International Science Index

22
10008822
Antibody Reactivity of Synthetic Peptides Belonging to Proteins Encoded by Genes Located in Mycobacterium tuberculosis-Specific Genomic Regions of Differences
Abstract:

The comparisons of mycobacterial genomes have identified several Mycobacterium tuberculosis-specific genomic regions that are absent in other mycobacteria and are known as regions of differences. Due to M. tuberculosis-specificity, the peptides encoded by these regions could be useful in the specific diagnosis of tuberculosis. To explore this possibility, overlapping synthetic peptides corresponding to 39 proteins predicted to be encoded by genes present in regions of differences were tested for antibody-reactivity with sera from tuberculosis patients and healthy subjects. The results identified four immunodominant peptides corresponding to four different proteins, with three of the peptides showing significantly stronger antibody reactivity and rate of positivity with sera from tuberculosis patients than healthy subjects. The fourth peptide was recognized equally well by the sera of tuberculosis patients as well as healthy subjects. Predication of antibody epitopes by bioinformatics analyses using ABCpred server predicted multiple linear epitopes in each peptide. Furthermore, peptide sequence analysis for sequence identity using BLAST suggested M. tuberculosis-specificity for the three peptides that had preferential reactivity with sera from tuberculosis patients, but the peptide with equal reactivity with sera of TB patients and healthy subjects showed significant identity with sequences present in nob-tuberculous mycobacteria. The three identified M. tuberculosis-specific immunodominant peptides may be useful in the serological diagnosis of tuberculosis.

Paper Detail
95
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21
10008984
Identification of Promiscuous Epitopes for Cellular Immune Responses in the Major Antigenic Protein Rv3873 Encoded by Region of Difference 1 of Mycobacterium tuberculosis
Abstract:

Rv3873 is a relatively large size protein (371 amino acids in length) and its gene is located in the immunodominant genomic region of difference (RD)1 that is present in the genome of Mycobacterium tuberculosis but deleted from the genomes of all the vaccine strains of Bacillus Calmette Guerin (BCG) and most other mycobacteria. However, when tested for cellular immune responses using peripheral blood mononuclear cells from tuberculosis patients and BCG-vaccinated healthy subjects, this protein was found to be a major stimulator of cell mediated immune responses in both groups of subjects. In order to further identify the sequence of immunodominant epitopes and explore their Human Leukocyte Antigen (HLA)-restriction for epitope recognition, 24 peptides (25-mers overlapping with the neighboring peptides by 10 residues) covering the sequence of Rv3873 were synthesized chemically using fluorenylmethyloxycarbonyl chemistry and tested in cell mediated immune responses. The results of these experiments helped in the identification of an immunodominant peptide P9 that was recognized by people expressing varying HLA-DR types. Furthermore, it was also predicted to be a promiscuous binder with multiple epitopes for binding to HLA-DR, HLA-DP and HLA-DQ alleles of HLA-class II molecules that present antigens to T helper cells, and to HLA-class I molecules that present antigens to T cytotoxic cells. In addition, the evaluation of peptide P9 using an immunogenicity predictor server yielded a high score (0.94), which indicated a greater probability of this peptide to elicit a protective cellular immune response. In conclusion, P9, a peptide with multiple epitopes and ability to bind several HLA class I and class II molecules for presentation to cells of the cellular immune response, may be useful as a peptide-based vaccine against tuberculosis.

Paper Detail
38
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20
10007846
Effect of Fat Percentage and Prebiotic Composition on Proteolysis, ACE-Inhibitory and Antioxidant Activity of Probiotic Yogurt
Abstract:
In recent years, the consumption of functional foods, including foods containing probiotic bacteria, has come to notice. Milk proteins have been identified as a source of angiotensin-I-converting enzyme )ACE( inhibitory peptides and are currently the best-known class of bioactive peptides. In this study, the effects of adding prebiotic ingredients (inulin and wheat fiber) and fat percentage (0%, 2% and 3.5%) in yogurt containing probiotic Lactobacillus casei on physicochemical properties, degree of proteolysis, antioxidant and ACE-inhibitory activity within 21 days of storage at 5 ± 1 °C were evaluated. The results of statistical analysis showed that the application of prebiotic compounds led to a significant increase in water holding capacity, proteolysis and ACE-inhibitory of samples. The degree of proteolysis in yogurt increases as storage time elapses (P < 0.05) but when proteolysis exceeds a certain threshold, this trend begins to decline. Also, during storage time, water holding capacity reduced initially but increased thereafter. Moreover, based on our findings, the survival of Lactobacillus casei in samples treated with inulin and wheat fiber increased significantly in comparison to the control sample (P < 0.05) whereas the effect of fat percentage on the survival of probiotic bacteria was not significant (P = 0.095). Furthermore, the effect of prebiotic ingredients and the presence of probiotic cultures on the antioxidant activity of samples was significant (P < 0.05).
Paper Detail
274
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19
10007365
Displaying of GnRH Peptides on Bacteriophage T7 and Its Immunogenicity in Mice Model
Abstract:

T7 phage could be used as a perfect vector for peptides expression and haptens presentation. T7-3GnRH recombinant phage was constructed by inserting three copies of Gonadotrophin Releasing Hormone (GnRH) gene into the multiple cloning site of T7 Select 415-1b phage genome. The positive T7-3GnRH phage was selected by using polymerase chain reaction amplification, and the p10B-3GnRH fusion protein was verified by SDS-PAGE and Western-blotting assay. T7-3GnRH vaccine was made and immunized with 1010 pfu in 0.2 ml per dose in mice. Blood samples were collected at an interval in weeks, and anti-GnRH antibody and testosterone concentrations were detected by ELISA and radioimmunoassay, respectively. The results show that T7-3GnRH phage particles confer a high immunogenicity to the GnRH-derived epitope. Moreover, the T7-3GnRH vaccine induced higher level of anti-GnRH antibody than ImproVac®. However, the testosterone concentrations in both immunized groups were at a similar level, and the testis developments were significantly inhibited compared to controls. These findings demonstrated that the anti-GnRH antibody could neutralize the endogenous GnRH to down regulate testosterone level and limit testis development, highlighting the potential value of T7-3GnRH in the immunocastration vaccine research.

Paper Detail
222
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18
10005501
Radiochemical Purity of 68Ga-BCA-Peptides: Separation of All 68Ga Species with a Single iTLC Strip
Abstract:
In the present study, highly effective iTLC single strip method for the determination of radiochemical purity (RCP) of 68Ga-BCA-peptides was developed (with no double-developing, changing of eluents or other additional manipulation). In this method iTLC-SG strips and commonly used eluent TFAaq. (3-5 % (v/v)) are used. The method allows determining each of the key radiochemical forms of 68Ga (colloidal, bound, ionic) separately with the peaks separation being no less than 4 σ. Rf = 0.0-0.1 for 68Ga-colloid; Rf = 0.5-0.6 for 68Ga-BCA-peptides; Rf = 0.9-1.0 for ionic 68Ga. The method is simple and fast: For developing length of 75 mm only 4-6 min is required (versus 18-20 min for pharmacopoeial method). The method has been tested on various compounds (including 68Ga-DOTA-TOC, 68Ga-DOTA-TATE, 68Ga-NODAGA-RGD2 etc.). The cross-validation work for every specific form of 68Ga showed good correlation between method developed and control (pharmacopoeial) methods. The method can become convenient and much more informative replacement for pharmacopoeial methods, including HPLC.
Paper Detail
686
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17
10004204
Investigations of Protein Aggregation Using Sequence and Structure Based Features
Abstract:

The main cause of several neurodegenerative diseases such as Alzhemier, Parkinson and spongiform encephalopathies is formation of amyloid fibrils and plaques in proteins. We have analyzed different sets of proteins and peptides to understand the influence of sequence based features on protein aggregation process. The comparison of 373 pairs of homologous mesophilic and thermophilic proteins showed that aggregation prone regions (APRs) are present in both. But, the thermophilic protein monomers show greater ability to ‘stow away’ the APRs in their hydrophobic cores and protect them from solvent exposure. The comparison of amyloid forming and amorphous b-aggregating hexapeptides suggested distinct preferences for specific residues at the six positions as well as all possible combinations of nine residue pairs. The compositions of residues at different positions and residue pairs have been converted into energy potentials and utilized for distinguishing between amyloid forming and amorphous b-aggregating peptides. Our method could correctly identify the amyloid forming peptides at an accuracy of 95-100% in different datasets of peptides.

Paper Detail
514
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16
9999360
Proteolysis in Serbian Traditional Dry Fermented Sausage Petrovská klobása as Influenced by Different Ripening Processes
Abstract:

The aim of the study was to determine how different ripening processes (traditional vs. industrial) influenced the proteolysis in traditional Serbian dry-fermented sausage Petrovská klobása. The obtained results indicated more intensive pH decline (0.7 units after 9 days) in industrially ripened products (I), what had a positive impact on drying process and proteolytic changes in these samples. Thus, moisture content in I sausages was lower at each sampling time, amounting 24.7% at the end of production period (90 days). Likewise, the process of proteolysis was more pronounced in I samples, resulting in higher contents of non-protein nitrogen (NPN) and free amino acids nitrogen (FAAN), as well as in faster and more intensive degradation of myosin (≈220 kDa), actin (≈45 kDa) and other polypeptides during processing. Consequently, the appearance and accumulation of several protein fragments were registered.

Paper Detail
3758
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15
9999257
Comparative Studies on Interactions of Synthetic and Natural Compounds with Hen Egg-White Lysozyme
Abstract:

Amyloid aggregation of polypeptides is related to a growing number of pathologic states known as amyloid disorders. In recent years, blocking or reversing amyloid aggregation via the use of small compounds are considered as two useful approaches in hampering the development of these diseases. In this research, we have compared the ability of several manganese-salen derivatives, as synthetic compounds, and apigenin, as a natural flavonoid, to inhibit of hen egg-white lysozyme (HEWL) aggregation, as an in vitro model system. Different spectroscopic analyses such as Thioflavin T (ThT) and Anilinonaphthalene-8-sulfonic acid (ANS) fluorescence, Congo red (CR) absorbance along with transmission electron microscopy were used in this work to monitor the HEWL aggregation kinetic and inhibition. Our results demonstrated that both type of compounds were capable to prevent the formation of lysozyme amyloid aggregation in vitro. In addition, our data indicated that synthetic compounds had higher activity to inhibit of the β-sheet structures relative to natural compound. Regarding the higher antioxidant activities of the salen derivatives, it can be concluded that in addition to aromatic rings of each of the compounds, the potent antioxidant properties of salen derivatives contributes to lower lysozyme fibril accumulation.

Paper Detail
1512
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14
9999387
Antioxidant and Aِntimicrobial Properties of Peptides as Bioactive Components in Beef Burger
Abstract:

Dried soy protein hydrolysate powder was added to the burger in order to enhance the oxidative stability as well as decreases the microbial spoilage. The soybean bioactive compounds (soy protein hydrolysate) as antioxidant and antimicrobial were added at level of 1, 2 and 3 %.Chemical analysis and physical properties were affected by protein hydrolysate addition. The TBA values were significantly affected (P < 0.05) by the storage period and the level of soy protein hydrolysate. All the tested soybean protein hydrolysate additives showed strong antioxidant properties. Samples of soybean protein hydrolysate showed the lowest (P < 0.05) TBA values at each time of storage. The counts of all determined microbiological indicators were significantly (P < 0.05) affected by the addition of the soybean protein hydrolysate. Decreasing trends of different extent were also observed in samples of the treatments for total viable counts, Coliform, Staphylococcus aureus, yeast and molds. Storage period was being significantly (P < 0.05) affected on microbial counts in all samples Staphylococcus aureus were the most sensitive microbe followed by Coliform group of the sample containing protein hydrolysate, while molds and yeast count showed a decreasing trend but not significant (P < 0.05) until the end of the storage period compared with control sample. Sensory attributes were also performed, added protein hydrolysate exhibits beany flavor which was clear about samples of 3% protein hydrolysate.

Paper Detail
1490
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13
9999150
Quality Characterization of Burger Affected by Soybean Additives (Natto & Protein Hydrolysate) and Ascorbic Acid
Abstract:

Soy protein is a common ingredient added to processed meats to enhance its functional characteristics. In our study, soybean products (fermented soy Natto and protein hydrolysate) containing hydrolyzed peptides and amino acids, with or without ascorbic acid were added to burger in order to improve its quality characteristics. Results showed that soy additives significantly increased moisture and protein content and reduced (P < 0.05) fat values. Ash content did not affect with Natto additive. Color tools, lightness and yellowness were higher (P<0.05) for the samples with added soybean products (with or without ascorbic acid), while redness decreased. Both of protein hydrolysate and ascorbic acid increased the softiness while, Natto additive increased the hardness of samples. Natto & protein hydrolysate additives increased the total volatile basic nitrogen while, samples with ascorbic acid decreased TVBN values at significant levels. Also, soy additives were improved both of cooking quality and sensory evaluation of the burger in order to prove that soy products actually affect the quality characteristics of meat products.

Paper Detail
1196
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12
9998620
Utilization of Bioactive Components Produced from Fermented Soybean (Natto) in Beef Burger
Abstract:

Soybean Natto powder was added to the burger in order to enhance the oxidative stability as well as decreases the microbial spoilage. The soybean bioactives compound (soybean Natto) as antioxidant and antimicrobial were added at level of 1, 2 and 3%. Chemical analysis and physical properties were affected by soybean Natto addition. All the tested soybean Natto additives showed strong antioxidant properties. The microbiological indicators were significantly (P < 0.05) affected by the addition of the soybean Natto. Decreasing trends of different extent were also observed in samples of the treatments for total viable counts, Coliform, Staphylococcus aureus, yeast and molds. Storage period was significantly (P < 0.05) affected on microbial counts in all samples Staphylococcus aureus were the most sensitive microbe followed by Coliform group of the sample containing soybean Natto. Sensory attributes were also performed, added soybean Natto exhibits beany flavor which was clear about samples of 3% soybean Natto.

Paper Detail
1570
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11
9997576
New Kinetic Approach to the Enzymatic Hydrolysis of Proteins – A Case of Thermolysin-Catalyzed Albumin
Abstract:

Using an enzyme of known specificity the hydrolysis of protein was carried out in a controlled manner. The aim was to obtain oligopeptides being the so-called active peptides or their direct precursors. An original way of expression of the protein hydrolysis kinetics was introduced. Peptide bonds contained in the protein were recognized as a diverse-quality substrate for hydrolysis by the applied protease. This assumption was positively verified taking as an example the hydrolysis of albumin by thermolysin. Peptide linkages for this system should be divided into at least four groups. One of them is a group of bonds non-hydrolyzable by this enzyme. These that are broken are hydrolyzed at a rate that differs even by tens of thousands of times. Designated kinetic constants were k'F = 10991.4 L/g.h, k'M = 14.83L/g.h, k'S about 10-1 L/g.h for fast, medium and slow bonds, respectively. Moreover, a procedure for unfolding of the protein, conducive to the improved susceptibility to enzymatic hydrolysis (approximately three-fold increase in the rate) was proposed.

Paper Detail
1998
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10
17073
Partial Purification of Cytotoxic Peptides against Gastric Cancer Cells from Protein Hydrolysate of Euphorbia hirta Linn.
Abstract:

Protein hydrolysates prepared from a number of medicinal plants are promising sources of various bioactive peptides. In this work, proteins from dried whole plant of Euphorbia hirta Linn. were extracted and digested with pepsin for 12h. The hydrolysates of lesser than 3 KDa were fractionated by a cut-off membrane. The peptide hydrolysate was then purified by an anion-exchange chromatography on DEAE-Sephacel™ column and reverse-phase chromatography on Sep-pak C18 column, respectively. The cytotoxic effect of each peptide fraction against a gastric carcinoma cell line (KATO-III, ATCC No. HTB103) was investigated using colorimetric MTT viability assay. A human liver cell line (Chang Liver, CLS No. 300139) was used as a control normal cell line. Two purified peptide peaks, peak l and peak ll at 100µg peptides mL-1 affected cell viability of the gastric cancer cell lines to 63.85±4.94 and 66.92±6.46%, respectively. Our result showed for the first time that the peptide fractions derived from protein hydrolysate of Euphorbia hirta Linn. have anti-gastric cancer activity, which offers a potential novel and natural anti-gastric cancer remedy.

Paper Detail
1536
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9
16297
Characterization of Antioxidant Peptides of Soybean Protein Hydrolysate
Abstract:

In order to characterize the soy protein hydrolysate obtained in this study, gel chromatography on Sephadex G-25 was used to perform the separation of the peptide mixture and electrophoresis in SDS-polyacrylamide gel has been employed. Protein hydrolysate gave high antioxidant activities, but didn't give any antimicrobial activities. The antioxidant activities of protein hydrolysate was in the same trend of peptide content which gave high antioxidant activities and high peptide content between fractions 15 to 50. With increasing peptide concentrations, the scavenging effect on DPPH radical increased until about 70%, thereafter reaching a plateau. In compare to different concentrations of BHA, which exhibited higher activity (90%), soybean protein hydrolysate exhibited high antioxidant activities (70%) at a concentration of 1.45 mg/ml at fraction 25. Electrophoresis analysis indicated that, low- MW hydrolysate fractions (F1) appeared, on average, to have higher DPPH scavenging activities than high-MW fractions. These results revealed that soybean peptides probably contain substances that were proton donors and could react with free radicals to convert them to stable diamagnetic molecules. 

Paper Detail
3763
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8
9560
Preparation and Bioevaluation of DOTA-Cyclic RGD Peptide Dimer Labeled with 68Ga
Abstract:

Radiolabeled cyclic RGD peptides targeting integrin αvβ3 are reported as promising agents for the early diagnosis of metastatic tumors. With an aim to improve tumor uptake and retention of the peptide, cyclic RGD peptide dimer E[c (RGDfK)] 2 (E = Glutamic acid, f = phenyl alanine, K = lysine) coupled to the bifunctional chelator DOTA was custom synthesized and radiolabelled with 68Ga. Radiolabelling of cyclic RGD peptide dimer with 68Ga was carried out using HEPES buffer and biological evaluation of the complex was done in nude mice bearing HT29 tumors.

Paper Detail
1724
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7
4955
Quantification of Peptides based on Isotope Dilution Surface Enhanced Raman Scattering
Abstract:
This study aims to demonstrate the quantification of peptides based on isotope dilution surface enhanced Raman scattering (IDSERS). SERS spectra of phenylalanine (Phe), leucine (Leu) and two peptide sequences TGQIFK (T13) and YSFLQNPQTSLCFSESIPTPSNR (T6) as part of the 22-kDa human growth hormone (hGH) were obtained on Ag-nanoparticle covered substrates. On the basis of the dominant Phe and Leu vibrational modes, precise partial least squares (PLS) prediction models were built enabling the determination of unknown T13 and T6 concentrations. Detection of hGH in its physiological concentration in order to investigate the possibility of protein quantification has been achieved.
Paper Detail
1078
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6
13949
Bioactive Component in Milk and Dairy Product
Abstract:
Recent research has shown that milk proteins can yield bioactive peptides with opioid, mineral binding, cytomodulatory, antihypertensive, immunostimulating, antimicrobial and antioxidative activity in the human body. Bioactive peptides are encrypted in milk proteins and are only released by enzymatic hydrolysis in vivo during gastrointestinal digestion, food processing or by microbial enzymes in fermented products. At present significant research is being undertaken on the health effects of bioactive peptides. A variety of naturally formed bioactive peptides have been found in fermented dairy products, such as yoghurt, sour milk and cheese. In particular, antihypertensive peptides have been identified in fermented milks, whey and ripened cheese. Some of these peptides have been commercialized in the form of fermented milks. Bioactive peptides have the potential to be used in the formulation of health-enhancing nutraceuticals, and as potent drugs with well defined pharmacological effects.
Paper Detail
3094
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5
8237
An Information Theoretic Approach to Rescoring Peptides Produced by De Novo Peptide Sequencing
Abstract:
Tandem mass spectrometry (MS/MS) is the engine driving high-throughput protein identification. Protein mixtures possibly representing thousands of proteins from multiple species are treated with proteolytic enzymes, cutting the proteins into smaller peptides that are then analyzed generating MS/MS spectra. The task of determining the identity of the peptide from its spectrum is currently the weak point in the process. Current approaches to de novo sequencing are able to compute candidate peptides efficiently. The problem lies in the limitations of current scoring functions. In this paper we introduce the concept of proteome signature. By examining proteins and compiling proteome signatures (amino acid usage) it is possible to characterize likely combinations of amino acids and better distinguish between candidate peptides. Our results strongly support the hypothesis that a scoring function that considers amino acid usage patterns is better able to distinguish between candidate peptides. This in turn leads to higher accuracy in peptide prediction.
Paper Detail
1135
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4
13224
Structural Basis of Resistance of Helicobacterpylori DnaK to Antimicrobial Peptide Pyrrhocoricin
Abstract:

Bacterial molecular chaperone DnaK plays an essential role in protein folding, stress response and transmembrane targeting of proteins. DnaKs from many bacterial species, including Escherichia coli, Salmonella typhimurium and Haemophilus infleunzae are the molecular targets for the insect-derived antimicrobial peptide pyrrhocoricin. Pyrrhocoricin-like peptides bind in the substrate recognition tunnel. Despite the high degree of crossspecies sequence conservation in the substrate-binding tunnel, some bacteria are not sensitive to pyrrhocoricin. This work addresses the molecular mechanism of resistance of Helicobacter pylori DnaK to pyrrhocoricin. Homology modelling, structural and sequence analysis identify a single aminoacid substitution at the interface between the lid and the β-sandwich subdomains of the DnaK substrate-binding domain as the major determinant for its resistance.

Paper Detail
1215
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3
10460
Wasp Venom Peptides may play a role in the Pathogenesis of Acute Disseminated Encephalomyelitis in Humans: A Structural Similarity Analysis
Abstract:
Acute disseminated encephalomyelitis (ADEM) has been reported to develop after a hymenoptera sting, but its pathogenesis is not known in detail. Myelin basic protein (MBP)- specific T cells have been detected in the blood of patients with ADEM, and a proportion of these patients develop multiple sclerosis (MS). In an attempt to understand the mechanisms underlying ADEM, molecular mimicry between hymenoptera venom peptides and the human immunodominant MBP peptide was scrutinized, based on the sequence and structural similarities, whether it was the root of the disease. The results suggest that the three wasp venom peptides have low sequence homology with the human immunodominant MBP residues 85-99. Structural similarity analysis among the three venom peptides and the MS-related HLA-DR2b (DRA, DRB1*1501)-associated immunodominant MHC binding/TCR contact residues 88-93, VVHFFK showed that hyaluronidase residues 7-12, phospholipase A1 residues 98-103, and antigen 5 residues 109-114 showed a high degree of similarity 83.3%, 100%, and 83.3% respectively. In conclusion, some wasp venom peptides, particularly phospholipase A1, may potentially act as the molecular motifs of the human 3HLA-DR2b-associated immunodominant MBP88-93, and possibly present a mechanism for induction of wasp sting-associated ADEM.
Paper Detail
1020
downloads
2
7718
Molecular Dynamics and Circular Dichroism Studies on Aurein 1.2 and Retro Analog
Abstract:
Aurein 1.2 is a 13-residue amphipathic peptide with antibacterial and anticancer activity. Aurein1.2 and its retro analog were synthesized to study the activity of the peptides in relation to their structure. The antibacterial test result showed the retro-analog is inactive. The secondary structural analysis by CD spectra indicated that both of the peptides at TFE/Water adopt alpha-helical conformation. MD simulation was performed on aurein 1.2 and retro-analog in water and TFE in order to analyse the factors that are involved in the activity difference between retro and the native peptide. The simulation results are discussed and validated in the light of experimental data from the CD experiment. Both of the peptides showed a relatively similar pattern for their hydrophobicity, hydrophilicity, solvent accessible surfaces, and solvent accessible hydrophobic surfaces. However, they showed different in directions of dipole moment of peptides. Also, Our results further indicate that the reversion of the amino acid sequence affects flexibility .The data also showed that factors causing structural rigidity may decrease the activity. Consequently, our finding suggests that in the case of sequence-reversed peptide strategy, one has to pay attention to the role of amino acid sequence order in making flexibility and role of dipole moment direction in peptide activity. KeywordsAntimicrobial peptides, retro, molecular dynamic, circular dichroism.
Paper Detail
1280
downloads
1
15
The Impact of Germination and In Vitro Digestion on the Formation of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides from Lentil Proteins Compared to Whey Proteins
Abstract:
Biologically active peptides are of particular interest in food science and human nutrition because they have been shown to play several physiological roles. In vitro gastrointestinal digestion of lentil and whey proteins in this study produced high angiotensin-I converting enzyme inhibitory activity with 75.5±1.9 and 91.4±2.3% inhibition, respectively. High ACE inhibitory activity was observed in lentil after 5 days of germination (84.3±1.2%). Fractionation by reverse phase chromatography gave inhibitory activities as high as 86.3±2.0 for lentil, 94.8±1.8% for whey and 93.7±1.7% at 5th day of germination. Further purification by HPLC resulted in several inhibitory peptides with IC50 values ranging from 0.064 to 0.164 mg/ml. These results demonstrate that lentil proteins are a good source of peptides with ACE inhibitory activity that can be released by germination or gastrointestinal digestion. Despite the lower bioactivity in comparison with whey proteins, incorporation of lentil proteins in functional food formulations and natural drugs look promising.
Paper Detail
1673
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