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Richard J Fitzgerald - One of the best experts on this subject based on the ideXlab platform.
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Variable Glycemic Responses to Intact and Hydrolyzed Milk Proteins in Overweight and Obese Adults Reveal the Need for Precision Nutrition.
The Journal of nutrition, 2019Co-Authors: Aoife M. Curran, Alice B Nongonierma, Richard J Fitzgerald, Solène Le Maux, Katy Horner, Victoria O’sullivan, Eoin G. Murphy, Phil M. Kelly, Lorraine BrennanAbstract:Background Dietary modifications can contribute to improved pancreatic β cell function and enhance glycemic control. Objectives The objectives of this study were as follows: 1) to investigate the potential of Milk Protein Hydrolysates to modulate postprandial glucose response; 2) to assess individual responses; and 3) to explore the inter- and intraindividual reproducibility of the response. Methods A 14-d randomized crossover study investigated interstitial glucose levels of participants in response to 12% w/v Milk Protein drinks (intact caseinate and casein hydrolysate A and B) consumed in random order with a 2-d washout between treatments. Milk Protein drinks were consumed immediately prior to study breakfast and evening meals. Twenty participants (11 men, 9 women) aged 50 ± 8 y with a body mass index (in kg/m2) of 30.2 ± 3.1 were recruited. Primary outcome was glucose levels assessed at 15-min intervals with the use of glucose monitors. Results Repeated-measures ANOVA revealed that for breakfast there was a significant difference across the 3 treatment groups (P = 0.037). The ability to reduce postprandial glucose was specific to casein hydrolysate B in comparison with intact caseinate (P = 0.039). However, despite this significant difference, further examination revealed that only 3 out of 18 individuals were classified as responders (P
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Enhancing bioactive peptide release and identification using targeted enzymatic hydrolysis of Milk Proteins
Analytical and Bioanalytical Chemistry, 2018Co-Authors: Alice B Nongonierma, Richard J FitzgeraldAbstract:Milk Proteins have been extensively studied for their ability to yield a range of bioactive peptides following enzymatic hydrolysis/digestion. However, many hurdles still exist regarding the widespread utilization of Milk Protein-derived bioactive peptides as health enhancing agents for humans. These mostly arise from the fact that most Milk Protein-derived bioactive peptides are not highly potent. In addition, they may be degraded during gastrointestinal digestion and/or have a low intestinal permeability. The targeted release of bioactive peptides during the enzymatic hydrolysis of Milk Proteins may allow the generation of particularly potent bioactive Hydrolysates and peptides. Therefore, the development of Milk Protein Hydrolysates capable of improving human health requires, in the first instance, optimized targeted release of specific bioactive peptides. The targeted hydrolysis of Milk Proteins has been aided by a range of in silico tools. These include peptide cutters and predictive modeling linking bioactivity to peptide structure [i.e., molecular docking, quantitative structure activity relationship (QSAR)], or hydrolysis parameters [design of experiments (DOE)]. Different targeted enzymatic release strategies employed during the generation of Milk Protein Hydrolysates are reviewed herein and their limitations are outlined. In addition, specific examples are provided to demonstrate how in silico tools may help in the identification and discovery of potent Milk Protein-derived peptides. It is anticipated that the development of novel strategies employing a range of in silico tools may help in the generation of Milk Protein Hydrolysates containing potent and bioavailable peptides, which in turn may be used to validate their health promoting effects in humans. Graphical abstractThe targeted enzymatic hydrolysis of Milk Proteins may allow the generation of highly potent and bioavailable bioactive peptides.
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Enhancing bioactive peptide release and identification using targeted enzymatic hydrolysis of Milk Proteins
Analytical and bioanalytical chemistry, 2017Co-Authors: Alice B Nongonierma, Richard J FitzgeraldAbstract:Milk Proteins have been extensively studied for their ability to yield a range of bioactive peptides following enzymatic hydrolysis/digestion. However, many hurdles still exist regarding the widespread utilization of Milk Protein-derived bioactive peptides as health enhancing agents for humans. These mostly arise from the fact that most Milk Protein-derived bioactive peptides are not highly potent. In addition, they may be degraded during gastrointestinal digestion and/or have a low intestinal permeability. The targeted release of bioactive peptides during the enzymatic hydrolysis of Milk Proteins may allow the generation of particularly potent bioactive Hydrolysates and peptides. Therefore, the development of Milk Protein Hydrolysates capable of improving human health requires, in the first instance, optimized targeted release of specific bioactive peptides. The targeted hydrolysis of Milk Proteins has been aided by a range of in silico tools. These include peptide cutters and predictive modeling linking bioactivity to peptide structure [i.e., molecular docking, quantitative structure activity relationship (QSAR)], or hydrolysis parameters [design of experiments (DOE)]. Different targeted enzymatic release strategies employed during the generation of Milk Protein Hydrolysates are reviewed herein and their limitations are outlined. In addition, specific examples are provided to demonstrate how in silico tools may help in the identification and discovery of potent Milk Protein-derived peptides. It is anticipated that the development of novel strategies employing a range of in silico tools may help in the generation of Milk Protein Hydrolysates containing potent and bioavailable peptides, which in turn may be used to validate their health promoting effects in humans.
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Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel Milk Protein Hydrolysates.
Food chemistry, 2017Co-Authors: Alice B Nongonierma, Sara Paolella, Priti Mudgil, Sajid Maqsood, Richard J FitzgeraldAbstract:Abstract Nine novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (FLQY, FQLGASPY, ILDKEGIDY, ILELA, LLQLEAIR, LPVP, LQALHQGQIV, MPVQA and SPVVPF) were identified in camel Milk Proteins hydrolysed with trypsin. This was achieved using a sequential approach combining liquid chromatography tandem mass spectrometry (LC-MS/MS), qualitative/quantitative structure activity relationship (QSAR) and confirmatory studies with synthetic peptides. The most potent camel Milk Protein-derived DPP-IV inhibitory peptides, LPVP and MPVQA, had DPP-IV half maximal inhibitory concentrations (IC50) of 87.0 ± 3.2 and 93.3 ± 8.0 µM, respectively. DPP-IV inhibitory peptide sequences identified within camel and bovine Milk Protein Hydrolysates generated under the same hydrolysis conditions differ. This was linked to differences in enzyme selectivity for peptide bond cleavage of camel and bovine Milk Proteins as well as dissimilarities in their amino acid sequences. Camel Milk Proteins contain novel DPP-IV inhibitory peptides which may play a role in the regulation of glycaemia in humans.
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Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel Milk Protein Hydrolysates generated with trypsin
Journal of Functional Foods, 2017Co-Authors: Alice B Nongonierma, Sara Paolella, Priti Mudgil, Sajid Maqsood, Richard J FitzgeraldAbstract:Abstract Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel Milk Proteins. Camel Milk was hydrolysed with trypsin using a design of experiments (DOE, temperature (40–60 °C), enzyme to substrate (E:S) ratio (0.50–2.00% (w/w)) and time (60–240 min)). Fifteen Hydrolysates (H1–H15) having DPP-IV half maximal inhibitory concentration (IC50) values between 0.52 ± 0.06 (H9) and 1.26 ± 0.13 (H1) mg mL−1 were produced. Camel and bovine Milk Proteins hydrolysed at 40 °C, 1.8% E:S and 218 min had DPP-IV IC50 values of 0.68 ± 0.08 and 0.85 ± 0.10 mg mL−1 (p
Alice B Nongonierma - One of the best experts on this subject based on the ideXlab platform.
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Variable Glycemic Responses to Intact and Hydrolyzed Milk Proteins in Overweight and Obese Adults Reveal the Need for Precision Nutrition.
The Journal of nutrition, 2019Co-Authors: Aoife M. Curran, Alice B Nongonierma, Richard J Fitzgerald, Solène Le Maux, Katy Horner, Victoria O’sullivan, Eoin G. Murphy, Phil M. Kelly, Lorraine BrennanAbstract:Background Dietary modifications can contribute to improved pancreatic β cell function and enhance glycemic control. Objectives The objectives of this study were as follows: 1) to investigate the potential of Milk Protein Hydrolysates to modulate postprandial glucose response; 2) to assess individual responses; and 3) to explore the inter- and intraindividual reproducibility of the response. Methods A 14-d randomized crossover study investigated interstitial glucose levels of participants in response to 12% w/v Milk Protein drinks (intact caseinate and casein hydrolysate A and B) consumed in random order with a 2-d washout between treatments. Milk Protein drinks were consumed immediately prior to study breakfast and evening meals. Twenty participants (11 men, 9 women) aged 50 ± 8 y with a body mass index (in kg/m2) of 30.2 ± 3.1 were recruited. Primary outcome was glucose levels assessed at 15-min intervals with the use of glucose monitors. Results Repeated-measures ANOVA revealed that for breakfast there was a significant difference across the 3 treatment groups (P = 0.037). The ability to reduce postprandial glucose was specific to casein hydrolysate B in comparison with intact caseinate (P = 0.039). However, despite this significant difference, further examination revealed that only 3 out of 18 individuals were classified as responders (P
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Enhancing bioactive peptide release and identification using targeted enzymatic hydrolysis of Milk Proteins
Analytical and Bioanalytical Chemistry, 2018Co-Authors: Alice B Nongonierma, Richard J FitzgeraldAbstract:Milk Proteins have been extensively studied for their ability to yield a range of bioactive peptides following enzymatic hydrolysis/digestion. However, many hurdles still exist regarding the widespread utilization of Milk Protein-derived bioactive peptides as health enhancing agents for humans. These mostly arise from the fact that most Milk Protein-derived bioactive peptides are not highly potent. In addition, they may be degraded during gastrointestinal digestion and/or have a low intestinal permeability. The targeted release of bioactive peptides during the enzymatic hydrolysis of Milk Proteins may allow the generation of particularly potent bioactive Hydrolysates and peptides. Therefore, the development of Milk Protein Hydrolysates capable of improving human health requires, in the first instance, optimized targeted release of specific bioactive peptides. The targeted hydrolysis of Milk Proteins has been aided by a range of in silico tools. These include peptide cutters and predictive modeling linking bioactivity to peptide structure [i.e., molecular docking, quantitative structure activity relationship (QSAR)], or hydrolysis parameters [design of experiments (DOE)]. Different targeted enzymatic release strategies employed during the generation of Milk Protein Hydrolysates are reviewed herein and their limitations are outlined. In addition, specific examples are provided to demonstrate how in silico tools may help in the identification and discovery of potent Milk Protein-derived peptides. It is anticipated that the development of novel strategies employing a range of in silico tools may help in the generation of Milk Protein Hydrolysates containing potent and bioavailable peptides, which in turn may be used to validate their health promoting effects in humans. Graphical abstractThe targeted enzymatic hydrolysis of Milk Proteins may allow the generation of highly potent and bioavailable bioactive peptides.
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Enhancing bioactive peptide release and identification using targeted enzymatic hydrolysis of Milk Proteins
Analytical and bioanalytical chemistry, 2017Co-Authors: Alice B Nongonierma, Richard J FitzgeraldAbstract:Milk Proteins have been extensively studied for their ability to yield a range of bioactive peptides following enzymatic hydrolysis/digestion. However, many hurdles still exist regarding the widespread utilization of Milk Protein-derived bioactive peptides as health enhancing agents for humans. These mostly arise from the fact that most Milk Protein-derived bioactive peptides are not highly potent. In addition, they may be degraded during gastrointestinal digestion and/or have a low intestinal permeability. The targeted release of bioactive peptides during the enzymatic hydrolysis of Milk Proteins may allow the generation of particularly potent bioactive Hydrolysates and peptides. Therefore, the development of Milk Protein Hydrolysates capable of improving human health requires, in the first instance, optimized targeted release of specific bioactive peptides. The targeted hydrolysis of Milk Proteins has been aided by a range of in silico tools. These include peptide cutters and predictive modeling linking bioactivity to peptide structure [i.e., molecular docking, quantitative structure activity relationship (QSAR)], or hydrolysis parameters [design of experiments (DOE)]. Different targeted enzymatic release strategies employed during the generation of Milk Protein Hydrolysates are reviewed herein and their limitations are outlined. In addition, specific examples are provided to demonstrate how in silico tools may help in the identification and discovery of potent Milk Protein-derived peptides. It is anticipated that the development of novel strategies employing a range of in silico tools may help in the generation of Milk Protein Hydrolysates containing potent and bioavailable peptides, which in turn may be used to validate their health promoting effects in humans.
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Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel Milk Protein Hydrolysates.
Food chemistry, 2017Co-Authors: Alice B Nongonierma, Sara Paolella, Priti Mudgil, Sajid Maqsood, Richard J FitzgeraldAbstract:Abstract Nine novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (FLQY, FQLGASPY, ILDKEGIDY, ILELA, LLQLEAIR, LPVP, LQALHQGQIV, MPVQA and SPVVPF) were identified in camel Milk Proteins hydrolysed with trypsin. This was achieved using a sequential approach combining liquid chromatography tandem mass spectrometry (LC-MS/MS), qualitative/quantitative structure activity relationship (QSAR) and confirmatory studies with synthetic peptides. The most potent camel Milk Protein-derived DPP-IV inhibitory peptides, LPVP and MPVQA, had DPP-IV half maximal inhibitory concentrations (IC50) of 87.0 ± 3.2 and 93.3 ± 8.0 µM, respectively. DPP-IV inhibitory peptide sequences identified within camel and bovine Milk Protein Hydrolysates generated under the same hydrolysis conditions differ. This was linked to differences in enzyme selectivity for peptide bond cleavage of camel and bovine Milk Proteins as well as dissimilarities in their amino acid sequences. Camel Milk Proteins contain novel DPP-IV inhibitory peptides which may play a role in the regulation of glycaemia in humans.
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Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel Milk Protein Hydrolysates generated with trypsin
Journal of Functional Foods, 2017Co-Authors: Alice B Nongonierma, Sara Paolella, Priti Mudgil, Sajid Maqsood, Richard J FitzgeraldAbstract:Abstract Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel Milk Proteins. Camel Milk was hydrolysed with trypsin using a design of experiments (DOE, temperature (40–60 °C), enzyme to substrate (E:S) ratio (0.50–2.00% (w/w)) and time (60–240 min)). Fifteen Hydrolysates (H1–H15) having DPP-IV half maximal inhibitory concentration (IC50) values between 0.52 ± 0.06 (H9) and 1.26 ± 0.13 (H1) mg mL−1 were produced. Camel and bovine Milk Proteins hydrolysed at 40 °C, 1.8% E:S and 218 min had DPP-IV IC50 values of 0.68 ± 0.08 and 0.85 ± 0.10 mg mL−1 (p
Joris Kloek - One of the best experts on this subject based on the ideXlab platform.
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IPP-rich Milk Protein hydrolysate lowers blood pressure in subjects with stage 1 hypertension, a randomized controlled trial
Nutrition journal, 2010Co-Authors: Esther Boelsma, Joris KloekAbstract:Background Milk derived peptides have been identified as potential antihypertensive agents. The primary objective was to investigate the effectiveness of IPP-rich Milk Protein Hydrolysates (MPH) on reducing blood pressure (BP) as well as to investigate safety parameters and tolerability. The secondary objective was to confirm or falsify ACE inhibition as the mechanism underlying BP reductions by measuring plasma renin activity and angiotensin I and II.
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IPP-rich Milk Protein hydrolysate lowers blood pressure in subjects with stage 1 hypertension, a randomized controlled trial
Nutrition Journal, 2010Co-Authors: Esther Boelsma, Joris KloekAbstract:Background Milk derived peptides have been identified as potential antihypertensive agents. The primary objective was to investigate the effectiveness of IPP-rich Milk Protein Hydrolysates (MPH) on reducing blood pressure (BP) as well as to investigate safety parameters and tolerability. The secondary objective was to confirm or falsify ACE inhibition as the mechanism underlying BP reductions by measuring plasma renin activity and angiotensin I and II. Methods We conducted a randomized, placebo-controlled, double blind, crossover study including 70 Caucasian subjects with prehypertension or stage 1 hypertension. Study treatments consisted of daily consumption of two capsules MPH1 (each containing 7.5 mg Isoleucine-Proline-Proline; IPP), MPH2 (each containing 6.6 mg Methionine-Alanine-Proline, 2.3 mg Leucine-Proline-Proline, 1.8 mg IPP), or placebo (containing cellulose) for 4 weeks. Results In subjects with stage 1 hypertension, MPH1 lowered systolic BP by 3.8 mm Hg (P = 0.0080) and diastolic BP by 2.3 mm Hg (P = 0.0065) compared with placebo. In prehypertensive subjects, the differences in BP between MPH1 and placebo were not significant. MPH2 did not change BP significantly compared with placebo in stage I hypertensive or prehypertensive subjects. Intake of MPHs was well tolerated and safe. No treatment differences in hematology, clinical laboratory parameters or adverse effects were observed. No significant differences between MPHs and placebo were found in plasma renin activity, or angiotensin I and II. Conclusions MPH1, containing IPP and no minerals, exerts clinically relevant BP lowering effects in subjects with stage 1 hypertension. It may be included in lifestyle changes aiming to prevent or reduce high BP. Trial registration ClinicalTrials.gov NCT00471263
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IPP-rich Milk Protein hydrolysate lowers blood pressure in subjects with stage 1 hypertension, a randomized controlled trial
Nutrition Journal, 2010Co-Authors: Esther Boelsma, Joris KloekAbstract:Background Milk derived peptides have been identified as potential antihypertensive agents. The primary objective was to investigate the effectiveness of IPP-rich Milk Protein Hydrolysates (MPH) on reducing blood pressure (BP) as well as to investigate safety parameters and tolerability. The secondary objective was to confirm or falsify ACE inhibition as the mechanism underlying BP reductions by measuring plasma renin activity and angiotensin I and II. Methods We conducted a randomized, placebo-controlled, double blind, crossover study including 70 Caucasian subjects with prehypertension or stage 1 hypertension. Study treatments consisted of daily consumption of two capsules MPH1 (each containing 7.5 mg Isoleucine-Proline-Proline; IPP), MPH2 (each containing 6.6 mg Methionine-Alanine-Proline, 2.3 mg Leucine-Proline-Proline, 1.8 mg IPP), or placebo (containing cellulose) for 4 weeks. Results In subjects with stage 1 hypertension, MPH1 lowered systolic BP by 3.8 mm Hg (P = 0.0080) and diastolic BP by 2.3 mm Hg (P = 0.0065) compared with placebo. In prehypertensive subjects, the differences in BP between MPH1 and placebo were not significant. MPH2 did not change BP significantly compared with placebo in stage I hypertensive or prehypertensive subjects. Intake of MPHs was well tolerated and safe. No treatment differences in hematology, clinical laboratory parameters or adverse effects were observed. No significant differences between MPHs and placebo were found in plasma renin activity, or angiotensin I and II. Conclusions MPH1, containing IPP and no minerals, exerts clinically relevant BP lowering effects in subjects with stage 1 hypertension. It may be included in lifestyle changes aiming to prevent or reduce high BP. Trial registration ClinicalTrials.gov NCT00471263
Karin Schwarz - One of the best experts on this subject based on the ideXlab platform.
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surface accumulation of Milk Proteins and Milk Protein Hydrolysates at the air water interface on a time scale relevant for spray drying
Food Research International, 2012Co-Authors: Stephan Drusch, S. Hamann, A. Berger, Yvonne Serfert, Karin SchwarzAbstract:Abstract Accumulation of surface-active compounds may significantly alter the surface composition of food powders compared to the bulk composition of the product and therefore affects the functional properties. Through modification of a commercial contact angle meter surface accumulation of Milk Proteins and Protein Hydrolysates could be analysed via surface tension measurements in a time interval relevant for atomisation of emulsions during microencapsulation. The different caseins showed a slower surface occupation compared to industrially processed sodium caseinate and casein hydrolysate with β-casein being more surface-active than α- and κ-casein. In a similar manner, β-lactoglobulin showed a lower surface activity than whey Protein isolate and whey Protein hydrolysate. It is concluded that molecular weight profile plays an important role for the surface activity of Milk Proteins, but other factors like surface hydrophobicity, number of ionisable groups and state of aggregation also need to be considered.
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Surface accumulation of Milk Proteins and Milk Protein Hydrolysates at the air–water interface on a time-scale relevant for spray-drying
Food Research International, 2012Co-Authors: Stephan Drusch, S. Hamann, A. Berger, Yvonne Serfert, Karin SchwarzAbstract:Abstract Accumulation of surface-active compounds may significantly alter the surface composition of food powders compared to the bulk composition of the product and therefore affects the functional properties. Through modification of a commercial contact angle meter surface accumulation of Milk Proteins and Protein Hydrolysates could be analysed via surface tension measurements in a time interval relevant for atomisation of emulsions during microencapsulation. The different caseins showed a slower surface occupation compared to industrially processed sodium caseinate and casein hydrolysate with β-casein being more surface-active than α- and κ-casein. In a similar manner, β-lactoglobulin showed a lower surface activity than whey Protein isolate and whey Protein hydrolysate. It is concluded that molecular weight profile plays an important role for the surface activity of Milk Proteins, but other factors like surface hydrophobicity, number of ionisable groups and state of aggregation also need to be considered.
Sajid Maqsood - One of the best experts on this subject based on the ideXlab platform.
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Effect of camel Milk Protein Hydrolysates against hyperglycemia, hyperlipidemia, and associated oxidative stress in streptozotocin (STZ)-induced diabetic rats.
Journal of dairy science, 2020Co-Authors: Bhanu Priya Kilari, Priti Mudgil, Azimullah, Nidhi Bansal, Shreesh Ojha, Sajid MaqsoodAbstract:ABSTRACT This study investigated the effect of camel Milk Protein Hydrolysates (CMPH) at 100, 500 and 1,000 mg/kg of body weight (BW) for 8 wk on hyperglycemia, hyperlipidemia, and associated oxidative stress in streptozotocin-induced diabetic rats. Body weights and fasting blood glucose levels were observed after every week until 8 wk, and oral glucose tolerance test (OGTT) levels and biochemical parameters were evaluated after 8 wk in blood and serum samples. Antioxidant enzyme activity and lipid peroxidation in the liver were estimated, and histological examination of the liver and pancreatic tissues was also conducted. Results showed that CMPH at 500 mg/kg of BW [camel Milk Protein hydrolysate, mid-level dosage (CMPH-M)] exhibited potent hypoglycemic activity, as shown in the reduction in fasting blood glucose and OGTT levels. The hypolipidemic effect of CMPH was indicated by normalization of serum lipid levels. Significant improvement in activity of superoxide dismutase and catalase, and reduced glutathione levels were observed, along with the attenuation of malondialdehyde content in groups fed CMPH, especially CMPH-M, was observed. Decreased levels of liver function enzymes (aspartate aminotransferase and alanine aminotransferase) in the CMPH-M group was also noted. Histology of liver and pancreatic tissue displayed absence of lipid accumulation in hepatocytes and preservation of β-cells in the CMPH-M group compared with the diabetic control group. This is the first study to report anti-hyperglycemic and anti-hyperlipidemic effect of CMPH in an animal model system. This study indicates that CMPH can be suggested for its therapeutic benefits for hyperglycemia and hyperlipidemia, thus validating its use for better management of diabetes and associated comorbidities.
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identification and molecular docking study of novel cholesterol esterase inhibitory peptides from camel Milk Proteins
Journal of Dairy Science, 2019Co-Authors: Priti Mudgil, Bincy Baby, Ying-yuan Ngoh, Ranjit Vijayan, Sajid MaqsoodAbstract:ABSTRACT Novel bioactive peptides from camel Milk Protein Hydrolysates (CMPH) were identified and tested for inhibition of cholesterol esterase (CEase), and their possible binding mechanisms were elucidated by molecular docking. Papain-generated CMPH showed the highest degree of hydrolysis. All CMPH produced upon enzymatic degradation demonstrated a dramatic enhancement of CEase inhibition compared with intact camel Milk Proteins, with papain-generated hydrolysate P9 displaying the highest inhibition. Peptide identification and their modeling through PepSite 2 revealed that among 20 potential bioactive peptides in alcalase-generated hydrolysate A9, only 3 peptides, with sequences KFQWGY, SQDWSFY, and YWYPPQ, showed the highest binding toward CEase catalytic sites. Among 43 peptides in 9-h papain-generated hydrolysate P9, 4 peptides were found to be potent CEase inhibitors. Molecular docking revealed that WPMLQPKVM, CLSPLQMR, MYQQWKFL, and CLSPLQFR from P9 Hydrolysates were able to bind to the active site of CEase with good docking scores and molecular mechanics–generalized born surface area binding energies. Overall, this is the first study reporting CEase inhibitory potential of peptides generated from Milk Proteins.
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Molecular binding mechanism and identification of novel anti-hypertensive and anti-inflammatory bioactive peptides from camel Milk Protein Hydrolysates
LWT, 2019Co-Authors: Priti Mudgil, Bincy Baby, Ying-yuan Ngoh, Hina Kamal, Ranjit Vijayan, Chee-yuen Gan, Sajid MaqsoodAbstract:Abstract Camel Milk Protein Hydrolysates (CMPHs) were investigated for anti-hypertensive and anti-inflammatory activities using in-vitro assays. CMPHs with potent ACE inhibitory and anti-inflammatory activities were subjected to peptide identification and their possible binding mechanism to ACE were depicted via molecular docking. Papain generated CMPHs showed higher degradation of Proteins compared to bromelain and alcalase generated CMPHs as depicted in SDS-PAGE profile. Dramatic increase in ACE inhibitory and anti-inflammatory activity was demonstrated in CMPHs with highest activity for papain and alcalase generated Hydrolysates, respectively. Based on peptide ranking score, a total of 20, 3 and 43 peptides were potentially regarded as bioactive peptides in Hydrolysates A9, B9 and P9, respectively. Binding studies based on pepsite-2 modelling suggested that among 20 potential bioactive peptides in A9 hydrolysate, only 1 (AEWLHDWKL) showed high binding towards three catalytic sites of ACE. While, among 43 bioactive peptides of P9, 14 peptides were found to be potent binder to ACE catalytic sites. Further insight into molecular mechanism of binding revealed that 4 peptides were able to bind to active site of ACE with good docking scores and MM-GBSA binding energies. Overall, the current report remains among very few reports on identification and molecular docking of ACE inhibitory peptides from camel Milk.
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Characterization and identification of novel antidiabetic and anti-obesity peptides from camel Milk Protein Hydrolysates.
Food chemistry, 2018Co-Authors: Priti Mudgil, Hina Kamal, Gan Chee Yuen, Sajid MaqsoodAbstract:In-vitro inhibitory properties of peptides released from camel Milk Proteins against dipeptidyl peptidase-IV (DPP-IV), porcine pancreatic α-amylase (PPA), and porcine pancreatic lipase (PPL) were studied. Results revealed that upon hydrolysis by different enzymes, camel Milk Proteins displayed dramatic increase in inhibition of DPP-IV and PPL, but slight improvement in PPA inhibition was noticed. Peptide sequencing revealed a total of 20 and 3 peptides for A9 and B9 Hydrolysates respectively, obtained the score of 0.8 or more on peptide ranker and were categorized as potential DPP-IV inhibitory peptides. KDLWDDFKGL in A9 and MPSKPPLL in B9 were identified as most potent PPA inhibitory peptide. For PPL inhibition only 7 and 2 peptides qualified as PPL inhibitory peptides from Hydrolysates A9 and B9, respectively. The present study report for the first time PPA and PPL inhibitory and only second for DPP-IV inhibitory potential of Protein Hydrolysates from camel Milk.
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camel Milk Protein Hydrolysates with improved technofunctional properties and enhanced antioxidant potential in in vitro and in food model systems
Journal of Dairy Science, 2018Co-Authors: Kholoud Awad Alshamsi, Priti Mudgil, Hassan Mohamed Hassan, Sajid MaqsoodAbstract:Camel Milk Protein Hydrolysates (CMPH) were generated using proteolytic enzymes, such as alcalase, bromelain, and papain, to explore the effect on the technofunctional properties and antioxidant potential under in vitro and in real food model systems. Characterization of the CMPH via degree of hydrolysis, sodium dodecyl sulfate-PAGE, and HPLC revealed that different Proteins in camel Milk underwent degradation at different degrees after enzymatic hydrolysis using 3 different enzymes for 2, 4, and 6 h, with papain displaying the highest degradation. Technofunctional properties, such as emulsifying activity index, surface hydrophobicity, and Protein solubility, were higher in CMPH than unhydrolyzed camel Milk Proteins. However, the water and fat absorption capacity were lower in CMPH compared with unhydrolyzed camel Milk Proteins. Antioxidant properties as assessed by 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) and 2,2-diphenyl-1-picrylhydrazyl radical scavenging activities and metal-chelating activity were enhanced after hydrolysis, in contrast to ferric-reducing antioxidant power which showed a decrease after hydrolysis. The CMPH were also tested in real food model systems for their potential to inhibit lipid peroxidation in fish mince and grape seed oil-in-water emulsion, and we found that papain-produced hydrolysate displayed higher inhibition than alcalase- and bromelain-produced Hydrolysates. Therefore, the CMPH demonstrated effective antioxidant potential in vitro as well as in real food systems and showed enhanced functional properties, which guarantees their potential applications in functional foods. The present study is one of few reports available on CMPH being explored in vitro as well as in real food model systems.