Displaying publications 1 - 20 of 31 in total

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  1. Tunability of Pickering particle features of whey protein isolate via remodeling partial unfolding during ultrasonication-assisted complexation with chitosan/chitooligosaccharide
    Yu H, Zheng Y, Zhou C, Liu L, Wang L, Cao J, et al.
    Carbohydr Polym, 2024 Feb 01;325:121583.
    PMID: 38008470 DOI: 10.1016/j.carbpol.2023.121583
    The potential of ultrasonication-driven molecular self-assembly of whey protein isolate (WPI) with chitosan (CS)/chitooligosaccharide (COS) to stabilize Pickering emulsions was examined, based on CS/COS ligands-induced partial unfolding in remodeling the Pickering particles features. Multi-spectral analysis suggested obvious changes in conformational structures of WPI due to interaction with CS/COS, with significantly higher unfolding degrees of WPI induced by COS. Non-covalent interactions were identified as the major forces for WPI-CS/COS conjugates. Ultrasonication enhanced electrostatic interaction between CS's -NH3 groups and WPI's -COO- groups which improved emulsification activity and storability of WPI-COS stabilized Pickering emulsion. This was attributed to increased surface hydrophobicity and decreased particle size compared to WPI-CS associated with differential unfolding degrees induced by different saccharide ligands. CLSM and SEM consistently observed smaller emulsion droplets in WPI-COS complexes than WPI-CS/COS particles tightly adsorbed at the oil-water interface. The electrostatic self-assembly of WPI with CS/COS greatly enhanced the encapsulation efficiency of quercetin than those stabilized by WPI alone and ultrasound further improved encapsulation efficiency. This corresponded well with the quantitative affinity parameters between quercetin and WPI-CS/COS complexes. This investigation revealed the great potential of glycan ligands-induced conformational transitions of extrinsic physical disruption in tuning Pickering particle features.
    Matched MeSH terms: Whey Proteins/chemistry
  2. Toxicity study and blood pressure-lowering efficacy of whey protein concentrate hydrolysate in rat models, plus peptide characterization
    Hussein FA, Chay SY, Ghanisma SBM, Zarei M, Auwal SM, Hamid AA, et al.
    J Dairy Sci, 2020 Mar;103(3):2053-2064.
    PMID: 31882211 DOI: 10.3168/jds.2019-17462
    We evaluated the acute (single-dose) and subacute (repeated-dose) oral toxicity of alcalase-hydrolyzed whey protein concentrate. Our acute study revealed no death or treatment-related complications, and the median lethal dose of whey protein concentrate hydrolysate was >2,500 mg/kg. In the subacute study, when the hydrolysate was fed at 3 different concentrations (200, 400, and 800 mg/kg), no groups showed toxicity changes compared with controls. Then, whey protein concentrate hydrolysate was orally administered to spontaneously hypertensive rats. Results revealed significant reductions in blood pressure in a dose-dependent manner, and dosing at 400 mg/kg led to significant blood pressure reduction (-47.8 mm Hg) compared with controls (blood pressure maintained) and the findings of previous work (-21 mm Hg). Eight peptides-RHPEYAVSVLLR, GGAPPAGRL, GPPLPRL, ELKPTPEGDL, VLSELPEP, DAQSAPLRVY, RDMPIQAF, and LEQVLPRD-were sequentially identified and characterized. Of the peptides, VLSELPEP and LEQVLPRD showed the most prominent in vitro angiotensin-I converting enzyme inhibition with half-maximal inhibitory concentrations of 0.049 and 0.043 mM, respectively. These findings establish strong evidence for the in vitro and in vivo potential of whey protein concentrate hydrolysate to act as a safe, natural functional food ingredient that exerts antihypertensive activity.
    Matched MeSH terms: Whey Proteins/pharmacology*; Whey Proteins/toxicity; Whey Proteins/chemistry
  3. The binding mechanism of oat phenolic acid to whey protein and its inhibition mechanism against AGEs as revealed using spectroscopy, chromatography and molecular docking
    Dong L, Zhang Y, Li Y, Liu Y, Chen Q, Liu L, et al.
    Food Funct, 2023 Nov 13;14(22):10221-10231.
    PMID: 37916290 DOI: 10.1039/d3fo02474a
    Heat sterilization of dairy products can promote the formation of advanced glycation end products (AGEs), protein oxidation products (POPs) and α-dicarbonyl compounds, which have a significant influence on health due to the close association of these products with diabetes complications. In this study, eight oat phenolic acids were first analyzed for their inhibitory effect against AGEs formation. Due to their strong inhibitory effects and structural differences, caffeic acid (CA) and gallic acid (GA) were further selected to assess their anti-glycosylation mechanisms using spectroscopy, chromatography and molecular docking. CA/GA reduced the production of total AGEs and POPs in various bovine milk simulation models and protected whey proteins from structural modifications, oxidation, and cross-linking. Comparative analyses showed a structure-effect relationship between CA/GA and AGEs inhibition. Oat phenolic acids against AGEs and POPs might be related to the unique bonding of key amino acid residues in whey proteins, the inhibitory role of early fructosamine and the trapping of reactive α-dicarbonyl groups to form adducts. In conclusion, oat phenolic acids might present a promising dietary strategy to alleviate AGEs production and glycation of proteins in dairy products upon storage.
    Matched MeSH terms: Whey Proteins/analysis
  4. The Potential Source of B. licheniformis Contamination During Whey Protein Concentrate 80 Manufacture
    Md Zain SN, Bennett R, Flint S
    J Food Sci, 2017 Mar;82(3):751-756.
    PMID: 28135405 DOI: 10.1111/1750-3841.13633
    The objective of this study was to determine the possible source of predominant Bacillus licheniformis contamination in a whey protein concentrate (WPC) 80 manufacturing plant. Traditionally, microbial contaminants of WPC were believed to grow on the membrane surfaces of the ultrafiltration plant as this represents the largest surface area in the plant. Changes from hot to cold ultrafiltration have reduced the growth potential for bacteria on the membrane surfaces. Our recent studies of WPCs have shown the predominant microflora B. licheniformis would not grow in the membrane plant because of the low temperature (10 °C) and must be growing elsewhere. Contamination of dairy products is mostly due to bacteria being released from biofilm in the processing plant rather from the farm itself. Three different reconstituted WPC media at 1%, 5%, and 20% were used for biofilm growth and our results showed that B. licheniformis formed the best biofilm at 1% (low solids). Further investigations were done using 3 different media; tryptic soy broth, 1% reconstituted WPC80, and 1% reconstituted WPC80 enriched with lactose and minerals to examine biofilm growth of B. licheniformis on stainless steel. Thirty-three B. licheniformis isolates varied in their ability to form biofilm on stainless steel with stronger biofilm in the presence of minerals. The source of biofilms of thermo-resistant bacteria such as B. licheniformis is believed to be before the ultrafiltration zone represented by the 1% WPC with lactose and minerals where the whey protein concentration is about 0.6%.
    Matched MeSH terms: Whey Proteins*
  5. Stabilization of water in oil in water (W/O/W) emulsion using whey protein isolate-conjugated durian seed gum: enhancement of interfacial activity through conjugation process
    Tabatabaee Amid B, Mirhosseini H
    Colloids Surf B Biointerfaces, 2014 Jan 1;113:107-14.
    PMID: 24060935 DOI: 10.1016/j.colsurfb.2013.08.042
    The present work was conducted to investigate the effect of purification and conjugation processes on functional properties of durian seed gum (DSG) used for stabilization of water in oil in water (W/O/W) emulsion. Whey protein isolate (WPI) was conjugated to durian seed gum through the covalent linkage. In order to prepare WPI-DSG conjugate, covalent linkage of whey protein isolate to durian seed gum was obtained by Maillard reaction induced by heating at 60 °C and 80% (±1%) relative humidity. SDS-polyacrylamide gel electrophoresis was used to test the formation of the covalent linkage between whey protein isolate and durian seed gum after conjugation process. In this study, W/O/W stabilized by WPI-conjugated DSG A showed the highest interface activity and lowest creaming layer among all prepared emulsions. This indicated that the partial conjugation of WPI to DSG significantly improved its functional characteristics in W/O/W emulsion. The addition of WPI-conjugated DSG to W/O/W emulsion increased the viscosity more than non-conjugated durian seed gum (or control). This might be due to possible increment of the molecular weight after linking the protein fraction to the structure of durian seed gum through the conjugation process.
    Matched MeSH terms: Whey Proteins
  6. Phospholipid-Protein Structured Membrane for Microencapsulation of DHA Oil and Evaluation of Its In Vitro Digestibility: Inspired by Milk Fat Globule Membrane
    Chen Y, Ge H, Zheng Y, Zhang H, Li Y, Su X, et al.
    J Agric Food Chem, 2020 Jun 03;68(22):6190-6201.
    PMID: 32379465 DOI: 10.1021/acs.jafc.0c01250
    The present study aims to design a milk fat globule membrane (MFGM)-inspired structured membrane (phospholipid- and protein-rich) for microencapsulation of docosahexaenoic acid (DHA) oil. DHA-enriched oil emulsions were prepared using different ratios of sunflower phospholipid (SPL), proteins [whey protein concentrate (WPC), soy protein isolate (SPI), and sodium caseinate (SC)], and maltodextrin and spray-dried to obtain DHA microcapsules. The prepared DHA oil emulsions have nanosized particles. SPLs were found to affect the secondary structure of WPC, which resulted in increased exposure of the protein hydrophobic site and emulsion stability. SPL also reduced the surface tension and viscosity of the DHA oil emulsions. In vitro digestion of the spray-dried DHA microcapsules showed that they were able to effectively resist gastric proteolysis and protect their bioactivity en route to the intestine. The DHA microcapsules have a high lipid digestibility in the small intestine with a high DHA hydrolysis efficiency (74.3%), which is higher than that of commercial DHA microcapsules.
    Matched MeSH terms: Whey Proteins/metabolism; Whey Proteins/chemistry*
  7. Performance evaluation of whey flux in dead-end and cross-flow modes via convolutional neural networks
    Yogarathinam LT, Velswamy K, Gangasalam A, Ismail AF, Goh PS, Narayanan A, et al.
    J Environ Manage, 2022 Jan 01;301:113872.
    PMID: 34607142 DOI: 10.1016/j.jenvman.2021.113872
    Effluent originating from cheese production puts pressure onto environment due to its high organic load. Therefore, the main objective of this work was to compare the influence of different process variables (transmembrane pressure (TMP), Reynolds number and feed pH) on whey protein recovery from synthetic and industrial cheese whey using polyethersulfone (PES 30 kDa) membrane in dead-end and cross-flow modes. Analysis on the fouling mechanistic model indicates that cake layer formation is dominant as compared to other pore blocking phenomena evaluated. Among the input variables, pH of whey protein solution has the biggest influence towards membrane flux and protein rejection performances. At pH 4, electrostatic attraction experienced by whey protein molecules prompted a decline in flux. Cross-flow filtration system exhibited a whey rejection value of 0.97 with an average flux of 69.40 L/m2h and at an experimental condition of 250 kPa and 8 for TMP and pH, respectively. The dynamic behavior of whey effluent flux was modeled using machine learning (ML) tool convolutional neural networks (CNN) and recursive one-step prediction scheme was utilized. Linear and non-linear correlation indicated that CNN model (R2 - 0.99) correlated well with the dynamic flux experimental data. PES 30 kDa membrane displayed a total protein rejection coefficient of 0.96 with 55% of water recovery for the industrial cheese whey effluent. Overall, these filtration studies revealed that this dynamic whey flux data studies using the CNN modeling also has a wider scope as it can be applied in sensor tuning to monitor flux online by means of enhancing whey recovery efficiency.
    Matched MeSH terms: Whey Proteins
  8. New insights into the cholesterol esterase- and lipase-inhibiting potential of bioactive peptides from camel whey hydrolysates: Identification, characterization, and molecular interaction
    Baba WN, Mudgil P, Baby B, Vijayan R, Gan CY, Maqsood S
    J Dairy Sci, 2021 Jul;104(7):7393-7405.
    PMID: 33934858 DOI: 10.3168/jds.2020-19868
    Novel antihypercholesterolemic bioactive peptides (BAP) from peptic camel whey protein hydrolysates (CWPH) were generated at different time, temperature, and enzyme concentration (%). Hydrolysates showed higher pancreatic lipase- (PL; except 3 CWPH) and cholesterol esterase (CE)-inhibiting potential, as depicted by lower half-maximal inhibitory concentration values (IC50 values) compared with nonhydrolyzed camel whey proteins (CWP). Peptide sequencing and in silico data depicted that most BAP from CWPH could bind active site of PL, whereas as only 3 peptides could bind the active site of CE. Based on higher number of reactive residues in the BAP and greater number of substrate binding sites, FCCLGPVPP was identified as a potential CE-inhibitory peptide, and PAGNFLPPVAAAPVM, MLPLMLPFTMGY, and LRFPL were identified as PL inhibitors. Molecular docking of selected peptides showed hydrophilic and hydrophobic interactions between peptides and target enzymes. Thus, peptides derived from CWPH warrant further investigation as potential candidates for adjunct therapy for hypercholesterolemia.
    Matched MeSH terms: Whey Proteins
  9. Molecular basis of the anti-diabetic properties of camel milk through profiling of its bioactive peptides on dipeptidyl peptidase IV (DPP-IV) and insulin receptor activity
    Ashraf A, Mudgil P, Palakkott A, Iratni R, Gan CY, Maqsood S, et al.
    J Dairy Sci, 2021 Jan;104(1):61-77.
    PMID: 33162074 DOI: 10.3168/jds.2020-18627
    The molecular basis of the anti-diabetic properties of camel milk reported in many studies and the exact active agent are still elusive. Recent studies have reported effects of camel whey proteins (CWP) and their hydrolysates (CWPH) on the activities of dipeptidyl peptidase IV (DPP-IV) and the human insulin receptor (hIR). In this study, CWPH were generated, screened for DPP-IV binding in silico and inhibitory activity in vitro, and processed for peptide identification. Furthermore, pharmacological action of intact CWP and their selected hydrolysates on hIR activity and signaling and on glucose uptake were investigated in cell lines. Results showed inhibition of DPP-IV by CWP and CWPH and their positive action on hIR activation and glucose uptake. Interestingly, the combination of CWP or CWPH with insulin revealed a positive allosteric modulation of hIR that was drastically reduced by the competitive hIR antagonist. Our data reveal for the first time the profiling and pharmacological actions of CWP and their derived peptides fractions on hIR and their pathways involved in glucose homeostasis. This sheds more light on the anti-diabetic properties of camel milk by providing the molecular basis for the potential use of camel milk in the management of diabetes.
    Matched MeSH terms: Whey Proteins/metabolism
  10. Fulltext Mixed biopolymer systems based on starch
    Abd Elgadir M, Akanda MJ, Ferdosh S, Mehrnoush A, Karim AA, Noda T, et al.
    Molecules, 2012 Jan 09;17(1):584-97.
    PMID: 22231495 DOI: 10.3390/molecules17010584
    A binary mixture of starch-starch or starch with other biopolymers such as protein and non-starch polysaccharides could provide a new approach in producing starch-based food products. In the context of food processing, a specific adjustment in the rheological properties plays an important role in regulating production processing and optimizing the applicability, stability, and sensory of the final food products. This review examines various biopolymer mixtures based on starch and the influence of their interaction on physicochemical and rheological properties of the starch-based foods. It is evident that the physicochemical and rheological characteristics of the biopolymers mixture are highly dependent on the type of starch and other biopolymers that make them up mixing ratios, mixing procedure and presence of other food ingredients in the mixture. Understanding these properties will lead to improve the formulation of starch-based foods and minimize the need to resort to chemically modified starch.
    Matched MeSH terms: Whey Proteins
  11. Mechanism of the structural interaction between whey and lentil proteins in the unique creation of a protein structure
    Alrosan M, Tan TC, Easa AM, Gammoh S, Alu'datt MH
    J Food Sci, 2021 Dec;86(12):5282-5294.
    PMID: 34796499 DOI: 10.1111/1750-3841.15974
    Poor solubility is a substantial factor that restricts the production of high value-added lentil proteins (LPs). In this study, whey protein isolates (WPIs), which have high solubility and are used in various food industries, were mixed with LPs at pH 12 to create LP-WPI protein complexes with improved water solubility properties using pH-recycling approach (maintained at pH 12.0 for 60 min and then readjusting to pH 7.0). LP-WPI protein complexes produced in this study have gained high surface charge, increased in the solubilization of protein complexes to ≈92%, as well as improved resistance against protein aggregation. The ratio of LPs to WPIs has a significant effect on the generation of unique tertiary and secondary protein structures based on the protein-protein interaction (PPI) technique via pH-recycling. The protein interaction between LPs and WPIs resulted in alteration on the surface morphology of the produced protein complexes. This study showed that electrostatic interaction, hydrophobic force, and hydrogen bond appear as major molecular forces in this PPI. The efficacy of the pH-recycling method used in this research indicates that this approach could be a robust approach to enhance the functional properties of food proteins. PRACTICAL APPLICATION: The pH-recycling technique is a proven technique for protein complexation in creating novel protein complexes with improved functional properties. Even though lentils are a rich source of plant-based protein, its utilization by food industries is restricted due to the poor water solubility of lentil proteins (LPs). However, by using complexing lentil proteins with whey protein isolates (WPIs), that is, LP-WPI protein complex, was developed. The water solubility of LP-WPI protein complex was significantly higher than LPs, up to approximately 92%. In addition, this could improve the utilization of lentil seeds in food application as an alternative for animal-based proteins.
    Matched MeSH terms: Whey Proteins
  12. Lycopene loaded whey protein isolate nanoparticles: An innovative endeavor for enhanced bioavailability of lycopene and anti-cancer activity
    Jain A, Sharma G, Ghoshal G, Kesharwani P, Singh B, Shivhare US, et al.
    Int J Pharm, 2018 Jul 30;546(1-2):97-105.
    PMID: 29715533 DOI: 10.1016/j.ijpharm.2018.04.061
    The work entails a novel strategy of formulating the lycopene loaded whey protein isolate nanoparticles (LYC-WPI-NPs) solely using the rational blend of biomacromolecule without using equipment-intensive techniques. The LYC-WPI-NPs were fabricated as a substantial drug delivery platform, with maximum entrapment, spatial and controlled release manners, exceptional plasma concentration, and perspective for discrepancy delivery of therapeutics. Prepared nano-formulations were measured in ultra-fine size (100-350 nm) with sphere-shaped. The percent lycopene entrapment of prepared LYC-WPI-NPs was estimated in the range to 50 and 65%. In vitro percent cumulative release study demonstrated deaden and extended release i.e. approximately 75% following 16th h. The in vitro percent cell survival (cytotoxicity study) of prepared nanoparticles was evaluated against MCF-7 breast cancer cells by MTT based colorimetric assay. Sub-cellular localization of lycopene when delivered by LYC-WPI-NPs was assessed by HPLC (high performance liquid chromatography). The WPI-NPs enhance the oral bioavailability of lycopene by controlling its release from nano-formulation and facilitating its absorption through lymphatic pathways. Prophylactic anticancer efficacy of LYC-WPI-NPs was evaluated thereafter on experimentally induced breast cancer animal model. Conclusively, it may quite reasonable that lycopene loaded protein nanoparticles are competent to improve the biopharmaceutical attributes of lycopene and demonstrated prophylactic anticancer activity, decrease tumor proliferation and increase the survival rate of treated animals, thus signifying their feasible usefulness in cancer therapeutic and intervention.
    Matched MeSH terms: Whey Proteins/administration & dosage*; Whey Proteins/pharmacokinetics; Whey Proteins/chemistry
  13. In situ quantification of β-carotene partitioning in oil-in-water emulsions by confocal Raman microscopy
    Wan Mohamad WAF, Buckow R, Augustin M, McNaughton D
    Food Chem, 2017 Oct 15;233:197-203.
    PMID: 28530566 DOI: 10.1016/j.foodchem.2017.04.086
    Confocal Raman microscopy (CRM) was able to quantify the β-carotene concentration in oil droplets and determine the partitioning characteristics of β-carotene within the emulsion system in situ. The results were validated by a conventional method involving solvent extraction of β-carotene separately from the total emulsion as well as the aqueous phase separated by centrifugation, and quantification by absorption spectrophotometry. CRM also enabled the localization of β-carotene in an emulsion. From the Raman image, the β-carotene partitioning between the aqueous and oil phases of palm olein-in-water emulsions stabilized by whey protein isolate (WPI) was observed. Increasing the concentration of β-carotene in an emulsion (from 0.1 to 0.3g/kg emulsion) with a fixed gross composition (10% palm olein:2% WPI) decreased the concentration of β-carotene in the oil droplet. CRM is a powerful tool for in situ analyses of components in heterogeneous systems such as emulsions.
    Matched MeSH terms: Whey Proteins
  14. Fulltext Implications of partial conjugation of whey protein isolate to durian seed gum through Maillard reactions: foaming properties, water holding capacity and interfacial activity
    Amid BT, Mirhosseini H, Poorazarang H, Mortazavi SA
    Molecules, 2013 Dec 06;18(12):15110-25.
    PMID: 24322494 DOI: 10.3390/molecules181215110
    This paper deals with the conjugation of durian seed gum (DSG) with whey protein isolate (WPI) through Maillard reactions. Subsequently, the functional properties of durian seed gum in the non-conjugated (control sample) and conjugated forms were compared with several commercial gums (i.e., Arabic gum, sodium alginate, kappa carrageenan, guar gum, and pectin). The current study revealed that the conjugation of durian seed gum with whey protein isolate significantly (p < 0.05) improved its foaming properties. In this study, the conjugated durian seed gum produced the most stable foam among all samples. On the other hand, the emulsion stabilized with the conjugated durian seed gum also showed more uniform particles with a larger specific surface area than the emulsion containing the non-conjugated durian seed gum. The conjugated durian seed gum showed significant different foaming properties, specific surface area, particle uniformity and water holding capacity (WHC) as compared to the target polysaccharide gums. The conjugated durian seed gum showed more similar functional properties to Arabic gum rather than other studied gums.
    Matched MeSH terms: Whey Proteins
  15. Fulltext Impact of stirring speed on β-lactoglobulin fibril formation
    Ng SK, Nyam KL, Nehdi IA, Chong GH, Lai OM, Tan CP
    Food Sci Biotechnol, 2016;25(Suppl 1):15-21.
    PMID: 30263481 DOI: 10.1007/s10068-016-0093-8
    β-Lactoglobulin (β-lg) can produce fibrils that have multi-functional properties. Impacts of different stirring speeds on characteristics of β-lg fibrils as a stable form in β-lg fibril solutions were investigated. Fibril concentration, fibril morphology, turbidity, particle size distribution, zeta potential, and rheological behavior of solutions were studied. Stirring enhanced fibril formation and stability of a fibril solution, in comparison with unstirred solutions. Increasing the stirring speed produced more turbidity and a greater distribution of particle sizes, higher viscosity values, but no differences in zeta potential values of β-lg fibril solutions. However, a high stirring speed is not feasible due to reduction of the fibril yield and changes in fibril morphology.
    Matched MeSH terms: Whey Proteins
  16. Identification and characterization of novel α-amylase and α-glucosidase inhibitory peptides from camel whey proteins
    Baba WN, Mudgil P, Kamal H, Kilari BP, Gan CY, Maqsood S
    J Dairy Sci, 2021 Feb;104(2):1364-1377.
    PMID: 33309363 DOI: 10.3168/jds.2020-19271
    This study explores the inhibitory properties of camel whey protein hydrolysates (CWPH) toward α-amylase (AAM) and α-glucosidase (AG). A general full factorial design (3 × 3) was applied to study the effect of temperature (30, 37, and 45°C), time (120, 240, and 360 min), and enzyme (pepsin) concentration (E%; 0.5, 1, and 2%). The results showed that maximum degree of hydrolysis was obtained when hydrolysis was carried out at higher temperature (45°C; P < 0.05), compared with lower temperatures of 30 and 37°C. Electrophoretic pattern displays degradation of all protein bands upon hydrolysis by pepsin at various hydrolysis conditions applied. All the 27 CWPH generated showed significant AAM and AG inhibitory potential as indicated by their lower IC50 values (mg/mL) compared with intact whey proteins. In total 196 peptides were identified from selected hydrolysates and 15 potential peptides (PepSite score > 0.8; http://pepsite2.russelllab.org/) were explored via in silico approach. Novel peptides PAGNFLMNGLMHR, PAVACCLPPLPCHM, MLPLMLPFTMGY, and PAGNFLPPVAAAPVM were identified as potential inhibitors for both AAM and AG due to their high number of binding sites and highest binding probability toward the target enzymes. CCGM and MFE, as well as FCCLGPVPP were identified as AG and AAM inhibitory peptides, respectively. This is the first study that reports novel AG and AAM inhibitory peptides from camel whey proteins. The future direction for this research involves synthesis of these potential AG and AAM inhibitory peptides in a pure form and investigate their antidiabetic properties in the in vitro, as well as in vivo models. Thus, CWPH can be considered for potential applications in glycaemic regulation.
    Matched MeSH terms: Whey Proteins/chemistry*
  17. Fulltext Fast-track- recovery surgery with a whey-protein-infused carbohydrate-loading drink pre-operatively and early oral feeding post-operatively among surgical gynaecological cancer patients: study protocol of an open-labelled, randomised controlled trial
    Ho CY, Ibrahim Z, Abu Zaid Z, Mat Daud Z', Md Yusop NB
    Trials, 2020 Jun 16;21(1):533.
    PMID: 32546217 DOI: 10.1186/s13063-020-04462-4
    INTRODUCTION: There has been growing evidence on the favourable outcomes of fast-track-recovery (FTR) surgery; to expedite recovery, minimise complications, and reduce the length of hospital stay for surgical patients. However, there is lack of evidence on the effectiveness of FTR in surgical gynaecological cancer (GC) patients. Most of the previous studies did not focus on feeding composition in the FTR surgery protocol. This study aims to determine the effectiveness of FTR feeding with a whey-protein-infused carbohydrate-loading drink pre-operatively and early oral feeding post-operatively on post-operative outcomes among surgical GC patients.

    METHODS/DESIGN: This open-labelled, randomised controlled trial (RCT) will randomly allocate patients into intervention and control groups. Ambulated Malaysian aged over 18 years and scheduled for elective surgery for (suspected) GC, will be included in this study. The intervention group will be given whey-protein-infused carbohydrate-loading drinks on the evening before their operation and 3 h before their operation as well as started on early oral feeding 4 h post-operatively. The control group will be fasted overnight pre-operation and only allowed plain water, and return to a normal diet is allowed when bowel sounds return post-operatively. The primary outcomes of study are length of post-operative hospital stay, length of clear-fluid tolerance, solid-food tolerance and bowel function. Additional outcome measures are changes in nutritional status, biochemical profile and functional status. Data will be analysed on an intention-to-treat basis.

    TRIAL REGISTRATION: ClinicalTrials.gov, ID: NCT03667755. Retrospectively registered on 12 September 2018; Protocol version: version 3 dated 27 September 2017.

    Matched MeSH terms: Whey Proteins/administration & dosage*; Whey Proteins/adverse effects
  18. Fulltext Efficacy and safety of pre-gastroscopy commercial carbohydrate-rich whey protein beverage vs. plain water: a randomised controlled trial
    Lua BC, Md Hashim MN, Wong MS, Lee YY, Zakaria AD, Zakaria Z, et al.
    Sci Rep, 2022 Oct 17;12(1):17355.
    PMID: 36253448 DOI: 10.1038/s41598-022-22363-1
    Clinical benefits and safety of carbohydrate loading pre-gastroscopy remain unclear. We aimed to determine the effects of a commercial carbohydrate-rich whey protein beverage versus plain water given pre-gastroscopy on gastric residual volume and well-being, and to determine adverse events. This was a single centre, single-blinded, parallel-group, sex-stratified randomized controlled trial. Participants were randomized either to carbohydrate-rich whey protein beverage group (Resource®, Nestle Health Science) or control group (250 ml plain water) given pre-gastroscopy. Gastric contents were aspirated into a suction reservoir bottle to determine the gastric residual volume (GRV). Visual analogue scale (VAS) of well-being (anxiety, hunger, thirst, tiredness, and weakness) was compared before and after the intervention. Adverse events were also evaluated post-intervention. Of 369 screened, 78 participants (36 males, mean age 49 ± 14.3 years) were randomized. Compared with the control group, carbohydrate beverage was associated with significantly higher GRV (p 
    Matched MeSH terms: Whey Proteins
  19. Fulltext Efficacy and Safety of Whey Protein Supplements on Vital Sign and Physical Performance Among Athletes: A Network Meta-Analysis
    Lam FC, Bukhsh A, Rehman H, Waqas MK, Shahid N, Khaliel AM, et al.
    Front Pharmacol, 2019;10:317.
    PMID: 31068804 DOI: 10.3389/fphar.2019.00317
    Introduction: Athletes train physically to reach beyond their potential maximum aerobic threshold. Whey protein supplements (WPS) are often used in conjunction with physiotherapy and psychotherapy to regain better vital sign and physical performances. This review aimed to explore the clinical evidence on the efficacy and safety of WPS in sports performance and recovery among athletes. Methodology: A comprehensive literature search was performed to identify relevant randomized control trials (RCTs) that investigated the efficacy and safety of WPS on the vital sign and physical performance among athletes. The Cochrane Risk of Bias (ROB) Assessment tools were used to assess the quality of the studies. Meta-analysis was conducted using the frequentist model with STATA version 14.2®. Results: A total of 333,257 research articles were identified out of which 20 RCTs were included for qualitative synthesis and network meta-analysis with 351 participants. Among the studies, 7 had low ROB and 3 RCTs had high ROB. Of these 20 trials, 16 trials were randomized clinical trials which compared whey protein supplements (WPS) with various comparators i.e., L-alanine, bovine colostrum, carbohydrate, casein, leucine, maltodextrin, rice, protein + caffeine were compared with placebo. Analysis from the pairwise meta-analysis revealed that for respiratory exchange ratio (RER) WPS was found to be significantly improving compared to maltodextrin (WMD = 0.012; 95%CI = 0.001, 0.023). Similarity to RPE (Rate Perceived Exertion), slight difference between WPS and the comparators, however, when the estimation was favorable to the comparators, there was moderate-high heterogeneity. For VO2max, high heterogeneity appeared when WPS compared to maltodextrin with the I2 = 97.8% (WMD = 4.064; 95% CI = -4.230, 12.359), meanwhile bovine colostrum (WMD = -2.658; 95%CI = -6.180, 0.865) only comparator that was better than WPS. According to the estimated effect of the supplements on physical performance outcome results, maximum power (8 studies, 185 athletes), highest ranked was bovine colostrum (SUCRA = 70.7%) and the lowest ranked was placebo (SUCRA = 17.9%), yet all insignificant. Then again, on average power (nine studies, 187 athletes), WPS was the highest ranked (SUCRA = 75.4 %) about -112.00 watt (-187.91, -36.08) and most of the estimations were significant. Body mass was reported in 10 studies (171 athletes), carbohydrate may be at the highest ranked (SUCRA = 66.9%) but it is insignificant. Thought the second highest ranked was WPS (SUCRA = 64.7%) and it is significant (WMD = -6.89 kg; CI = -8.24, -5.54). Conclusion: The findings of this review support the efficacy and safety of WPS as an ergogenic aid on athletes' sports performance and recovery. The overall quality of clinical evidence was found to be valid and reliable from the comprehensive search strategy and ROB assessment.
    Matched MeSH terms: Whey Proteins
  20. Effects of supplementation with milk protein on glycemic parameters: a GRADE-assessed systematic review and dose-response meta-analysis
    Mohammadi S, Asbaghi O, Dolatshahi S, Omran HS, Amirani N, Koozehkanani FJ, et al.
    Nutr J, 2023 Oct 06;22(1):49.
    PMID: 37798798 DOI: 10.1186/s12937-023-00878-1
    BACKGROUND: It is suggested that supplementation with milk protein (MP) has the potential to ameliorate the glycemic profile; however, the exact impact and certainty of the findings have yet to be evaluated. This systematic review and dose-response meta-analysis of randomized controlled trials (RCTs) assessed the impact of MP supplementation on the glycemic parameters in adults.

    METHODS: A systematic search was carried out among online databases to determine eligible RCTs published up to November 2022. A random-effects model was performed for the meta-analysis.

    RESULTS: A total of 36 RCTs with 1851 participants were included in the pooled analysis. It was displayed that supplementation with MP effectively reduced levels of fasting blood glucose (FBG) (weighted mean difference (WMD): -1.83 mg/dL, 95% CI: -3.28, -0.38; P = 0.013), fasting insulin (WMD: -1.06 uU/mL, 95% CI: -1.76, -0.36; P = 0.003), and homeostasis model assessment of insulin resistance (HOMA-IR) (WMD: -0.27, 95% CI: -0.40, -0.14; P  8 weeks) with high or moderate doses (≥ 60 or 30-60 g/d) of MP or whey protein (WP). Serum FBG levels were considerably reduced upon short-term administration of a low daily dose of WP (

    Matched MeSH terms: Whey Proteins
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