peptides have good thermal, pH, and digestive stability. MD trajectories elucidate the dynamic correlation between peptides and ACE and verify the specific binding interaction. Noteworthily, FPHPP is the best inhibitor with a strongest binding affinity and significantly increases NO, SOD production, and AT2R expression, and decreases ROS, MDA, ET-1 levels, ACE, and AT1R accumulation in Ang II-injury HUVEC cells.

Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide-calcium complex.

Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide-calcium complex. Peptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography-tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide-calcium complex (PPH21-Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco-2 cell model tests revealed that the bioavailability of PPH21-Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%. Peanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide-calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry.

Light-Colored Maillard Peptides: Formation from Reduced Fluorescent Precursors of Browning and Enhancement of Saltiness Perception.

The browning formation and taste enhancement of peptides derived from soybean, peanut, and corn were studied in the light-colored Maillard reaction compared with the deep-colored reaction. The fluorescent compounds, as the browning precursors, were accumulated during the early Maillard reaction of peptides and subsequently degraded into dark substances, which resulted in a higher browning degree of deep-colored Maillard peptides (MPs), especially for the MPs derived from corn peptide. However, the addition of l-cysteine in light-colored Maillard reaction reduced the formation of deoxyosones and short-chain reactive α-dicarbonyls, thereby weakening the generation of fluorescent compounds and inhibited the browning of MPs. Synchronously, the peptides were thermally degraded into small peptides and amino acids, which were consumed less during light-colored thermal reaction due to its shorter reaction time at high temperature compared with deep-colored ones, thus contributing to a stronger saltiness perception of light-colored MPs than deep-colored MPs. Besides, the Maillard reaction products derived from soybean and peanut peptides possessed an obvious "kokumi" taste, making them suitable for enhancing the soup flavors.

Fast impedimetric immunosensing of IgGs associated with peanut and hazelnut allergens

Food allergies trigger a variety of clinical adverse symptoms and clinical evidence suggests that the presence of food allergy-related IgG can be helpful in the diagnosis when analyzed at the peptide-epitope level. To validate and select the peptides based on their specificity toward hazelnut or peanut epitopes, the authors of this study developed a silicon-based microchip coupled with click-chemistry bound peptides identified by the Fraunhofer Institute for Cell Therapy and Immunology. Peptides related to hazelnut and peanut allergies were identified and used to develop a silicon-based microchip. Peptides were coupled with click-chemistry to the sensor surface. The immunosensor was developed by electrografting diazotized amino phenylacetic acid and subsequently, dibenzocyclooctyne-amine (DBCO-NH2) was used as click-chemistry to allow coupling of the peptides with a C-terminal linker and azide structure. Energy-dispersive X-ray spectroscopy, electrochemical impedance spectroscopy (EIS), and fluorescence microscopy techniques have been used to analyze the bio-functionalization of the developed electrode. The peptide-epitope recognition was studied for seven allergen-derived peptides. The electrochemical responses were studied with sera from rabbits immunized with hazelnut and peanut powder. The microchips functionalized with the chosen peptides (peanut peptides T12 and EO13 and hazelnut peptides S4 and EO14 with an RSD of 4%, 3%, 9%, and 1% respectively) demonstrated their ability to specifically detect prevalent anti-nut related IgGs in rabbit sera in a range of dilutions from 1:500000 (0.0002%) until 1:50000 (0.002%). In addition, the other peptides showed promising differentiation abilities which can be further studied to perform multivariable detection fingerprint of anti-allergens in blood sera.

Purification and Identification of Novel Antioxidant Peptides from Hydrolysates of Peanuts (Arachis hypogaea) and Their Neuroprotective Activities.

Peanut (Arachis hypogaea) peptides have various functional activities and a high utilization value. This study aims to isolate and characterize antioxidant peptides from peanut protein hydrolysates and further evaluate their neuroprotection against oxidative damage to PC12 cells induced by 6-hydroxydopamine (6-OHDA). After the peanut protein was hydrolyzed with pepsin and purified using ultrafiltration and gel chromatography, six peptides were identified and sequenced by high-performance liquid chromatography (HPLC) and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Out of these six peptides, Pro-Gly-Cys-Pro-Ser-Thr (PGCPST) exhibited a desirable antioxidant capacity, as determined using the 1,1-diphenyl-2-picrylhydrazyl, 2,2-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt, and hydroxyl radical scavenging assays. Moreover, our results indicated that the peptide PGCPST effectively increased the cell viability and reduced the cell apoptosis in 6-OHDA-induced PC12. RNA sequencing further showed that the neuroprotective effect of the peptide PGCPST was mediated via sphingolipid metabolism-related pathways. With further research efforts, the peptide PGCPST was expected to develop into a new neuroprotective agent.

Development of a simplified, sensitive, and accurate LC-MS/MS method for peanut quantification in wheat flour-based dry matrices

ABSTRACT In this study, an ELISA-based method was observed to overestimate quantification of peanut in three wheat flour-based dry matrices (both raw and cooked). A reliable method using liquid chromatography tandem mass spectrometry (LC-MS/MS) was developed to quantify peanut accurately in these matrices. This method simplified both sample preparation and quantification compared with previous approaches, by digesting peanut proteins without reduction and alkylation and using Ara h 1 to build calibration curves. A significantly increased amount of peanut peptides was detected by heating the extracts. The sensitivity and linearity were superior to most commercial ELISA kits. The limit of quantification (LOQ) was 0.31 mg/kg total peanut in wheat flour and the linear range was between 0.3 and 40 mg/kg. This LC-MS/MS method could be applied as a confirmatory method for peanut allergen management when positive ELISA results raise suspicion of contamination.

Structural characterization of calcium-binding sunflower seed and peanut peptides and enhanced calcium transport by calcium complexes in Caco-2 cells.

Peptide-Ca complexes can promote Ca absorption. The present study aimed to determine the transport mechanism and structural characteristics of sunflower seed and peanut peptides with high Ca binding capacity with respect to developing third-generation Ca supplements and functional food ingredients. High Ca-binding fractions of 1-3 kDa sunflower seed peptide (SSP4 ) and ≥ 10 kDa peanut peptide (PP1 ) had higher amount of Ca transported than CaCl2 and two hydrolyzed proteins in Caco-2 cells. SSP4 and PP1 were separated by Ca ion metal chelate affinity chromatography, and high Ca-binding fractions were observed for SSP4 -P2 and PP1 -P2 . The amino acid sequences of SSP4 -P2 and PP1 -P2 were characterized by high-performance liquid chromatography-electrospray ionization-time of flight mass spectrometry. Seven and eight peptides were identified from SSP4 -P2 and PP1 -P2 , respectively. These peptides had molecular weights ranging from 1500 Da to 2500 Da and a large number of characteristic amino acid sequences, such as EEEQQQ, EQ-QQQ-QQ, QQ-QQQQQ, E-EEE, EE-EEQ, RR, Q-QQ-QQQ, EE-EQ-EE-Q, QQ-QQQQ, and Q-QQQQ, where 'E' is glutamic acid and 'Q' is glutamine. SSP4 and PP1 can promote Ca transport in Caco-2 cells without affecting cell permeability. The amino acid sequences of SSP4 -P2 and PP1 -P2 with high Ca-binding abilities contain characteristic sequences, such as continuous glutamic acid and glutamine, and have low molecular weights. © 2020 Society of Chemical Industry.

IgE to epitopes of Ara h 2 enhance the diagnostic accuracy of Ara h 2-specific IgE.

Understanding the discrepancy between IgE sensitization and allergic reactions to peanut could facilitate diagnosis and lead to novel means of treating peanut allergy. To identify differences in IgE and IgG4 binding to peanut peptides between peanut-allergic (PA) and peanut-sensitized but tolerant (PS) children. PA (n=56), PS (n=42) and nonsensitized nonallergic (NA, n=10) patients were studied. Synthetic overlapping 15-mer peptides of peanut allergens (Ara h 1-11) were spotted onto microarray slides, and patients' samples were tested for IgE and IgG4 binding using immunofluorescence. IgE and IgG4 levels to selected peptides were quantified using ImmunoCAP. Diagnostic model comparisons were performed using likelihood-ratio tests between each specified nominal logistic regression models. Seven peptides on Ara h 1, Ara h 2, and Ara h 3 were bound more by IgE of PA compared to PS patients on the microarray. IgE binding to one peptide on Ara h 5 and IgG4 binding to one Ara h 9 peptide were greater in PS than in PA patients. Using ImmunoCAP, IgE to the Ara h 2 peptides enhanced the diagnostic accuracy of Ara h 2-specific IgE. Ratios of IgG4/IgE to 4 out of the 7 peptides were higher in PS than in PA subjects. Ara h 2 peptide-specific IgE added diagnostic value to Ara h 2-specific IgE. Ability of peptide-specific IgG4 to surmount their IgE counterpart seems to be important in established peanut tolerance.

Preparation and structural characterization of peanut peptide–zinc chelate

ABSTRACT Peanut protein isolate was hydrolyzed by trypsin. The resulting peanut peptide fractions (PPF) were then divided into three molecular weight components by ultrafiltration (PPF1, MW >5 kDa; PPF2, 3 kDa < MW <5 kDa; PPF3, MW <3 kDa; and untreated PPF). Experiments showed that PPF3 had the best capacity for chelation with zinc. PPF3 and the PPF3–Zn chelate were characterized by Ultraviolet spectrophotometry, Fourier-transform infrared spectroscopy, X-ray diffraction, Scanning electron microscopy, Energy disperse spectroscopy, Fluorescence spectroscopy, and Thermogravimetric analysis. The results showed that the apparent characteristics and internal structures of PPF3 were changed by chelation of Zn2+. PPF3 contained sufficient metal-binding sites, with – COOH, – OH, and – NH2 potentially participating in coordination with Zn2+ to form the PPF3-Zn chelate. Furthermore, the results suggested that peanut peptides might chelate with zinc to act as an emerging carrier for zinc supplements.

Additional band broadening of peptides in the first size-exclusion chromatographic dimension of an automated stop-flow two-dimensional high performance liquid chromatography

The need to improve the peak capacity of liquid chromatography motivates the development of two-dimensional analysis systems. This paper presented a fully automated stop-flow two-dimensional liquid chromatography system with size exclusion chromatography followed by reversed phase liquid chromatography (SEC×RPLC) to efficiently separate peptides. The effects of different stop-flow operational parameters (stop-flow time, peak parking position, number of stop-flow periods and column temperature) on band broadening in the first dimension (1st D) SEC column were quantitatively evaluated by using commercial small proteins and peptides. Results showed that the effects of peak parking position and the number of stop-flow periods on band broadening were relatively small. Unlike stop-flow analysis of large molecules with a long running time, additional band broadening was evidently observed for small molecule analytes due to the relatively high effective diffusion coefficient (Deff). Therefore, shorter analysis time and lower 1st D column temperature were suggested for analyzing small molecules. The stop-flow two-dimensional liquid chromatography (2D-LC) system was further tested on peanut peptides and an evidently improved resolution was observed for both stop-flow heart-cutting and comprehensive 2D-LC analysis (in spite of additional band broadening in SEC). The stop-flow SEC×RPLC, especially heart-cutting analysis with shorter analysis time and higher 1st D resolution for selected fractions, offers a promising approach for efficient analysis of complex samples.

In vitro antithrombotic activities of peanut protein hydrolysates

The antithrombotic activities of peanut protein hydrolysates were investigated using a microplates assay. When peanut proteins were hydrolyzed to a limited extent by various enzymes, their thrombin inhibitory abilities were significantly enhanced. However, the resultant hydrolysates showed significantly different activities even at the same degrees of hydrolysis. The hydrolysates generated by Alcalase 2.4L displayed the best antithrombotic activities and the hydrolysis process was further optimized by response surface methodology. The antithrombotic activities were increased to 86% based on a protein concentration of 50mg/ml under the optimal conditions: pH 8.5, enzyme concentration of 5000IU/g of peanut proteins, and 2h hydrolysis time at 50°C. The Alcalase 2.4L crude hydrolysates were then fractionated successively by preparative and semi-preparative reverse-phase high-performance liquid chromatography (RP-HPLC). The peptide fraction collected inhibited thrombin-catalyzed coagulation of fibrinogen completely at a concentration of 0.4mg/ml, with an antithrombotic activity close to that of heparin at quite a low concentration (0.2mg/ml). This peptide fraction was further analyzed by online reverse-phase ultra-performance liquid chromatography (RP-UPLC) coupled to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS), and three new peptides were identified as Ser-Trp-Ala-Gln-Leu, Gly-Asn-His-Glu-Ala-Gly-Glu and Cys-Phe-Asn-Glu-Tyr-Glu, respectively. This research provided an effective way to produce antithrombotic peptides from peanut proteins, and also helped to elucidate the structure–function relationships of peanut peptides.

Isolation, purification and molecular mechanism of a peanut protein-derived ACE-inhibitory peptide.

Although a number of bioactive peptides are capable of angiotensin I-converting enzyme (ACE) inhibitory effects, little is known regarding the mechanism of peanut peptides using molecular simulation. The aim of this study was to obtain ACE inhibiting peptide from peanut protein and provide insight on the molecular mechanism of its ACE inhibiting action. Peanut peptides having ACE inhibitory activity were isolated through enzymatic hydrolysis and ultrafiltration. Further chromatographic fractionation was conducted to isolate a more potent peanut peptide and its antihypertensive activity was analyzed through in vitro ACE inhibitory tests and in vivo animal experiments. MALDI-TOF/TOF-MS was used to identify its amino acid sequence. Mechanism of ACE inhibition of P8 was analyzed using molecular docking and molecular dynamics simulation. A peanut peptide (P8) having Lys-Leu-Tyr-Met-Arg-Pro amino acid sequence was obtained which had the highest ACE inhibiting activity of 85.77% (half maximal inhibitory concentration (IC50): 0.0052 mg/ml). This peanut peptide is a competitive inhibitor and show significant short term (12 h) and long term (28 days) antihypertensive activity. Dynamic tests illustrated that P8 can be successfully docked into the active pocket of ACE and can be combined with several amino acid residues. Hydrogen bond, electrostatic bond and Pi-bond were found to be the three main interaction contributing to the structural stability of ACE-peptide complex. In addition, zinc atom could form metal-carboxylic coordination bond with Tyr, Met residues of P8, resulting into its high ACE inhibiting activity. Our finding indicated that the peanut peptide (P8) having a Lys-Leu-Tyr-Met-Arg-Pro amino acid sequence can be a promising candidate for functional foods and prescription drug aimed at control of hypertension.

Isolation And Identification Of An Antioxidant Peptide Prepared From Fermented Peanut Meal Using Bacillus Subtilis Fermentation

In order to recover and utilize peanut protein resource, peanut meal was fermented using Bacillus subtilis to prepare antioxidant peptides in this study. The antioxidant activities of the peanut peptides were evaluated via six in vitro tests, namely, 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) scavenging activity, inhibition of linoleic acid autoxidation, reducing power, and metal chelating capacity. The peanut peptides showed 63.28% of scavenging effect on 1,1-diphenyl-2-picrylhydrazyl radical, 70.67% of scavenging effect on 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) and 39.32% of superoxide anion radical scavenging activity at 1.0 mg/ml, and 62.69% of inhibition on linoleic acid autooxidation at 0.8 mg/ml. Besides, the peanut peptides exhibited 32.8% of reducing power and 60.44% of Fe2+-chelating capacity at 2 mg/ml. Then the peanut peptides were desalted with macroporous resin; the fraction eluted with 75% ethanol showed the highest scavenging activity on 1,1-diphenyl-2-picrylhydrazyl radical. This fraction was subject to further purification using gel filtration chromatography and reverse phase-high performance liquid chromatography. At last, a peptide was gained, and it was identified to be Tyr-Pro with matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry. The results indicated that it is feasible to prepare natural antioxidants from peanut meal using B. subtilis fermentation.

Legume Genetics and Genomics: Recent Advances

Legumes are the major source for providing worldwide human food, animal feed and forage. They constitute one of the major plant groups that provide key components including proteins in the diets of resource-poor people in the world including semi-arid tropic regions. Grain legumes accounts for 27 % of the world’s primary crop production and 33 % of the dietary proteins [1]. In addition, grain legumes may be used to make bread, doughnuts, chips, snacks etc. [2]. Consumption of legumes in diet complements the nutritional profiles of cereals and tubers [1]. Some of these legumes have been used as medicine. For instance, Isoflavones from soybean and other legumes have been used to lower risk of cancer and lower serum cholesterol level [2] and thereby helps to improve overall health of human beings. Besides, legumes also sometimes serve as model crop plants for the improvement of other crops. In order to discuss the advances made in the area of legume biology the VI international conference on Legume Genetics and Genomics (ICLGG) was organized in Hyderabad, India during October 2–7, 2012. With more than 500 participants from 44 countries, it emerged as the biggest ICLGG conferences so far. It was 6th meeting in the series of ICLGG that were held earlier in USA (I & V), France (II), Australia (III) and Mexico (IV). The conference had 10 themes covered in 11 sessions with theme symbiosis and development split in two sessions. The other themes included: (i) Next Generation Genomics, (ii) Evolution and Diversity, (iii) Harnessing Germplasm Resources, (iv) Abiotic Stress, (v) Pathogenesis and Disease Resistance, (vi) Genomic Resources and Trait Mapping, (vii) Genomics-Assisted Breeding, (viii) Nutrition and Quality and (ix) Translational Genomics. All these sessions covered the entire aspects of legume genetics and genomics. In addition, a special session on ‘‘Young Scientists in Legume Genetics and Genomics’’ had presentations from eight young scientists representing range of legume crops, disciplines and countries. The details of conference program are available at http://www.icrisat.org/gt-bt/VI-ICLGG/Homepage.htm. During the conference, a total of 63 presentations were made with 57 % of them selected from the abstracts submitted by the participants, while the remaining abstracts were presented in the poster sessions. Huge amount of information has now been generated on various aspects of legumes crops and most of this was presented during this conference. However, only the summary of some selected talks is presented in this report. The innovativeness which was observed during the conference was that each poster presenter was given 1 min to talk about his/her poster before all the participants and the best performers in each theme were given awards during the closing ceremony of the conference. Several workshops were also organised before the start of actual conference on October 2, 2012, which included workshop on mungbean, the peanut genome project, small RNAs and peptides, and FabaTropiMed (an integrated project on the ecological services of legumes that is carried out through a cooperative research in six agro-ecosystems of Africa under Mediterranean or tropical climate), while R. R. Mir (&) Division of Plant Breeding & Genetics, Shere-Kashmir University of Agricultural Sciences & Technology of Jammu (SKUAST-J), Chatha, Jammu 180009, J&K, India e-mail: imrouf2006@gmail.com

Evaluation of Physicochemical and Antioxidant Properties of Peanut Protein Hydrolysate

Peanut protein and its hydrolysate were compared with a view to their use as food additives. The effects of pH, temperature and protein concentration on some of their key physicochemical properties were investigated. Compared with peanut protein, peanut peptides exhibited a significantly higher solubility and significantly lower turbidity at pH values 2–12 and temperature between 30 and 80°C. Peanut peptide showed better emulsifying capacity, foam capacity and foam stability, but had lower water holding and fat adsorption capacities over a wide range of protein concentrations (2–5 g/100 ml) than peanut protein isolate. In addition, peanut peptide exhibited in vitro antioxidant properties measured in terms of reducing power, scavenging of hydroxyl radical, and scavenging of DPPH radical. These results suggest that peanut peptide appeared to have better functional and antioxidant properties and hence has a good potential as a food additive.

Optimization of a Microwave-Coupled Enzymatic Digestion Process to Prepare Peanut Peptides

The best enzyme to prepare peanut peptides, papain, coupled with microwave irradiation was selected from five common proteases according to the results of the yield of peanut peptides [nitrogen solution index (NSI) in trichloroacetic acid (TCA), TCA-NSI] and the degree of hydrolysis (DH). The main factors that influenced the microwave-coupled enzymatic digestion method were optimized by response surface analysis. The optimal conditions obtained were as follows: microwave extraction time, 9.5 min; power, 600 W; substrate concentration, 4%; enzymatic reaction temperature, 50 °C; enzyme quantity, 6,500 U/g; pH, 7.1 (phosphate buffer, 0.05 mol/L). Under these conditions, TCA-NSI was 62.00% and DH was 25.89%, which is higher than that obtained with either protease hydrolysis or microwave hydrolysis alone.