MyMedR

Displaying publications 1 - 20 of 33 in total

Abstract:

Sort:

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*; Whey Proteins
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*; Whey Proteins
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
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
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; Whey Proteins
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
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
Fulltext Camel whey protein hydrolysates induced G2/M cellcycle arrest in human colorectal carcinoma

Murali C, Mudgil P, Gan CY, Tarazi H, El-Awady R, Abdalla Y, et al.

Sci Rep, 2021 03 29;11(1):7062.
PMID: 33782460 DOI: 10.1038/s41598-021-86391-z

Camel milk has been gaining immmense importance due to high nutritious value and medicinal properties. Peptides from milk proteins is gaining popularity in various therapeutics including human cancer. The study was aimed to investigate the anti-cancerous and anti-inflammatory properties of camel whey protein hydrolysates (CWPHs). CWPHs were generated at three temperatures (30 ℃, 37 ℃, and 45 ℃), two hydrolysis timepoints (120 and 360 min) and with three different enzyme concentrations (0.5, 1 and 2 %). CWPHs demonstrated an increase in anti-inflammatory effect between 732.50 (P-6.1) and 3779.16 (P-2.1) µg Dicolfenac Sodium Equivalent (DSE)/mg protein. CWPHs (P-4.3 & 5.2) inhibited growth of human colon carcinoma cells (HCT116) with an IC50 value of 231 and 221 μg/ml, respectively. P-4.3 induced G2/M cell cycle arrest and modulated the expression of Cdk1, p-Cdk1, Cyclin B1, p-histone H3, p21 and p53. Docking of two peptides (AHLEQVLLR and ALPNIDPPTVER) from CWPHs (P-4.3) identified Polo like kinase 1 as a potential target, which strongly supports our in vitro data and provides an encouraging insight into developing a novel peptide-based anticancer formulation. These results suggest that the active component, CWPHs (P-4.3), can be further studied and modeled to form a small molecule anti-cancerous therapy.

Matched MeSH terms: Whey Proteins/pharmacology*
Fulltext Exercise and pre-habilitation with high whey-protein-based meal replacement therapy promote weight loss and preserve muscle mass before bariatric surgery

Ho C, Samwil SNM, Kahairudin Z, Jamhuri N, Abd Aziz A

Asian J Surg, 2023 Sep;46(9):3716-3721.
PMID: 36931924 DOI: 10.1016/j.asjsur.2023.03.026

BACKGROUND: Bariatric surgery is considered as an effective therapy for those with morbid obesity. Preoperative weight loss with a very low-calorie diet is commonly used to ease the bariatric surgery. Pre-habilitation increases functional and physiological capacity. The study demonstrated the changes of body composition and functional status following short term pre-habilitation before bariatric surgery.
METHOD: This prospective study targeted those admitted for bariatric surgery. Participants underwent the biweekly pre-habilitation program included an individualized high whey-based protein very low-calorie (VLCHP) enteral regime (600-900 kcal/day) and moderate intensive exercise before bariatric surgery. Body composition and waist circumference were assessed after fortnight. Participants were segregated into morbid obese (MOG) (BMI <49 kg/m2) and super morbid obese group (SMOG) (BMI ≥50 kg/m2) for analysis.
RESULT: Majority of participants were female (71%) with median age 36.0 years old (MOG) and 34.3 years old (SMOG) respectively. SMOG achieved significant greater loss in weight (-7.4 kg vs -4.0 kg), fat percentage (-4.4% vs -1.7%) and fat mass (-9.9 kg vs -3.8 kg); but MOG had a significant increment in muscle mass (3.2 kg vs 2.8 kg) as compared to SOG (p

Matched MeSH terms: Whey/metabolism
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*
Fulltext Effects of different types and doses of whey protein on the physiological and intestinal flora in D-galactose induced aging mice

Ma Z, Zhang F, Ma H, Chen X, Yang J, Yang Y, et al.

PLoS One, 2021;16(4):e0248329.
PMID: 33857162 DOI: 10.1371/journal.pone.0248329

The elderly usually suffer from many diseases. Improving the quality of life of the elderly is an urgent social issue. In this present study, D-galactose treated aging mice models were used to reveal the effects of different animal sources and different doses of whey protein (WP) on the immune indexes organs and intestinal flora. A total of 9 groups were set up, including normal control (NC), negative control (NS), positive control (Vc), low-, medium- and high-doses of cow WP intervention groups (CL, CM and CH for short, correspondingly) and low-, medium- and high-doses of goat WP intervention groups (GL, GM and GH for short, correspondingly). The body weight gain, thymus/body weight ratio, superoxide dismutase (SOD) activity, malondialdehyde (MDA) content, spleen immunoglobulins G (IgG), spleen interleukin-2 (IL-2) and spleen interleukin-2 (IL-6) were measured. Then, the intestinal contents were collected, and 16s genes of intestinal bacteria were sequenced to reveal the changes in bacterial flora structure. WP intervention significantly increased the weight gain, thymus/body ratio and SOD activity, but decrease the content of MDA. WP intervention increased some immune indicators. All the WP treated aging mice showed similar values of physiological indexes to that of the Vc group, even better. The relative abundance of Lactobacillus and Stenotrophomonas was increased and decreased, respectively, by both cow and goat WP. Lactobacillus may be involved in regulating the functional repair of organisms. In contrast, Stenotrophomonas might play a negative role in the immune and antioxidant capacity of the body. Combining physiological indicators and intestinal flora structure, low-concentration WP for cow and goat might be optimal for aging models.

Matched MeSH terms: Whey Proteins/metabolism; Whey Proteins/pharmacology*
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
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
Characterisation of β-carotene partitioning in protein emulsions: Effects of pre-treatments, solid fat content and emulsifier type

Wan Mohamad WAF, McNaughton D, Augustin MA, Buckow R

Food Chem, 2018 Aug 15;257:361-367.
PMID: 29622223 DOI: 10.1016/j.foodchem.2018.03.027

Understanding the bioactive partitioning between the phases of an emulsion system underpins strategies for improving the efficiency of bioactive protection against degradation. We analysed partitioning of β-carotene in emulsions with various formulations in-situ using confocal Raman microscopy (CRM). The partitioning of β-carotene into the aqueous phase of emulsions increased when whey protein isolate (WPI) was heat or high pressure-treated prior to emulsion formation. However, increasing the concentration of high pressure-treated WPI reduced the β-carotene partitioning into the aqueous phase. Increasing the solid fat content in the carrier oil favoured the migration of β-carotene into the aqueous phase. The use of WPI as the emulsifier resulted in a greater partitioning of β-carotene into the aqueous phase compared to when Tween 40 was the emulsifier. This study demonstrates that partitioning of β-carotene between the aqueous and oil phase is dependent on the characteristics of the oil phase, emulsifier type and processing.

Matched MeSH terms: Whey Proteins/chemistry*
Fulltext Effectiveness of whey protein supplements on the serum levels of amino acid, creatinine kinase and myoglobin of athletes: a systematic review and meta-analysis

Lam FC, Khan TM, Faidah H, Haseeb A, Khan AH

Syst Rev, 2019 05 31;8(1):130.
PMID: 31151484 DOI: 10.1186/s13643-019-1039-z

BACKGROUND: Consuming whey protein supplements, along with physiotherapy and psychotherapy, have been recognised in sports performance. Whey protein supplements (WPS) is one of the commonly used supplements as ergogenic aids for athletes to enhance their muscle performance and recovery during sport-related injuries. The purpose of this systematic review is to investigate the effectiveness of WPS over the blood biochemistry mainly amino acids, creatinine kinase and myoglobin which influence performance and recovery among athletes.
METHOD: A comprehensive literature search was conducted to identify randomised control trials (RCTs) and non-RCTs that investigated the effectiveness of WPS on amino acids, creatinine kinase and myoglobin among athletes. Risk of Bias in Non-Randomised Studies of Interventions tool (ROBINS-I) and Cochrane Risk of Bias Assessment tool were used to rule out the quality of studies. Meta-analysis was performed using a random effect model with STATA version 14.2. The weighted mean difference was used to estimate the effectiveness of WPS against other supplements.
RESULTS: A total of 333,257 research articles were identified; of these, 15 records were included to proceed with the analysis. Meta-analysis has shown that WPS has significantly overall increased the level of essential amino acids level by 624.03 nmol/L (CI = 169.27, 1078.8; I2 = 100%; p = 0.00) and branched-chain amino acids level by 458.57 nmol/L (CI = 179.96, 737.18; I2 = 100%; p = 0.00) compared to the control group (without WPS). Moreover, was observed to decrease myoglobin level by 11.74 ng/ml (CI = - 30.24, 6.76; I2 = 79.6%; p = 0.007) and creatine kinase level by 47.05 U/L (CI = - 129.47, 35.37; I2 = 98.4%; p = 0.000) compared to the control group.
CONCLUSION: The findings revealed that the clinical evidence supports the effectiveness of WPS as a positive ergogenic aid on athletes' amino acids, creatinine kinase and myoglobin.

Matched MeSH terms: Whey Proteins/pharmacology*
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*
A comprehensive review of milk fouling on heated surfaces

Sadeghinezhad E, Kazi SN, Dahari M, Safaei MR, Sadri R, Badarudin A

Crit Rev Food Sci Nutr, 2015;55(12):1724-43.
PMID: 24731003 DOI: 10.1080/10408398.2012.752343

Heat exchanger performance degrades rapidly during operation due to formation of deposits on heat transfer surfaces which ultimately reduces service life of the equipment. Due to scaling, product deteriorates which causes lack of proper heating. Chemistry of milk scaling is qualitatively understood and the mathematical models for fouling at low temperatures have been produced but the behavior of systems at ultra high temperature processing has to be studied further to understand in depth. In diversified field, the effect of whey protein fouling along with pressure drop in heat exchangers were conducted by many researchers. Adding additives, treatment of heat exchanger surfaces and changing of heat exchanger configurations are notable areas of investigation in milk fouling. The present review highlighted information about previous work on fouling, influencing parameters of fouling and its mitigation approach and ends up with recommendations for retardation of milk fouling and necessary measures to perform the task.

Matched MeSH terms: Whey Proteins/chemistry
Fulltext Benefits and side effects of protein supplementation and exercise in sarcopenic obesity: A scoping review

Cheah KJ, Cheah LJ

Nutr J, 2023 Oct 23;22(1):52.
PMID: 37872544 DOI: 10.1186/s12937-023-00880-7

BACKGROUND: Protein supplements have been widely used among those who are struggling with sarcopenic obesity among older adults. However, despite their popularity, there is still a lack of concrete evidence on both the potential benefits and side effects of protein supplementation and exercise on sarcopenic obesity (SO).
OBJECTIVE: Thus, we aimed to determine the impacts of protein supplementation and exercise in older adults with sarcopenic obesity.
METHOD: A systematic database search was conducted for randomised controlled trials, quasi experimental study and pre-post study design addressing the effects of protein supplementation in improving sarcopenic obesity among older adults. This scoping review was conducted based on PRISMA-Scr guidelines across PubMed, Embase, Web of Science and Cochrane Library databases. To assess record eligibility, two independent reviewers performed a rigorous systematic screening process.
RESULTS: Of the 1,811 citations identified, 7 papers met the inclusion criteria. Six studies were randomised controlled trials and one study was a pre-post test study design. The majority of studies discussed the use of both protein supplements and exercise training. The included studies prescribed protein intake ranging from 1.0 to 1.8 g/kg/BW/day for the intervention group, while the duration of exercise performed ranged from 2 to 3 times per week, with each session lasting for 1 hour. Whey protein supplementation has been shown to be effective in improving sarcopenic conditions and weight status in SO individuals. The combination of exercise training especially resistance training and the used of protein supplement provided additional benefits in terms of lean muscle mass as well as biomarkers. The study also revealed a lack of consistency in exercise design among interventions for sarcopenic obesity.
CONCLUSION: Overall, it appears to be a promising option for SO individuals to improve their sarcopenic condition and weight status through the combination of resistance exercise and whey protein supplementation. However, it also highlights the need for caution when it comes to high amounts of protein intake prescription. Future research is warranted to investigate the optimal exercise design for this population, given the limited research conducted in this specific area.

Matched MeSH terms: Whey Proteins/therapeutic use
Fulltext Economic value of atopic dermatitis prevention via infant formula use in high-risk Malaysian infants

Bhanegaonkar AJ, Horodniceanu EG, Abdul Latiff AH, Woodhull S, Khoo PC, Detzel P, et al.

Asia Pac Allergy, 2015 Apr;5(2):84-97.
PMID: 25938073 DOI: 10.5415/apallergy.2015.5.2.84

BACKGROUND: Breastfeeding is best for infants and the World Health Organization recommends exclusive breastfeeding for at least the first 6 months of life. For those who are unable to be breastfed, previous studies demonstrate that feeding high-risk infants with hydrolyzed formulas instead of cow's milk formula (CMF) may decrease the risk of atopic dermatitis (AD).
OBJECTIVE: To estimate the economic impact of feeding high-risk, not exclusively breastfed, urban Malaysian infants with partiallyhydrolyzed whey-based formula (PHF-W) instead of CMF for the first 17 weeks of life as an AD risk reduction strategy.
METHODS: A cohort Markov model simulated the AD incidence and burden from birth to age 6 years in the target population fed with PHF-W vs. CMF. The model integrated published clinical and epidemiologic data, local cost data, and expert opinion. Modeled outcomes included AD-risk reduction, time spent post AD diagnosis, days without AD flare, quality-adjusted life years (QALYs), and costs (direct and indirect). Outcomes were discounted at 3% per year. Costs are expressed in Malaysian Ringgit (MYR; MYR 1,000 = United States dollar [US $]316.50).
RESULTS: Feeding a high-risk infant PHF-W vs. CMF resulted in a 14% point reduction in AD risk (95% confidence interval [CI], 3%-23%), a 0.69-year (95% CI, 0.25-1.10) reduction in time spent post-AD diagnosis, additional 38 (95% CI, 2-94) days without AD flare, and an undiscounted gain of 0.041 (95% CI, 0.007-0.103) QALYs. The discounted AD-related 6-year cost estimates when feeding a high-risk infant with PHF-W were MYR 1,758 (US $556) (95% CI, MYR 917-3,033) and with CMF MYR 2,871 (US $909) (95% CI, MYR 1,697-4,278), resulting in a per-child net saving of MYR 1,113 (US $352) (95% CI, MYR 317-1,884) favoring PHF-W.
CONCLUSION: Using PHF-W instead of CMF in this population is expected to result in AD-related costs savings.

Matched MeSH terms: Whey; Whey Proteins
Impacts of supplementation with milk proteins on inflammation: a systematic review and meta-analysis

Mohammadi S, Ashtary-Larky D, Mehrbod M, Kouhi Sough N, Salehi Omran H, Dolatshahi S, et al.

Inflammopharmacology, 2025 Mar;33(3):1061-1083.
PMID: 39775243 DOI: 10.1007/s10787-024-01615-8

BACKGROUND: Impacts of milk proteins (MPs) on inflammation are uncertain. The current systematic review and dose-response meta-analysis of randomized controlled trials (RCTs) evaluated the effects of whey protein (WP), casein protein (CP), or MP supplementation on serum levels of cytokines and adipokines in adults.
METHODS: A comprehensive search of various online databases was conducted to find appropriate clinical trials published until September 2024. A random-effect statistical model was implemented.
RESULTS: The meta-analysis included 53 RCTs. It was indicated that MP supplements had no substantial effects on serum values of C-reactive protein (CRP), tumor necrosis factor-alpha (TNF-α), adiponectin, and leptin. However, there were statistically significant decreases in serum levels of interleukin-6 (IL-6) following supplementation with MP (weighted mean difference (WMD): - 0.25 pg/mL, 95% CI - 0.48, - 0.03; P = 0.026) in the intervention group compared with the control group.
CONCLUSION: This study revealed that MP supplementation may not have any considerable impacts on the levels of cytokines and adipokines.

Matched MeSH terms: Whey Proteins/administration & dosage

Filters

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links