Journal articles: 'Casein/whey protein ratio'

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HERMANSEN, JOHN E., STEEN OSTERSEN, NIELS C. JUSTESEN, and OLE AAES. "Effects of dietary protein supply on caseins, whey proteins, proteolysis and renneting properties in milk from cows grazing clover or N fertilized grass." Journal of Dairy Research 66, no. 2 (May 1999): 193–205. http://dx.doi.org/10.1017/s0022029999003477.

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The objective of this work was to examine whether variation in the amino acid supply to cows could be a reason for the reduced casein content and poorer renneting properties of milk that often occur in late summer, or whether these effects are related to proteolysis in the raw milk. In a 2×2×2 factorial design, we investigated the effects of sward (clover v. rye-grass) and supplementary feed with a high or low level of rumen-soluble N or of rumen undegradable protein on milk protein composition during the grazing season. A total of 32 Danish Holstein cows were included in the experiment. Milk protein and casein contents and the ratios casein N[ratio ]total N and casein[ratio ]true protein were at a minimum in late summer, whereas the contents of urea, non-protein N and whey protein were higher during this period. These seasonal effects were unrelated to either the type of supplementary feed or the type of sward; neither were they clearly related to proteolysis, although casein[ratio ]true protein was related to the proteose peptone content. The results indicated that whey proteins other than α-lactalbumin or β-lactoglobulin accounted for the higher proportion or concentration of whey protein in late summer. Based on a principal component analysis including variables such as citric acid, lactose and non-protein N, we suggest that the cows' energy supply during this period may be a critical factor in determining the milk protein composition, although our results were not conclusive. There was an interaction between the supplement of rumen undegradable protein and type of sward. When clover was grazed, a high supplement increased the concentrations of protein and casein in milk and the κ-casein[ratio ]total casein ratio. When rye-grass was grazed, the opposite response was found, and overall milk protein yield was not affected. The very low N content of clover in early summer reduced milk protein and casein protein during this period.

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Hallén, Elin, Anne Lundén, Toomas Allmere, and Anders Andrén. "Casein retention in curd and loss of casein into whey at chymosin-induced coagulation of milk." Journal of Dairy Research 77, no. 1 (November 26, 2009): 71–76. http://dx.doi.org/10.1017/s0022029909990434.

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Impact of milk protein composition on casein (CN) retention in curd during the milk coagulation process was studied using a model cheese making system. Individual milk samples from 110 cows in mid lactation of the Swedish Red and Swedish Holstein breeds with known genotypes of β-casein, κ-casein and β-lactoglobulin were defatted, coagulated with chymosin, subjected to syneresis and subsequent pressing simulated by centrifugation. The results indicated that κ-casein concentration of milk plays an important role in the curd formation process and initial syneresis (whey after cutting), whereas an increased CN ratio was associated with less casein in whey after simulated pressing. Increased κ-casein concentration of milk also characterized the milk samples with no measurable loss of casein in whey, compared with milk samples with casein lost in whey, both after cutting and after simulated pressing. Concentrations of αs1-casein, β-casein, and total casein in milk were positively associated with fresh curd yield, which showed a strong correlation with amount of casein retained in curd. No effect of protein genotype on fresh curd yield or casein in whey was found. The β-lactoglobulin BB genotype was associated with increased casein retention in curd, most likely due to the association of this genotype with CN ratio.

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VAN BERESTEIJN, EMERENTIA C. H., ROGER A. PEETERS, JAAP KAPER, RON J. G. M. MEIJER, ARJAN J. P. M. ROBBEN, and DANIËL G. SCHMIDT. "Molecular Mass Distribution Immunological Properties Nutritive Value of Whey Protein Hydrolysates." Journal of Food Protection 57, no. 7 (July 1, 1994): 619–25. http://dx.doi.org/10.4315/0362-028x-57.7.619.

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Whey protein concentrate was hydrolyzed using the technical food-grade enzyme Corolase 7092 in order to abolish the allergenicity of whey proteins. The immunological properties of the hydrolysates were tested in vitro with a human-immunoglobulin E (human-IgE) enzyme-linked immunosorbent assay (ELISA) using sera obtained from children allergic to milk proteins and in vivo with a mouse-rat heterologous passive cutaneous anaphylactic test and an anaphylactic shock test in mice. The protein efficiency ratio, determined in young growing rats, was compared to that of casein. Ultrafiltration of the hydrolysates appeared to be necessary to obtain a hypo-allergenic product. The minimal molecular mass to elicit immunogenicity and allergenicity of whey protein hydrolysates appeared to be between 3,000 and 5,000 Da, so the molecular weight cut-off value of the filters required must be in this range. Although there was no evidence that extensively hydrolyzed whey protein is nutritionally inferior to casein, the slightly bitter taste might reduce food intake.

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Dijk, Francina J., Zandrie Hofman, Yvette C. Luiking, Matthew J. W. Furber, Justin D. Roberts, Ardy van Helvoort, and Miriam van Dijk. "Muscle Protein Synthesis with a Hybrid Dairy and Plant-Based Protein Blend (P4) Is Equal to Whey Protein in a Murine Ageing Model after Fasting." Nutrients 15, no. 11 (May 30, 2023): 2569. http://dx.doi.org/10.3390/nu15112569.

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P4, a specific combination of dairy proteins (whey and casein) and plant-based protein isolates (pea and soy), has been shown to provide a more balanced amino acid (AA) profile than its single constituent proteins; however, less is known about how this translates to muscle protein synthesis (MPS). The aim of this study was to investigate the effect of P4 compared to whey or casein against fasted control on MPS. C57BL/6J mice, aged 25 months, were fasted overnight, followed by oral gavage of either whey, P4, casein, or water as a fasted control. Thirty minutes after ingestion, puromycin (0.04 µmol∙g−1 bodyweight) was subcutaneously injected; 30-min thereafter, mice were sacrificed. MPS was measured by the SUnSET method, and signalling proteins were determined in the left-tibialis anterior (TA) muscle by the WES technique. AA composition was determined in plasma and right-TA muscle. Dried blood spots (DBS) were analysed for postprandial AA dynamics at 10, 20, 45, 60 min. MPS was 1.6-fold increased with whey (p = 0.006) and 1.5-fold with P4 compared to fasted (p = 0.008), while no change was seen with casein. This was confirmed by a significant increase of phosphorylated/total ratio of 4E-BP1 for both whey (p = 0.012) and P4 (p = 0.001). No changes were observed in p70S6K and mTOR phosphorylation/total ratio with whey or P4. Intramuscular leucine levels were lower for P4 (0.71 µmol∙g dry weight−1) compared to whey (0.97 µmol∙g dry weight−1) (p = 0.0007). Ten minutes postprandial, DBS showed significantly increased blood AA levels of BCAAs, histidine, lysine, threonine, arginine, and tyrosine for P4 versus fasted. In conclusion, a hybrid mix of dairy and plant-based proteins (P4) resulted in a MPS response that was similar to whey protein in aged mice after fasting. This suggests that other anabolic triggers beyond leucine or the well-balanced amino acid profile and bioavailability of the blend benefit stimulation of MPS.

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Kunz, Clemens, and Bo Lönnerdal. "Re-evaluation of the whey protein/casein ratio of human milk." Acta Paediatrica 81, no. 2 (February 1992): 107–12. http://dx.doi.org/10.1111/j.1651-2227.1992.tb12184.x.

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Jeswan Singh, Mandeep, Jayani Chandrapala, Punsandani Udabage, Ian McKinnon, and Mary Ann Augustin. "Heat-induced changes in the properties of modified skim milks with different casein to whey protein ratios." Journal of Dairy Research 82, no. 2 (December 12, 2014): 135–42. http://dx.doi.org/10.1017/s0022029914000739.

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The heat-induced changes in pH, Ca activity and viscosity after heating at 90 °C for 10 min of five modified skim milks were studied as a function of the initial pH of the milks at 25 °C. The milks had (i) different ratios of casein : whey protein (0·03, 1·74, 3·97, 5·27 and 7·25), (ii) the same total solids concentration (9% w/w) and (iii) prior to the adjustment of the pH, similar values of pH (6·67–6·74), concentration of serum calcium, and calcium activity, suggesting that the sera have similar mineral composition. The total protein concentrations of the milks differ (2·8–4·0%, w/w). The pH decrease in situ upon heating from 25–90 °C was similar for all the modified skim milks with the same starting pH, suggesting that the pH changes to milk on heating were primarily mediated by the initial mineral composition of the serum and were unaffected by the casein : whey protein ratio or the total protein content of the milk. The heat-induced changes in pH and calcium activity were largely reversible on cooling. The two milks with the lowest ratios of casein to whey protein gelled on heating to 90 °C for 10 min and cooling to 25 °C when the pH was adjusted to pH = 6·2 prior to heating. The viscosities of all other milks with casein to whey protein ratio of 3·97, 5·27 and 7·25 and/or pH ≥6·7 prior to heating did not change significantly. The effect of casein : whey protein ratio and the pH are the dominant factors in controlling the susceptibility to thickening of the milks on heating in this study.

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Schiffer, Simon, Bello Teslim Adekunle, Andreas Matyssek, Martin Hartinger, and Ulrich Kulozik. "Effect of Pre-Heating Prior to Low Temperature 0.1 µm-Microfiltration of Milk on Casein–Whey Protein Fractionation." Foods 10, no. 5 (May 14, 2021): 1090. http://dx.doi.org/10.3390/foods10051090.

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During skim milk microfiltration (nominal pore size of 0.1 µm) at 10 °C, the whey protein purity in the permeate is reduced by an enhanced serum casein permeation, primarily of β-casein. To decrease casein permeation, the possibility of a pre-heating step under pasteurization conditions before the filtration step was investigated, so as to shift the equilibrium from soluble serum casein monomers to impermeable micellar casein. Immediately after the pre-heating step, low temperature microfiltration at 10 °C was conducted before the casein monomers could diffuse into the serum. The hypothesis was that the dissociation of β-casein into the serum as a result of a decreasing temperature takes more time than the duration of the microfiltration process. It was found that pre-heating reduced the β-casein permeation during microfiltration without significantly affecting the flux and whey protein permeation, compared with a microfiltration at 10 °C without the pre-heating step. Furthermore, the addition of calcium (5 and 10 mM) not only reduced the casein permeation and thus increased the permeate purity, defined as a high whey protein-to-casein (g L−1/g L−1) ratio, but also decreased the filtration performance, possibly due to the structural alteration of the deposited casein micelle layer, rendering the deposit more compact and more retentive. Therefore, the possible combination of the addition of calcium and pre-heating prior to microfiltration was also investigated in order to evidence the potential increase of whey protein (WP) purity in the permeate in the case of Ca2+ addition prior to microfiltration. This study shows that pre-heating very close to low temperature microfiltration results in an increased purity of the whey protein fraction obtained in the permeate.

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Rioux, Laurie-Eve, and Sylvie L. Turgeon. "The Ratio of Casein to Whey Protein Impacts Yogurt Digestion In Vitro." Food Digestion 3, no. 1-3 (October 2, 2012): 25–35. http://dx.doi.org/10.1007/s13228-012-0023-z.

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Ronayne De Ferrer, Patricia A., and Maria Elena Sambucetti. "Casein to Whey Protein Ratio in Rat and Human Milks: Effects of Maternal Protein Intake." Journal of Dairy Science 76, no. 6 (June 1993): 1645–53. http://dx.doi.org/10.3168/jds.s0022-0302(93)77498-6.

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Beaulieu, M., Y. Pouliot, and M. Pouliot. "Thermal Aggregation of Whey Proteins in Model Solutions as Affected by Casein/Whey Protein Ratios." Journal of Food Science 64, no. 5 (September 1999): 776–80. http://dx.doi.org/10.1111/j.1365-2621.1999.tb15910.x.

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Gandra, Jefferson Rodrigues, Francisco Palma Rennó, José Esler de Freitas Júnior, Marcos Veiga dos Santos, Luís Felipe Prada e. Silva, and Ana Paula Chaves de Araújo. "Productive performance and milk protein fraction composition of dairy cows supplemented with sodium monensin." Revista Brasileira de Zootecnia 39, no. 8 (August 2010): 1810–17. http://dx.doi.org/10.1590/s1516-35982010000800025.

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The objective of this work was to evaluate the levels of sodium monensin on lactating cows and their effects on productive performance and milk protein fraction composition. It was used 12 Holstein cows, distributed in four balanced 3 × 3 Latin squares, and fed three diets: one control without monensin, and two diets with monensin at the levels of 24 or 48 mg/kg DM added to the concentrate. Milk production was daily measured throughout the entire experimental period. The samples used for analysis of milk composition were collected on two alternated days from the two daily milking. Non-protein nitrogen, total nitrogen and non-casein nitrogen contents were directly evaluated in the milk, and casein, whey protein and true protein contents were indirectly determined. The use of monensin in the rations reduced dry matter and nutrient intake, especially when diet with 48 mg/kg of dry matter was given. The ration with 24 mg/kg of DM increased milk production, with or without correction, and also fat and lactose yield, and it improved productive efficiency. The levels of monensin in the ratios did not influence contents of milk crude protein, non-protein nitrogen, non-casein nitrogen, true protein, casein, casein/true protein ratio, whey protein, and of all those fractions expressed as percentage of crude protein. The utilization of monensin in the ratio at the dose of 24 mg/kg of DM influences positively the productive performance of lactating cows, and it does not influence the composition of milk protein fractions.

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Jacobs, Wesley, Paul Johns, Phillip Haselberger, Joseph J. Thompson, Darryl Sullivan, and Steve Baugh. "Calculation of Whey Protein Fraction in Milk-Based Infant Formula: First Action 2012.07." Journal of AOAC INTERNATIONAL 96, no. 3 (May 1, 2013): 502–7. http://dx.doi.org/10.5740/jaoacint.13-033.

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Abstract A method for the calculation of whey protein fraction was developed for milk-based infant formula products, based upon an amino acid ratio calculated from amino acid profile data. Total amino acid data from 21 commercially available (five casein and 16 whey) commodities were used as the reference data from which the calculation model used in the validation study was built. This method has been evaluated for precision (repeatability, intermediate precision) and accuracy on nonfat dry milk and products manufactured with targeted whey levels of 32–63%, including National Institute of Standards and Technology infant formula Standard Reference Material (1849a). Estimates of repeatability were between 0.3 and 2.5% while those for intermediate precision were between 2.6 and 3.4%. Average recovery ranged from 97 to 100%. Additional reference material data are being gathered for better estimation of casein and whey amino acid reference values.

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Martinez Galan, Bryan S., Flavia Giolo De Carvalho, Simone C. S. Carvalho, Camila F. Cunha Brandao, Sara I. Morhy Terrazas, Gabriela Ferreira Abud, Monica S. S. Meirelles, et al. "Casein and Whey Protein in the Breast Milk Ratio: Could It Promote Protein Metabolism Enhancement in Physically Active Adults?" Nutrients 13, no. 7 (June 23, 2021): 2153. http://dx.doi.org/10.3390/nu13072153.

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Due to the utilization of milk proteins such as whey protein (WP) and casein as sports nutrition ergogenic aids, the present study investigated the effects of the association of WP and casein in a ratio of 80:20, a similar ratio of human breast milk, on blood branched-chain amino acid (BCAA) profiles, markers of protein metabolism and delayed onset muscle soreness (DOMS), after a single bout of resistance exercise. A double-blind, crossover and acute study was carried out with ten men (age 29 ± 8 years; BMI: 25.4 ± 2.9 kg/m2; 77 ± 12 kg; 1.74 ± 0.09 m); each one consumed the following supplements randomly, one per session: WP, CAS (casein), WP/CAS (80% WP/20% CAS), CAS/WP (80% CAS/20% WP) and PLA (placebo). They were also subjected to the following evaluations: the one repetition maximum (1RM) test; resistance training session; blood extraction during each session to determine the BCAA profile; two food records; 3-day evaluation of DOMS (24 h, 48 h and 72 h) and nitrogen balance in each treatment. The intervention resulted in similar nitrogen urinary, creatinine and urea plasma levels and showed a positive nitrogen balance in all the trials. Regarding the BCAAs, the peak occurred at 60 min post-ingestion and remained higher until 120 min for WP, WP/CAS and CAS/WP. The DOMS was significantly lower for WP, WP/CAS and CAS/WP compared to the CAS and PLA treatments. There were no advantages in the association of WP and CAS in the BCAAs profile when compared to WP itself, but it induced a lower DOMS compared to CAS and PLA (Clinical Trial registration number: clinicaltrials.gov, NCT04648384).

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COULON, JEAN-BAPTISTE, CATHERINE HURTAUD, BERNARD REMOND, and RAYMOND VERITE. "Factors contributing to variation in the proportion of casein in cows' milk true protein: a review of recent INRA experiments." Journal of Dairy Research 65, no. 3 (August 1998): 375–87. http://dx.doi.org/10.1017/s0022029998002866.

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The aim of this study was to identify and rank the various factors, in particular those involving feeding, that affect the proportion of caseins in milk true protein. Twenty-nine feeding trials involving 821 lactations were assessed, and lactoprotein genetic variants were known for 551 of these. The main factor affecting the casein: protein ratio was the genetic variant of β-lactoglobulin: once corrected for other factors, the milk of BB type animals had a ratio nearly 30 g/kg total protein higher than AA animals. κ-Casein variant B also had a positive effect (+12 g/kg in favour of BB relative to AA animals). Except in the last weeks of pregnancy and the first weeks of lactation, the casein[ratio ]protein ratio varied little during lactation. It was significantly reduced when milk cell count exceeded 200000 cells/ml, even in the absence of clinical mastitis. It also decreased slightly with parity. Among the various dietary factors studied (level and type of nitrogen and energy supplies, forage type and preservation method), none had any significant effect on the milk casein[ratio ]protein ratio, except in drastic dietary situations. That ratio increased very slightly in parallel with the animals' milk yield and milk protein content. In practice, measuring the milk protein content in animals free from clinical mastitis remains a very precise predictor of casein content, accounting for 93% of its variation.

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Fabre, Marina, Christophe Hausswirth, Eve Tiollier, Odeline Molle, Julien Louis, Alexandre Durguerian, Nathalie Neveux, and Xavier Bigard. "Effects of Postexercise Protein Intake on Muscle Mass and Strength During Resistance Training: Is There an Optimal Ratio Between Fast and Slow Proteins?" International Journal of Sport Nutrition and Exercise Metabolism 27, no. 5 (October 2017): 448–57. http://dx.doi.org/10.1123/ijsnem.2016-0333.

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While effects of the two classes of proteins found in milk (i.e., soluble proteins, including whey, and casein) on muscle protein synthesis have been well investigated after a single bout of resistance exercise (RE), the combined effects of these two proteins on the muscle responses to resistance training (RT) have not yet been investigated. Therefore, the aim of this study was to examine the effects of protein supplementation varying by the ratio between milk soluble proteins (fast-digested protein) and casein (slow-digested protein) on the muscle to a 9-week RT program. In a double-blind protocol, 31 resistance-trained men, were assigned to 3 groups receiving a drink containing 20g of protein comprising either 100% of fast protein (FP(100), n = 10), 50% of fast and 50% of slow proteins (FP(50), n = 11) or 20% of fast protein and 80% of casein (FP(20), n = 10) at the end of training bouts. Body composition (DXA), and maximal strength in dynamic and isometric were analyzed before and after RT. Moreover, blood plasma aminoacidemia kinetic after RE was measured. The results showed a higher leucine bioavailability after ingestion of FP(100) and FP(50) drinks, when compared with FP(20) (p< .05). However, the RT-induced changes in lean body mass (p < .01), dynamic (p < .01), and isometric muscle strength (p < .05) increased similarly in all experimental groups. To conclude, compared with the FP(20) group, the higher rise in plasma amino acids following the ingestion of FP(100) and FP(50) did not lead to higher muscle long-term adaptations.

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Tomaschunas, Maja, Jörg Hinrichs, Ehrhard Köhn, and Mechthild Busch-Stockfisch. "Effects of casein-to-whey protein ratio, fat and protein content on sensory properties of stirred yoghurt." International Dairy Journal 26, no. 1 (September 2012): 31–35. http://dx.doi.org/10.1016/j.idairyj.2012.04.005.

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Daviau, Célina, Alice Pierre, Marie-Hélène Famelart, Henri Goudédranche, Daniel Jacob, Maurice Garnier, and Jean-Louis Maubois. "Whey drainage during soft cheese manufacture and properties of drained curd as modified by casein concentration, whey protein to casein ratio, and pasteurisation of milk." Le Lait 80, no. 6 (November 2000): 573–87. http://dx.doi.org/10.1051/lait:2000145.

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Yukalo, Volodymyr, Kateryna Datsyshyn, and Liudmyla Storozh. "IMPROVEMENT OF THE METHOD OF COMPARATIVE STUDY OF MILK WHEY PROTEINS ENZYMATIC HYDROLYSIS." EUREKA: Life Sciences 5 (September 17, 2019): 52–57. http://dx.doi.org/10.21303/2504-5695.2019.00993.

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Milk whey proteins are valueble nutritional ingredients with a number of health-beneficial properties. Whey proteins are also a source of bioactive peptides that can be released in the process of proteins enzymatic hydrolysis. In this connection, there often is a need to compare their proteolytic action on milk whey proteins. It is important to take into account the specificities of the composition and properties of milk whey proteins. The aim of the research was to improve the method of comparative study of milk whey proteins enzymatic hydrolysis. Casein and whey were obtained from fresh cow skimmed milk. The whey was separated by centrifugation after casein precipitation at the isoelectric point. The following enzyme preparations were used in the research: neutral protease, papain, trypsin, chymotrypsin and pancreatin. To select β-LG, gel filtration of the milk whey on the chromatographic column with Sephadex G-150 (Pharmacia) was used. The homogeneity of the received β-LG preparation was analyzed by express electrophoresis in the polyacrylamide gel plates (PAG). The preparation of general casein was isolated by repeated precipitation at the isoelectric point. The fractional composition of the casein substrate was analyzed by electrophoresis in the anode system of homogeneous PAG in the presence of urea. Quantitative treatment of electrophoregrams of the β-LG preparation was performed using the imread reading function. Determination of proteolytic activity of enzyme preparations was carried out according to the method of V. F. Selemenev [6]. In the course of the research, it was determined, that for the research of proteolysis under conditions of identical total proteolytic activity, the concentration of neutral protease should be increased by 1.02 times, papain – by 4.2 times, trypsin – by 2.8 times, pancreatin – by 2.12 times as compared to chymotrypsin. As a result, it has been shown that the use of β-lactoglobulininstead of serum albumin in spectrophotometric determinations allows obtaining more accurate values of the concentrations of whey protein and proteolytic products. In determining the ratio of enzyme : substrate it is advisable to take into account the general proteolytic activity of various enzyme preparations in comparative studies of whey proteins proteolysis with various enzyme preparations. These will simplify the methodology and reduce the time for objective evaluation of enzymatic preparations for proteolysis of milk whey proteins. In some cases, considering the specificity of proteases it could increase the yield of biologically active peptides.

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Phosanam, Arissara, Jayani Chandrapala, Thom Huppertz, Benu Adhikari, and Bogdan Zisu. "In vitro digestion of infant formula model systems: Influence of casein to whey protein ratio." International Dairy Journal 117 (June 2021): 105008. http://dx.doi.org/10.1016/j.idairyj.2021.105008.

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Gilani, Sarwar, and Nana Farkye. "AOAC Expert Review Panel Adopts Official MethodsSM for Whey Protein/Casein Ratio in Infant Formula." Journal of AOAC INTERNATIONAL 96, no. 3 (May 1, 2013): 500. http://dx.doi.org/10.5740/jaoacint.gilani_whey_intro.

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Tseng, Emily, Susan M. Potter, and Mary Frances Picciano. "Dietary Protein Source and Plasma Lipid Profiles of Infants." Pediatrics 85, no. 4 (April 1, 1990): 548–52. http://dx.doi.org/10.1542/peds.85.4.548.

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Total cholesterol and triglyceride concentrations were measured in plasma samples taken at 4 and 8 weeks of age from 40 full-term infants who had been fed either human milk or one of three formulas containing casein-to-whey ratios of 82:18, 66:34, or 50:50 to investigate whether dietary protein influenced the development of plasma lipid profiles. Infants fed the formula with the casein-to-whey ratio of 82:18 had significantly higher plasma cholesterol levels at both 4 and 8 weeks of age compared with other groups of infants (P < .05). Infants fed the high-casein formula also showed an increase in plasma cholesterol levels with time (P < .001). Plasma triglyceride concentrations decreased as concentration of casein decreased (P < .05) among the formula-fed groups and increased with time. Infants fed human milk had plasma triglyceride concentrations similar to those infants who had been fed the 82:18 formula at 4 weeks of age; however, triglyceride concentrations eventually fell and were similar to those concentrations in infants who had been fed the 50:50 formula at 8 weeks of age. Results indicate that constituent lipids of human milk or formulas were not determining factors for changes observed in plasma cholesterol levels and triglyceride concentrations among groups. Since formulas differed only in proteins and their constituent amino acids, further investigation of the impact of dietary protein (amino acids) on development of blood lipid profiles in infants is warranted.

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BORCHERDING, KATJA, PETER C. H. R. LORENZEN, and WOLFGANG HOFFMANN. "Effect of protein content, casein-whey protein ratio and pH value on the foaming properties of skimmed milk." International Journal of Dairy Technology 62, no. 2 (May 2009): 161–69. http://dx.doi.org/10.1111/j.1471-0307.2009.00472.x.

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BORDIN, Cláudia Cantelli Daud, and Maria Margareth Veloso NAVES. "Hydrolyzed collagen (gelatin) decreases food efficiency and the bioavailability of high-quality protein in rats." Revista de Nutrição 28, no. 4 (August 2015): 421–30. http://dx.doi.org/10.1590/1415-52732015000400008.

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Objective Although deficient in all indispensable amino acids, gelatin is used in protein-restricted diets. Food efficiency and protein quality of casein and gelatin mixtures in low protein diets in Wistar rats were investigated. Methods The rats were treated with protein-restricted diets (10.0 and 12.5%) containing casein (control diets), casein with gelatin mixtures (4:1 of protein content), and gelatin as sources of protein. The food conversion ratio, protein efficiency ratio, relative and corrected protein efficiency ratio, true protein digestibility, and hepatic parameters were estimated. Results After 28 days of the experiment, food efficiency of 10.0% casein/gelatin diet decreased when compared to that of 10.0% casein diet, and the protein efficiency ratio of the casein/gelatin mixtures (10.0%=2.41 and 12.5%=2.03) were lower than those of the casein (10.0%=2.90 and 12.5%=2.32). After 42 days of the experiment, the weight of the liver of the animals treated with 10.0 and 12.5% casein/gelatin diets, and the liver protein retention of the 12.5% casein/gelatin diet group of animals were lower than those of the control group. Conclusion Gelatin decreases food efficiency and high-quality protein bioavailability in protein-restricted diets.

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Franceschi, Piero, Massimo Malacarne, Paolo Formaggioni, Claudio Cipolat-Gotet, Giorgia Stocco, and Andrea Summer. "Effect of Season and Factory on Cheese-Making Efficiency in Parmigiano Reggiano Manufacture." Foods 8, no. 8 (August 3, 2019): 315. http://dx.doi.org/10.3390/foods8080315.

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The assessment of the efficiency of the cheese-making process (ECMP) is crucial for the profitability of cheese-factories. A simple way to estimate the ECMP is the measure of the estimated cheese-making losses (ECL), expressed by the ratio between the concentration of each constituent in the residual whey and in the processed milk. The aim of this research was to evaluate the influence of the season and cheese factory on the efficiency of the cheese-making process in Parmigiano Reggiano cheese manufacture. The study followed the production of 288 Parmigiano Reggiano cheese on 12 batches in three commercial cheese factories. For each batch, samples of the processed milk and whey were collected. Protein, casein, and fat ECL resulted in an average of 27.01%, 0.72%, and 16.93%, respectively. Both milk crude protein and casein contents were negatively correlated with protein ECL, r = −0.141 (p ≤ 0.05), and r = −0.223 (p ≤ 0.001), respectively. The same parameters resulted in a negative correlation with casein ECL (p ≤ 0.001) (r = −0.227 and −0.212, respectively). Moreover, fat ECL was correlated with worse milk coagulation properties and negatively correlated with casein content (r = −0.120; p ≤ 0.05). In conclusion, ECLs depend on both milk characteristics and season.

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Chen, Fu-Tai A., and Ji-Hong Zang. "Determination of Milk Proteins by Capillary Electrophoresis." Journal of AOAC INTERNATIONAL 75, no. 5 (September 1, 1992): 905–9. http://dx.doi.org/10.1093/jaoac/75.5.905.

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Abstract The potential utility of capillary electrophoresis (CE) for routine determination of milk protein is established. Proteins in cow's milk can be determined by CE in 10 min with high separation efficiency. The major protein components of milk are well-separated and identified. Separations of milk proteins are achieved reliably and reproducibly in an untreated fused-silica column of 21 µm id x 23- 25 cm. Fresh homogenized, low-fat, and nonfat milk show almost identical contents of each protein species; dry milk has a substantially reduced amount of whey proteins, especially oc-lactalbumin. Extensive degradation of whey proteins is evident from a reconstituted dry milk, which may be used to differentiate dry from fresh milk. By using the ratio of β-casein to α-lactalbumin, the adulteration of fresh milk with 25% or more of dry milk could easily be detected.

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Xiong, Xiaoying, Minh Thao Ho, Bhesh Bhandari, and Nidhi Bansal. "Foaming properties of milk protein dispersions at different protein content and casein to whey protein ratios." International Dairy Journal 109 (October 2020): 104758. http://dx.doi.org/10.1016/j.idairyj.2020.104758.

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Kung, Bonnie, Sylvie L. Turgeon, Shirley Vien, Ruslan Kubant, Dalia El Khoury, Amanda J. Wright, H. Douglas Goff, and G. Harvey Anderson. "Role of Amino Acids in Blood Glucose Changes in Young Adults Consuming Cereal with Milks Varying in Casein and Whey Concentrations and Their Ratio." Journal of Nutrition 150, no. 12 (October 6, 2020): 3103–13. http://dx.doi.org/10.1093/jn/nxaa275.

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ABSTRACT Background Increasing the total protein content and reducing the casein to whey ratio in milks consumed with breakfast cereal reduce postprandial blood glucose (BG). Objectives We aimed to explore associations between plasma amino acids (AAs), BG, and glucoregulatory hormones. Methods In this repeated-measures design, 12 healthy adults consumed cereal (58 g) and milks (250 mL) with 3.1 wt% or high 9.3 wt% protein concentrations and with casein to whey ratios of either 80:20 or 40:60. Blood was collected at 0, 30, 60, 120, 140, 170, and 200 min for measurement of the primary outcome, BG, and for the exploratory outcomes such as plasma AA, gastric emptying, insulin (INS), and glucoregulatory hormones. Measures were made prior to and after an ad libitum lunch at 120 min. Exploratory correlations were conducted to determine associations between outcomes. Results Pre-lunch plasma AA groups [total (TAA), essential (EAA), BCAA, and nonessential (NEAA)] were higher after 9.3 wt% than 3.1 wt% milks by 12.7%, 21.4%, 20.9%, and 7.6%, respectively (P ≤ 0.05), while post-lunch AA groups were higher by 10.9%, 19.8%, 18.8%, and 6.0%, respectively (P ≤ 0.05). Except for NEAA, pre-lunch AAs were higher after 40:60 than 80:20 ratio milks by 4.5%, 8.3%, and 9.3% (P ≤ 0.05). When pooled by all treatments, pre-lunch AA groups associated negatively with BG (r/ρ ≥ −0.45, P ≤ 0.05), but post-lunch only TAA and NEAA correlated (r ≥ −0.37, P < 0.05). Pre-lunch BG was inversely associated with Leu, Ile, Lys, Met, Thr, Cys-Cys, Asn, and Gln (r/ρ ≥ −0.46, P ≤ 0.05), but post-lunch, only with Thr, Ala, and Gly (r ≥ −0.50, P ≤ 0.05). Pre-lunch associations between AA groups and INS were not found. Conclusions Protein concentration and the ratio of casein to whey in milks consumed at breakfast with cereal affect plasma AA concentrations and their associations with decreased BG. The decrease in BG could be explained by INS-independent mechanisms. This trial was registered at www.clinicaltrials.gov as NCT02471092.

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Fournaise, Tristan, Jennifer Burgain, Carole Perroud-Thomassin, and Jérémy Petit. "Impact of the whey protein/casein ratio on the reconstitution and flow properties of spray-dried dairy protein powders." Powder Technology 391 (October 2021): 275–81. http://dx.doi.org/10.1016/j.powtec.2021.06.026.

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Feng, Ping, Christophe Fuerer, Adrienne McMahon, K. Arendse, A. Chanady, H. Chen, W. Chen, et al. "Quantification of Whey Protein Content in Milk-Based Infant Formula Powders by Sodium Dodecyl Sulfate–Capillary Gel Electrophoresis (SDS-CGE): Multilaboratory Testing Study, Final Action 2016.15." Journal of AOAC INTERNATIONAL 101, no. 5 (September 1, 2018): 1566–77. http://dx.doi.org/10.5740/jaoacint.18-0057.

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Abstract A multilaboratory testing study was conducted on AOAC First Action Official Method SM 2016.15: Quantification of Whey Protein Content in Infant Formula Powders by Sodium Dodecyl Sulfate–Capillary Gel Electrophoresis (SDS-CGE). Nineteen laboratories participated in the analysis of duplicate blind-coded samples of 15 formula powder products for infants and young children. Electrophoregrams were recorded at UV220 nm and integrated. The normalized peak areas of whey and casein proteins were summed separately to calculate total whey protein content. Apart from one sample [NIST Standard Reference Material (SRM) 1849a], relative standard deviation of repeatability (RSDr) and reproducibility (RSDR) ranged from 0.83 to 2.11% and from 2.18 to 4.22%, respectively, and Horwitz ratios ranged from 1.02 to 1.85, meeting the precision limits specified in the whey protein Standard Method Performance Requirements and in the guidelines recommended for the Horwitz ratio. In these samples, the measured whey protein content was between 98 and 108% of the declared value. NIST SRM 1849a showed atypical results, with elevated RSDr (3.51%), RSDR (5.94%), Horwitz ratio (2.62), and recovery (134%). There is no clear reason for this. The percent whey protein value for NIST is calculated from the formulation and is not a reference or certified value. Multiple instrument models and makes, as well as capillary sources, were used in this collaborative study, demonstrating the robustness of the method. The method is fit-for-purpose for the quantification of whey protein content in milk-based formula powder products for infants and young children. It is not applicable to the analysis of hydrolyzed or plant protein–based infant formulas.

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Симоненко, Сергей Владимирович, Татьяна Алексеевна Антипова, Надежда Леонидовна Андросова, Светлана Валерьевна Фелик, Ольга Владимировна Кудряшова, and Елена Сергеевна Симоненко. "Milk protein concentrates for use in specialty foods." Food processing industry, no. 11 (October 27, 2022): 19–21. http://dx.doi.org/10.52653/ppi.2022.11.11.004.

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Недостаток пищевого белка в рационе питания ведет к нарушению работы желез внутренней секреции, состава крови; ослаблению умственной деятельности, замедлению роста и развития детей, снижению сопротивляемости к инфекциям. Это создает тенденцию к созданию продуктов с использованием молочно-белковых концентратов (МБК). Молочный белок, состоящий из казеина и сывороточных белков, является ценным источником белка, который обладает питательными и функциональными свойствами. Разделение определенных типов белковых фракций, переработка и использование их в пищевых продуктах стало возможно с появлением новых технологий. В данной статье рассматривается применение молочно-белковых концентратов (МБК) в специализированных рационах питания, направленных на устранение недостатка пищевого белка, улучшение аминокислотного состава и повышение биологической ценности продукта. Приведены некоторые характеристики наиболее технологичных и востребованных МБК, которые состоят из сывороточных белков, казеина или их сочетания. Приведены примеры использования МБК в качестве пищевой добавки при производстве различных пищевых продуктов: йогуртов, творога, сыров, десертов, высокобелковых продуктов. Указано различие МБК в зависимости от характеристик (массовой доли сухих веществ, формы, вида белка). Особую роль МБК играют в составе продуктов детского питания. Они являются поставщиком одновременно казеиновых и сывороточных белков. Особое внимание уделено МБК, получаемым при использовании мембранных технологий, позволяющих выделять молочные белки практически в нативном виде, без использования химических реагентов и других вспомогательных дорогостоящих материалов. Применение методов мембранного концентрирования при переработке молочного сырья позволяет молокоперерабатывающим предприятиям создавать новые технологии, увеличить рентабельность производства, обеспечить экологическую безопасность. Отмечено, что концентраты молочного белка, получаемые с использованием мембранной технологии, содержат как казеин, так и сывороточный белок в соотношении, существующем в молоке. Приведены отличительные особенности мицеллярного казеина, такие как содержание высококачественного белка, зависящего от способа очистки; растворимость в воде и др., позволяющие использовать его при разработке продуктов специализированного питания. The lack of dietary protein in the diet leads to disruption of the endocrine glands, blood composition, weakening of mental activity, slowing down the growth and development of children, and a decrease in resistance to infections. This creates a trend towards creating products using milk protein concentrates (MBC). Milk protein, composed of casein and whey proteins, is a valuable source of protein that has nutritional and functional properties. The separation of certain types of protein fractions, processing and use in food products, has become possible with the advent of new technologies. This article discusses the use of milk protein concentrates (MBC) in specialized diets aimed at eliminating the lack of dietary protein, improving the amino acid composition and increasing the biological value of the product. Some characteristics of the most technologically advanced and popular MBCs, which consist of whey proteins, casein, or a combination of both, are given. Examples of the use of MBC as a food additive in the production of various food products are given: yoghurts, cottage cheese, cheeses, desserts, high-protein products. The difference in MBC depending on the characteristics (mass fraction of solids, form, type of protein) is indicated. MBC play a special role in the composition of baby food. They are a supplier of both casein and whey proteins. Particular attention is paid to MBC obtained using membrane technologies that allow milk proteins to be isolated practically in their native form without the use of chemical reagents and other auxiliary expensive materials. The use of membrane concentration methods in the processing of raw milk allows milk processing enterprises to create new technologies, increase production profitability, and ensure environmental safety. It is noted that milk protein concentrates obtained using membrane technology contain both casein and whey protein in the ratio that exists in milk. The distinctive features of micellar casein are given, such as the content of high-quality protein, depending on the purification method; solubility in water, etc., allowing it to be used in the development of specialized food products.

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Fematt-Flores, Gabriela Eugenia, Ingrid Aguiló-Aguayo, Begonya Marcos, Belén Arely Camargo-Olivas, Rogelio Sánchez-Vega, Mayra Cristina Soto-Caballero, Nora Aideé Salas-Salazar, María Antonia Flores-Córdova, and María Janeth Rodríguez-Roque. "Milk Protein-Based Edible Films: Influence on Mechanical, Hydrodynamic, Optical and Antioxidant Properties." Coatings 12, no. 2 (February 2, 2022): 196. http://dx.doi.org/10.3390/coatings12020196.

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Edible films are thin preformed layers that provide food protection against adverse environmental conditions. Despite milk proteins being functional ingredients that can provide interesting features to films, there is scarce information evaluating their influence on film properties and stability. For this reason, this research work compared the mechanical (thickness, tensile strength, elongation at break), hydrodynamic (moisture content, water solubility, swelling ratio, water vapor transmission rate), color and antioxidant (DPPH) properties of edible films based on casein and whey protein isolate (two types, WPI1 and WPI2). Films with casein displayed the highest thickness (0.193 mm), elongation at break (49.67%), moisture content (40.21%) and antioxidant capacity (32.64% of DPPH inhibition), while obtaining the lowest water vapor transmission rate (15.28 g/m2·day). Significant differences were found in the color properties, mainly between films with casein and those made with WPI. Films containing WPI1 and WPI2 were statistically similar in thickness, tensile strength and color properties. The results showed that the properties of the edible films depended on the type of milk protein used. Thus, it is important to evaluate the features provided by different ingredients and formulations for obtaining edible films that properly preserve food.

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Sánchez-Hidalgo, Víctor Manuel, Samuel Flores-Huerta, Guadalupe Matute, Claudia Serrano, Bárbara Urquieta, and Rocío Espinosa. "Whey Protein/Casein Ratio and Nonprotein Nitrogen in Preterm Human Milk During the First 10 Days Postpartum." Journal of Pediatric Gastroenterology &amp Nutrition 26, no. 1 (January 1998): 64–69. http://dx.doi.org/10.1097/00005176-199801000-00011.

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Masum, A. K. M., Thom Huppertz, Jayani Chandrapala, Benu Adhikari, and Bogdan Zisu. "Physicochemical properties of spray-dried model infant milk formula powders: Influence of whey protein-to-casein ratio." International Dairy Journal 100 (January 2020): 104565. http://dx.doi.org/10.1016/j.idairyj.2019.104565.

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Aliev, Ayub Yu, Sergey V. Fedotov, and Natalya S. Belozertseva. "CHANGES IN THE PROTEIN COMPOSITION OF COWS' MILK FOR SUBCLINICAL MASTITIS." Problems of veterinary sanitation, hygiene and ecology 4, no. 44 (2022): 471–77. http://dx.doi.org/10.36871/vet.san.hyg.ecol.202204010.

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The nutritional value of milk and raw milk is determined by protein, so we paid special attention to determining the protein composition of raw milk. Were made measurements: the mass fraction of total nitrogen, the mass fraction of non-protein nitrogenous compounds, the content of urea, essential and non-essential amino acids. Biochemical studies of the protein composition of milk obtained from cows with suspected mastitis indicate that the content of total protein, casein, albumin and globulins in milk significantly changed with the growth of pathological processes in the mammary gland. Lactic cows underwent an express increase in the state of health, udder using Somatest manufactured and based on the result obtained, three groups of animals of 10 goals were formed. in everyone. 1st group detainees questionable test for Somatest express method; animals 2nd – weakly positive; the 3rd group included blood with a negative reaction to the tests. The difference in protein content was 5.71% (P < 0.05) and 3.27%; casein content – 13.27% (P < 0.001) and 11.98% (P < 0.05). According to the content of serum proteins, the opposite picture was observed, with the increase in udder pathology, the amount of albumins increased by 13.12% in the first group compared to the control; and by 26.39% – in the second group. In terms of the content of globulins, an increase was also noted in comparison with the control in the first group by 25.00% (P < 0.001) and 34.34% (P < 0.001). In milk samples of three test groups of animals, we identified 15 amino acids, of which 11 were essential and 4 non-essential. The test results indicate slight changes in the content of essential amino acids in cows with an increase in the inflammatory reaction in the udder. Diseases of the udder of cows are reflected in the quantitative ratio between the constituent parts of the protein fractions of milk, in particular, this is manifested in a decrease in casein, as well as in an increase in the content of whey proteins. Thus, the amount of casein needed to make cheese is reduced and whey protein is increased, making the milk unsuitable for cheese making.

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Jeong, Eun Woo, Gyu Ri Park, Jiyun Kim, So-Yul Yun, Jee-Young Imm, and Hyeon Gyu Lee. "Erratum to: Effect of Modified Casein to Whey Protein Ratio on Dispersion Stability, Protein Quality and Body Composition in Rats." Food Science of Animal Resources 43, no. 1 (January 2023): 195. http://dx.doi.org/10.5851/kosfa.2022.e78.

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Warncke, Malou, Ingrun Kieferle, Thanh Mai Nguyen, and Ulrich Kulozik. "Impact of heat treatment, casein/whey protein ratio and protein concentration on rheological properties of milk protein concentrates used for cheese production." Journal of Food Engineering 312 (January 2022): 110745. http://dx.doi.org/10.1016/j.jfoodeng.2021.110745.

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37

Kruchinin, Aleksandr G., Ekaterina I. Bolshakova, and Irina A. Barkovskaya. "Bioinformatic Modeling (In Silico) of Obtaining Bioactive Peptides from the Protein Matrix of Various Types of Milk Whey." Fermentation 9, no. 4 (April 14, 2023): 380. http://dx.doi.org/10.3390/fermentation9040380.

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Whey is a by-product of the production of various types of cottage cheese and cheese, casein, and coprecipitates. Conditions of milk coagulation directly affect the physico-chemical properties of whey and the formation of its protein profile. This fact makes it difficult to standardize the protein profile of milk whey for its further processing. Whey proteins have a great potential to release a wide range of bioactive peptides (BAP), capable of reducing the risk of a number of chronic food-related diseases. Computer modeling of an enzymatic hydrolysis of proteins is one of the ways to increase the efficiency of BAP release studies and to reduce the number of labor consuming experiments. This research is aimed at generating a digital model of the peptide complex of different whey types with predicted bioactivity, safety, and sensory properties using bioinformatic modeling approaches. The study was performed with the use of the proteomic databases tools according to the algorithm of hybrid strategy of bioinformatic modeling developed earlier. As a result of the study, taking into account the ranking of the proteins ratio in the protein profile, the hydrolysis by the protease complex chymotrypsin C-subtilisin was characterized as the maximum efficacy method to release peptides with both antioxidant and ACE-inhibitory activity. It was also observed that the bioactive peptides obtained as a result of in silico hydrolysis after GI digestion simulation can be considered safe in terms of allergic reactions and toxicological effects.

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Kalit, Samir, Milna Tudor Kalit, Iva Dolenčić Špehar, Krešimir Salajpal, Dubravka Samaržija, Jasna Anušić, and Ante Rako. "The Influence of Milk Standardization on Chemical Composition, Fat and Protein Recovery, Yield and Sensory Properties of Croatian PGI Lički Škripavac Cheese." Foods 10, no. 4 (March 24, 2021): 690. http://dx.doi.org/10.3390/foods10040690.

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The aim of this work was to evaluate the influence of cheese milk standardization on chemical composition, fat and protein recovery, yield and sensory properties of Croatian soft Protected Geographical Indication (PGI) Lički škripavac cheese. Standardization of milk to the casein/fat ratio of 0.7 was carried out by adding skimmed milk powder (SMP) to cheese milk and by skimming part of the milk fat. Results showed that losses of fat by whey were significantly (p < 0.05) lower after Lički škripavac cheese produced from standardized milk by skimming part of the milk fat. Standardization of cheese milk by addition of SMP caused higher losses of protein (p < 0.05) and total solids (p < 0.0001) by whey. Both methods of cheese milk standardization caused a significant (p < 0.01) decrease in milk fat and fat in dry matter content in cheese. In contrast, standardization of cheese milk caused a significant (p < 0.01) increase in protein content in cheese milk. Moisture in non-fat substance (MNFS) significantly (p < 0.05) decreased. Optimization of the casein/fat ratio did not cause a significant increase in fat recovery, but protein recovery significantly increased (p < 0.01). Addition of SMP to cheese milk significantly (p < 0.01) increased actual and adjusted cheese yield. The addition of SMP led to a noticeably higher (p = 0.10) sensory score of Lički škripavac cheese.

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Warncke, Malou, Sonja Keienburg, and Ulrich Kulozik. "Cold-Renneted Milk Powders for Cheese Production: Impact of Casein/Whey Protein Ratio and Heat on the Gelling Behavior of Reconstituted Rennet Gels and on the Survival Rate of Integrated Lactic Acid Bacteria." Foods 10, no. 7 (July 11, 2021): 1606. http://dx.doi.org/10.3390/foods10071606.

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The idea was to develop powders for fresh/hard cheese or quark production comprising milk proteins in optimal composition and functional properties for manufacturing each of those cheese types. The aim was to avoid whey protein drainage by their prior removal or by their heat-induced structural integration in the curd. The pre-renneted powders already contain additives such as starter cultures and calcium chloride to instantaneously form homogeneous curds upon reconstitution. The impact of the casein/whey protein ratio (86:14 by ultrafiltration and 98:2 by microfiltration) and upfront heat treatment (80 °C/30 min) on the gelling behavior of reconstituted rennet gels and on the survival rate of integrated Lactobacillus paracasei ssp. paracasei F19 was investigated. The assessment criteria for the rennet gelation were curd firming rate, gel strength, and whey drainage. Furthermore, the amount of integrated whey proteins and the resulting cheese yield were evaluated. It could be shown that heating had a positive effect on the viable cell count of the bacteria after spray drying and on the gelation behavior of the reconstituted ultrafiltration concentrates. The curd firming rate and the gel strength could be increased to higher values than the reconstituted microfiltration concentrate at 25% total solids.

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Solverson, Patrick, Sangita G. Murali, Adam S. Brinkman, David W. Nelson, Murray K. Clayton, Chi-Liang Eric Yen, and Denise M. Ney. "Glycomacropeptide, a low-phenylalanine protein isolated from cheese whey, supports growth and attenuates metabolic stress in the murine model of phenylketonuria." American Journal of Physiology-Endocrinology and Metabolism 302, no. 7 (April 1, 2012): E885—E895. http://dx.doi.org/10.1152/ajpendo.00647.2011.

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Phenylketonuria (PKU) is caused by a mutation in the phenylalanine (phe) hydroxylase gene and requires a low-phe diet plus amino acid (AA) formula to prevent cognitive impairment. Glycomacropeptide (GMP) contains minimal phe and provides a palatable alternative to AA formula. Our objective was to compare growth, body composition, and energy balance in Pahenu2 (PKU) and wild-type mice fed low-phe GMP, low-phe AA, or high-phe casein diets from 3–23 wk of age. The 2 × 2 × 3 design included main effects of genotype, sex, and diet. Fat and lean mass were assessed by dual-energy X-ray absorptiometry, and acute energy balance was assessed by indirect calorimetry. PKU mice showed growth and lean mass similar to wild-type littermates fed the GMP or AA diets; however, they exhibited a 3–15% increase in energy expenditure, as reflected in oxygen consumption, and a 3–30% increase in food intake. The GMP diet significantly reduced energy expenditure, food intake, and plasma phe concentration in PKU mice compared with the casein diet. The high-phe casein diet or the low-phe AA diet induced metabolic stress in PKU mice, as reflected in increased energy expenditure and intake of food and water, increased renal and spleen mass, and elevated plasma cytokine concentrations consistent with systemic inflammation. The low-phe GMP diet significantly attenuated these adverse effects. Moreover, total fat mass, %body fat, and the respiratory exchange ratio (CO2 produced/O2 consumed) were significantly lower in PKU mice fed GMP compared with AA diets. In summary, GMP provides a physiological source of low-phe dietary protein that promotes growth and attenuates the metabolic stress induced by a high-phe casein or low-phe AA diet in PKU mice.

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Liu, Weiji, Xiao Dong Chen, Romain Jeantet, Christophe André, Severine Bellayer, and Guillaume Delaplace. "Effect of casein/whey ratio on the thermal denaturation of whey proteins and subsequent fouling in a plate heat exchanger." Journal of Food Engineering 289 (January 2021): 110175. http://dx.doi.org/10.1016/j.jfoodeng.2020.110175.

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Burgain, J., C. Gaiani, C. Cailliez-Grimal, C. Jeandel, and J. Scher. "Encapsulation of Lactobacillus rhamnosus GG in microparticles: Influence of casein to whey protein ratio on bacterial survival during digestion." Innovative Food Science & Emerging Technologies 19 (July 2013): 233–42. http://dx.doi.org/10.1016/j.ifset.2013.04.012.

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43

Feng, Ping, Christophe Fuerer, and Adrienne McMahon. "Quantification of Whey Protein Content in Infant Formulas by Sodium Dodecyl Sulfate-Capillary Gel Electrophoresis (SDS-CGE): Single-Laboratory Validation, First Action 2016.15." Journal of AOAC INTERNATIONAL 100, no. 2 (March 1, 2017): 510–21. http://dx.doi.org/10.5740/jaoacint.16-0344.

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Abstract Protein separation by sodium dodecyl sulfate-capillary gel electrophoresis, followed by UV absorption at 220 nm, allows for the quantification of major proteins in raw milk. In processed dairy samples such as skim milk powder (SMP) and infant formulas, signals from individual proteins are less resolved, but caseins still migrate as one family between two groups of whey proteins. In the first group, α-lactalbumin and β-lactoglobulin migrate as two distinct peaks. Lactosylated adducts show delayed migration times and interfere with peak separation, but both native and modified forms as well as other low-MW whey proteins still elute before the caseins. The second group contains high-MW whey proteins (including bovine serum albumin, lactoferrin, and immunoglobulins) and elutes after the caseins. Caseins and whey proteins can thus be considered two distinct nonoverlapping families whose ratio can be established based on integrated areas without the need for a calibration curve. Because mass-to-area response factors for whey proteins and caseins are different, an area correction factor was determined from experimental measurement using SMP. Method performance assessed on five infant formulas showed RSDs of 0.2–1.2% (within day) and 0.5–1.1% (multiple days), with average recoveries between 97.4 and 106.4% of added whey protein. Forty-three different infant formulas and milk powders were analyzed. Of the 41 samples with manufacturer claims, the measured whey protein content was in close agreement with declared values, falling within 5% of the declared value in 76% of samples and within 10% in 95% of samples.

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Iváncsics, J., and A. Z. Kovács. "Zusammensetzung des Kolostrums bei einigen Fleischrinderrassen in Abhängigkeit von der nach dem Abkalben vergangenen Zeit." Archives Animal Breeding 42, no. 1 (October 10, 1999): 17–32. http://dx.doi.org/10.5194/aab-42-17-1999.

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Abstract. Title of the paper: The composition of the Colostrum of some beef cattle breeds according to time of post partum. This research was carried out to investigate the changes of main components of Colostrum with 0–4 days after calving by five beef cattle breds, kept in Hungary. After calving and 24 hours later beef cattle breeds had higher dry matter content in Colostrum compared to that of dairy breeds; but the dairy breeds were superior to the beef cattle breeds from the second day. This relates to the Colostrum of the beef cattle breeds more concentrated than the dairy breeds during the first 24 hours but they reached that values eariier which were characteristic to the normal milk. Examining the protein content of Colostrum there were similar tendencies in change of dry matter content with difference that the protein content of Colostrum of beef cattle breeds was higher than that of the dairy breeds between the 2nd and 4th days, too. On the first and the second days the fat content of Colostrum of the sucklers decreased which was related to the higher dilution in beef cattle breeds. The sugar content of Colostrum of the beef cattle breeds has increased between the calving and the 4th day post partum, and reached the values characteristic to the normal milk – (4.8–5.0%) – on the 5th–6th day. There was not significant difference between the beef and the dairy breeds, neither in sugar nor in the ash content. The ash content of Colostrum reached the values characteristic to the normal milk, 7–8 days after calving. The whey protein and the non protein nitrogen content of Colostrum of the beef cattle breeds were higher than that ofthe dairy breeds, significantly. Decreasing of these fractions in the beef cattle breeds were more moderate than the dairy breeds as in case of the total protein content, according to time. Our calculations show that whey protein content of the beef cattle breeds reached that values which were characteristic to the normal milk, after the 5th day post partum. Not having found a decided difference in the casein content of Colostrum between the beef and the dairy breeds. The casein content of Colostrum of blonde d' Aquitaine and Limousin higher than that ofthe other kind of beef cattle breeds, which manifests itself in the ratio of whey protein and casein, too. At the same time the ratio of whey protein and casein in both Angus types differ from the other beef cattle breeds in favour of the whey protein. The calculated immunglobulüj-G values of Colostrum milked immediately after calving were usually much higher at sucklers than at the dairy breeds. This was true especially beUveen the 1st and the 4th days which was connected with the more moderate decrease of IgG fraction in the beef cattle breeds. Similarly the data of the literature the IgG content ofthe fresh milked Colostrum was determined primarily by the breed. According to our examinations this determination becomes more unimportant moving off the time of calving. The energy content of Colostrum at Black Angus and Red Angus rose among the other kind of beef cattle breeds. The average energy content ofthe Colostrum of blonde d' Aquitaine and Limousin was connected with the high protein content of their Colostrum. The energy content of Colostrum of Hungarian Simmental was the lowest.

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Nielsen, Henrik K., P. A. Finot, and R. F. Hurrell. "Reactions of proteins with oxidizing lipids." British Journal of Nutrition 53, no. 1 (January 1985): 75–86. http://dx.doi.org/10.1079/bjn19850012.

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1. The consequences of reactions between protein and oxidizing lipids on the nutritional quality of food proteins have been investigated using a whey protein–methyl linolenate-water model system.2. In rat assays, significant reductions were observed in protein efficiency ratio, net protein ratio, net protein utilization, biological value and true nitrogen digestibility, especially when the reaction had taken place at high moisture content, high temperature and in the presence of excess oxygen.3. The losses of bioavailable lysine and tryptophan as measured by rat assays followed a similar pattern. The chemical value of each amino acid multiplied by the true N digestibility closely resembled the rat assay value. In general, the reaction products of lysine and tryptophan formed during lipid oxidation were biologically unavailable.4. The bioavailabilities of methionine and of ‘methionine plus cyst(e)ine’ were determined in separate assays. Cyst(e)ine was calculated as ‘methionine plus cyst(e)ine’ minus methionine. In whey protein which had reacted with oxidizing methyl linolenate, the bioavailable methionine content was not significantly reduced even though 82% of the methionine residues were present as methionine sulphoxide. In hydrogen peroxide-treated casein in which all methionine residues were oxidized to the sulphoxide, methionine sulphoxide was found to be 96% as utilizable as a methionine source to the rat. Free methionine sulphoxide was 87% utilizable.5. Cyst(e)ine appeared to be as sensitive as lysine to reactions with lipid oxidation products. In whey protein which had reacted with oxidizing methyl linolenate, the bioavailabilities of cyst(e)ine, lysine, tryptophan and methionine were reduced by 28, 24, 11 and 8% respectively and true N digestibility by 9%. These results are discussed in relation to food products.

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Puvanenthiran, A., R. P. W. Williams, and M. A. Augustin. "Structure and visco-elastic properties of set yoghurt with altered casein to whey protein ratios." International Dairy Journal 12, no. 4 (January 2002): 383–91. http://dx.doi.org/10.1016/s0958-6946(02)00033-x.

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Zhao, L. L., X. L. Wang, Q. Tian, and X. Y. Mao. "Effect of casein to whey protein ratios on the protein interactions and coagulation properties of low-fat yogurt." Journal of Dairy Science 99, no. 10 (October 2016): 7768–75. http://dx.doi.org/10.3168/jds.2015-10794.

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Jeong, Eun Woo, Gyu Ri Park, Jiyun Kim, Youjin Baek, Gwang-woong Go, and Hyeon Gyu Lee. "Whey Proteins-Fortified Milk with Adjusted Casein to Whey Proteins Ratio Improved Muscle Strength and Endurance Exercise Capacity without Lean Mass Accretion in Rats." Foods 11, no. 4 (February 16, 2022): 574. http://dx.doi.org/10.3390/foods11040574.

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This study investigated the effects of the casein to whey proteins (CW) ratio in milk on body composition, muscle strength, and endurance exercise capacity in rats. Thirty rats were assigned into five groups, and each treatment was administered for eight weeks: (1) control (isocaloric lactose supplementation), (2) CW8:2 (regular milk), (3) CW6:4, (4) CW5:5, and (5) nitrogen-free (lactose). The milk concentration was converted from a human equivalent dose (400 mL/60 kg body weight/day). All the milk-administered groups showed significantly greater growth performance, including body weight and weight gain compared to the isocaloric lactose control (p < 0.05). However, different CW ratios in milk had no effect on growth performance. Additionally, body composition, i.e., lean body mass and adiposity, was not affected by the CW ratio. Interestingly, CW6:4 and CW5:5 had significantly higher plasma branched-chain amino acids concentrations than control and CW8:2 (p < 0.05). In addition, CW5:5 showed significantly increased grip strength by 12–24% and time to exhaustion by 8–62% compared to the other groups (p < 0.05), indicating that the higher whey proteins ratio improved physical performance. We concluded that whey proteins-fortified milk enhances muscle strength and endurance exercise capacity without altering lean mass in rats.

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Sharp, Matthew Alan, and Gabriel Harris. "A Method for Determination of Unbound Fats in Protein Bar Formulations Compared with Isolated Fat/Protein Combinations to Optimize Shelf Life." Current Developments in Nutrition 4, Supplement_2 (May 29, 2020): 776. http://dx.doi.org/10.1093/cdn/nzaa052_045.

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Abstract Objectives Protein bars form a growing part of the snack food industry, but shelf life is typically limited by bar hardening due to protein aggregation related to the migration of other nutrients. Addressing these issues will extend protein bar shelf life while continuing to maintain nutrient density for military personnel and extreme athletes. We developed a method to examine the interaction of fats and proteins in bars and in simple mixtures in order to address lipid/protein interaction and lipid migration. Methods Mixtures of dairy protein and fats were created in order to determine ideal fat/protein ratios. Fats tested were palm kernel oil (PKO), cocoa butter, coconut oil, and canola oil. Proteins included milk protein isolate, a dairy protein blend, whey protein concentrate, and two whey protein isolates (WPI). Fats were liquified, mixed with protein at 0/100 up to a 50/50 ratio by weight and allowed to solidify. Solidified pellets were suspended in filters placed in conical tubes at a temperature four degrees Celsius above the melting point of the fat for twelve to twenty-four hours. The weight of melted fat that passed through the filter was then determined. Results At 50/50 ratios, the combinations of cocoa butter and PKO with WPI and whey protein concentrates demonstrated 1% and 3% fat loss, respectively. While a ratio of 59/41% lipid/protein respectively, cocoa butter and PKO with WPI continue to have the lowest residual fat at 14% while the highest is coconut oil and milk protein isolate at a residual fat content of 29%. Low residual fat is between one and three % residual in a 50%/50% matrix, while low-fat retention is anything above 14% residual fat. The dairy blend and milk protein isolate have low-fat retention with saturated fats but have increased retention with canola oil. Coconut oil has a high residual fat of 25% with the milk protein isolate that contains both casein and whey proteins. Conclusions The ideal fat protein mixtures for military personnel and extreme athletes are WPI's and with PKO or cocoa butter. By using these two fats with the whey protein isolates, it creates an ideal matrix for protein bar stability preventing bar hardening and long shelf life while keeping nutrient density. Funding Sources Military grant-funded by the Defence Logistics Agency and SMRC.

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Milenteva, Irina, Natalia Davydenko, and Aleksandr Rasshchepkin. "Casein Proteolysis in Bioactive Peptide Production: Optimal Operating Parameters." Food Processing: Techniques and Technology 50, no. 4 (December 30, 2020): 726–35. http://dx.doi.org/10.21603/2074-9414-2020-4-726-735.

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Introduction. Public health is gradually deteriorating as a result of unhealthy lifestyle and diet, which triggers allergic reaction to certain foods. Milk and dairy products are rich in biologically active substances, which makes them a good dietary supplement for athletes, diabetic patients, etc. However, this popular food contains allergens, for instance, such proteins as αS1-casein, αS2-casein, β-casein, and κ-casein. Therefore, one of the most urgent tasks of modern food science is to reduce the allergenic properties of casein. Heat treatment is an option, but thermal exposure leads to denaturation and produces new antigenic determinants, e.g. epitopes. Biotechnological processing is a more promising method. It is based on the catalytic properties of proteolytic enzymes. Enzymes make it possible to obtain a protein hydrolyzate with amino acids of various molecular weights. The present research provided the optimal working parameters of casein proteolysis by various enzymes (endopectidases), namely trypsin, chymotrypsin, and thermolysin. Study objects and methods. Casein hydrolysates are casein-based biopeptides, and casein is an accessible and valuable milk protein. Trypsin, chymotrypsin, and thermolysin were used as proteases. The experiment was based on standard methods. Results and its discussion. At 47 ± 2°C and pH 7.5 ± 0.2, the production of low-molecular-weight components of casein hydrolyzate proved feasible when thermolysin was used at a ratio of 1:100 for 24.00 ± 0.05 h, and chymotrypsin and trypsin – at a ratio of 1:25 for 24.00 ± 0.05 h. Conclusion. The resulting casein hydrolysates contain biologically active peptides and can be used in formulations of low-allergy functional dairy products in allergy-friendly, sports, and baby diets.

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Journal articles on the topic 'Casein/whey protein ratio'

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