Maillard Reaction in Milk-Based Foods: Nutritional Consequences

1998 ◽  
Vol 61 (2) ◽  
pp. 235-239 ◽  
Author(s):  
LAURA PIZZOFERRATO ◽  
PAMELA MANZI ◽  
VITTORIO VIVANTI ◽  
ISABELLA NICOLETTI ◽  
CLAUDIO CORRADINI ◽  
...  

Chemical reactions occurring during industrial treatments or storage of foods can lead to the formation of ε-deoxyketosyl compounds, the Amadori products. Food protein value can be adversely affected by these reactions, and in particular lysine, an essential amino acid having on its side chain a free amino group, can be converted to nonbioavailable N-substituted lysine or blocked lysine. By acid hydrolysis of ε-deoxyketosyl compounds, furosine is formed. In this paper furosine prepared from milk-based commercial products has been evaluated by use of a recently developed HPLC method using a microbore column and phosphate buffer as the mobile phase at controlled temperature. Furosine levels have been used, together with protein, total amino acids, and lysine content, as an estimate of protein quality of a few different products such as cooked-cream dessert, yogurt mousse, white chocolate, milk chocolate, milk chocolate with a soft nougat and caramel center, milk chocolate with a whipped white center, chocolate spread, part-skim milk tablets, milk-based dietetic meals, and baby foods. The protein content of the analyzed products ranged from 34.3 g · kg−1 (milk nougat) to 188.4 g · kg−1 (milk tablets). The Maillard reaction caused a loss in available lysine that varied from 2.5% (cooked cream) to 36.2% (condensed milk). The contribution to the lysine average daily requirement is heavily affected by this reaction and varied from 13% (milk tablets and soft nougat) to 61% (dietetic meal). Variable results were also obtained for the other essential amino acids.

Proceedings ◽  
2020 ◽  
Vol 70 (1) ◽  
pp. 4
Author(s):  
Sara Bautista-Expósito ◽  
Elena Peñas ◽  
Albert Vanderberg ◽  
Juana Frias ◽  
Cristina Martínez-Villaluenga

Legumes are alternative protein sources that have been successfully used to develop diverse meatless foods. Although these plant-based products have a lower impact on the environment than equivalent animal-based products, they have lower protein digestibility. Germination could be a useful bioprocess to enhance protein digestibility in legumes, although its effect at different times of seedling development has been little studied in lentils and faba beans. This work investigated the effect of germination time (4 and 6 days after full seed imbibition) on the proteins of three types of Canadian lentils (“gray zero tannin”, G; “caviar black”, B; and “red dehulled”, D) and faba beans (“zero vicin/convicin”, F). Germination increased total nitrogen (4–14% increase) and total levels of some amino acids: Asp in all the sprouts studied; Ser, Pro, Ala, Cys, His and Lys in G; and Met and Tyr in B. A concurrent degradation of the 7S and 11S globulin subunits, the accumulation of peptides below 20 kDa and free essential and non-essential amino acids (4- to 6-fold increase) were observed after germination in all the legumes studied. These effects were attributable to the increased protease activity observed after sprouting. Trypsin inhibitory activity was lower in legume sprouts, except for D, where a small increase was detected. Time, legume type and their interaction showed significant effects on the parameters studied. Germination effects were generally more remarkable at longer stages of seedling development. Among the legumes studied, D showed a differential behavior characterized by a faster protein degradation and release of small peptides, probably due to its higher protease activity as indicated by principal component analysis. These results evidence the positive effects of germination on the protein digestibility of different lentil types and faba beans. The protein quality of plant-based foods could be improved through the selection of legume species with higher germination-induced proteolytic rates and optimized germination times.


2020 ◽  
Vol 25 (2) ◽  
pp. 30
Author(s):  
Ayodeji Ahmed Ayeloja ◽  
W. A. Jimoh ◽  
T. O. Uthman ◽  
M. O. Shittu

Effect of storage time on the quality of smoked heteroclarias was studied. 108 samples of heteroclarias (average weight 210 + 15g) was used. Analysis carried out include: proximate, mineral composition (Ca, Na, Fe and Mg), biochemical, amino acid and sensory evaluation. Data obtained was subjected to Analysis of Variance (ANOVA) while the sensory data was subjected to nonparametric test (Kruskal Wallis test). Smoked heteroclarias have good nutritional quality in terms of proximate, mineral and amino acids all of which decrease with increase in duration of storage at ambient temperatures. Glutamic acid  was the most predominant amino acid and the highest non-essential amino acid (NEEA), lysine was the most predominant EAA. There was higher concentration of non-essential amino acids than essential amino acids, EAA/NEAA ratio (0.86 – 0.93) recorded indicates that the fish have excellent protein quality; its the predicted protein efficiency ratio (P-PER) ranged between 3.44-3.61 and its biological value ranged between 79.84 -75.04. Its chemical score and TEAA decrease with increase in storage time. Its texture quality reduced significantly (χ2 = 12.207, p<0.01) with increased storage period. It is therefore recommended that smoked heteroclarias be consumed as soon as it is smoked and regularly for good healthy conditions especially among children, aged and other vulnerable groups.


1972 ◽  
Vol 23 (5) ◽  
pp. 913 ◽  
Author(s):  
AC Kondos ◽  
GL McClymont

The effect on the protein quality of meat meals of processing them under commercial conditions in a continuous dry renderer at maximum temperatures ranging from 116 to 160°C for a running time of 115 min was studied. Although the total levels of amino acids were little affected by processing temperatures, the biological availability of all essential amino acids, as determined by the protozoan Tetrahymena pyriformis, was reduced as the processing temperature increased. At 140 and 160°C the availability of certain amino acids was reduced by 37-56%, lysine, histidine, and methionine being the most severely affected. The availability of essential amino acids in meals produced at temperatures from 121 to c. 138° was not significantly different. The growth-promoting ability of the meat meals for chickens was closely related to the availability of the essential amino acids. __________________ *Part VI, Aust. J. Agric. Res., 19: 171 (1968).


1995 ◽  
Vol 1995 ◽  
pp. 36-36
Author(s):  
R.M. Kay ◽  
P.A. Lee

In the UK, pollution of the water system with nitrate nitrogen leaching from the soil is seen as a major problem and farm animal effluents have been identified as a major source of nitrate pollution. It would, therefore, be beneficial to the livestock producer and to the environment if the nitrogen excretion from animals could be kept to a minimum. To limit the excretion of nitrogen by the pig, it is necessary to supply amino acids in the diet in better agreement with its dietary requirements. This could be achieved either by feeding diets according to the pig's requirements based on age and/or weight (phase feeding) or by improving protein quality. The best protein quality would be that which has the same balance of essential amino acids (EAA) with respect to lysine as that required by the pig, i.e. ideal protein. Diets formulated on the basis of total dietary EAA on an ideal protein basis, using crystalline EAA, could enable lower crude protein (CP) diets to be offered whilst maintaining nitrogen retention (NR). An alternative approach to formulating diets would be to base the formulations on either: 1) currently available, commercial database values for ileal digestible EAA values of ingredients to achieve diets as close to ideal protein as possible but within least cost formulation constraints; or 2) ingredients limited simply to cereals and pulses and supplemented with crystalline EAA to formulate as close to ideal protein as possible. The object of the present experiment was to evaluate diets, formulated on this basis, in terms of nitrogen intake (NI), excretion (NE) and retention (NR) in pigs using balance studies.


1979 ◽  
Vol 62 (6) ◽  
pp. 1358-1360
Author(s):  
Susan K Henderson ◽  
Lucia A Mclean

Abstract Vitamin A was determined in fortified chocolate milk and skim milk; vitamin D was determined in fortified chocolate milk, skim milk, and vitamin D concentrates, using reverse phase high pressure liquid chromatography (HPLC). The sample is saponified, extracted with hexane, and chromatographed in an HPLC system on a 10 μm Vydac TP reverse phase C18 column, using acetonitrile-methanol (9+1) as the mobile phase. For 6 replicates, the recoveries of vitamins A and D, using this procedure, were 99 and 98%, respectively.


2019 ◽  
Vol 110 (2) ◽  
pp. 255-264 ◽  
Author(s):  
Paolo Tessari

ABSTRACT Background Essential amino acids (EAAs) are key factors in determining dietary protein quality. Their RDAs have been estimated. However, although nonessential amino acids (NEAAs) are utilized for protein synthesis too, no estimates of their usage for body protein replenishment have been proposed so far. Objective The aim of this study was to provide minimum, approximate estimates of NEAA usage for body protein replenishment/conservation in humans. Methods A correlation between the pattern of both EAAs and NEAAs in body proteins, and their usage, was assumed. In order to reconstruct an “average” amino acid pattern/composition of total body proteins (as grams of amino acid per gram of protein), published data of relevant human organs/tissues (skeletal muscle, liver, kidney, gut, and collagen, making up ∼74% of total proteins) were retrieved. The (unknown) amino acid composition of residual proteins (∼26% of total proteins) was assumed to be the same as for the sum of the aforementioned organs excluding collagen. Using international EAA RDA values, an average ratio of EAA RDA to the calculated whole-body EAA composition was derived. This ratio was then used to back-calculate NEAA usage for protein replenishment. The data were calculated also using estimated organ/tissue amino acid turnover. Results The individual ratios of World Health Organization/Food and Agriculture Organization/United Nations University RDA to EAA content ranged between 1.35 (phenylalanine + tyrosine) and 3.68 (leucine), with a mean ± SD value of 2.72 ± 0.81. In a reference 70-kg subject, calculated NEAA usage for body protein replenishment ranged from 0.73 g/d for asparagine to 3.61 g/d for proline. Use of amino acid turnover data yielded similar results. Total NEAA usage for body protein replenishment was ∼19 g/d (45% of total NEAA intake), whereas ∼24 g/d was used for other routes. Conclusion This method may provide indirect minimum estimates of the usage of NEAAs for body protein replacement in humans.


Author(s):  
Radha Palaniswamy ◽  
Dhanyasri Selvaraj ◽  
Sandhiya Renganathan

Objective: To determine the protein quality, especially the amino acid content of 8 tropical fruits both raw and boiled samples. Eight different tropical fruits were used in the study (Apricot, Jamun, Dragonfruit, Pomegranate, Mangustan, Litchi, Jackfruit, and Kiwi.Methods: Ninhydrin method was used for the estimation of the concentration of amino acids present in the above fruits. Raw and boiled fruits were used for the study.Results: Both raw and boiled forms which showed thats Jamun and Mangustan contained highest concentration amino acids whereas apricot shows the lowest concentration of amino acids except in Jamun which showed higher values in the raw fruit whereas in others the boiled samples showed higher values.Conclusion: It was evident that tropical fruits have a good balance of the essential amino acids (both raw and boiled fomr) which provide significant sources of protein in our diet.


1985 ◽  
Vol 68 (1) ◽  
pp. 52-56 ◽  
Author(s):  
Ghulam Sarwar ◽  
Robert Blair ◽  
Mendel Friedman ◽  
Michael R Gumbmann ◽  
Ross L Hackler ◽  
...  

Abstract Estimates of inter- and intralaboratory variation of protein efficiency ratio (PER), relative PER (RPER), net protein ratio (NPR), relative NPR (RNPR), and nitrogen utilization (NU) were compared with those of amino acid analysis in the same batches of 7 protein sources (ANRC casein, egg white solids, minced beef, soy assay protein, rapeseed protein concentrate, pea flour, and whole wheat flour). Interlaboratory variation (estimated as between-laboratories coefficients of variation, CV) of NPR and RNPR (up to 6.0%) was lower than that of PER (up to 20.2%) and RPER (up to 18.5%). The interlaboratory determination of NPR and RNPR was also more reproducible than that of most essential amino acids (CV up to 10.0%), especially tryptophan (CV up to 23.7%), cystine (CV up to 17.6%), and methionine (CV up to 16.1%). Intralaboratory variation (estimated as within-laboratories CV) of amino acid analysis (up to 4.7%), however, was comparable to that of protein quality indices in most protein sources (up to 6.0%). The significant (P &lt;0.01) positive correlations (r = 0.68-0.74) between amino acid scores and protein quality indices based on rat growth were further improved when amino acid scores were corrected for digestibility of protein (r = 0.73-0.78) or individual amino acids (r = 0.79- 0.82).


2016 ◽  
Vol 99 (1) ◽  
pp. 153-169
Author(s):  
Robert S Salter ◽  
Gregory W Durbin ◽  
Patrick Bird ◽  
Kiel Fisher ◽  
Erin Crowley ◽  
...  

Abstract Peel Plate™ EC is a low-profile plastic, 47 mm culture dish with an adhesive top that contains a dried medium with Gram-negative selective agents and with enzyme substrate indicators for β-galactosidase (coliform) and β-glucuronidase (Escherichia coli). The method provides a conventional quantitative coliform (red) and E. coli (blue/purple/black) count with simple rehydration and incubation for 24 ± 2 h at 35 ± 1°C, while providing a total coliform result, sum of E. coli, and coliform without color differential in dairy products at 32 ± 1°C for 24 ± 2 h. Dairy matrixes claimed and supported with total coliform data are whole milk, skim milk, chocolate milk (2% fat), heavy cream (35% fat), pasteurized whole goat milk, ultra-high-temperature pasteurized milk, powdered milk, lactose-reduced milk, strawberry milk, shredded cheddar cheese, raw cow milk, raw goat milk, raw sheep milk, sour cream, condensed milk, eggnog, vanilla ice cream, condensed whey, yogurt, and cottage cheese. Matrixes claimed for E. coli and total coliform detection are raw ground beef, mixed cellulose 0.45 μm filtered bottled water, environmental sponge of stainless steel, raw ground turkey, dry dog food, liquid whole pasteurized eggs, milk chocolate, leafy green (mixed greens) rinse/flume water, irrigation water, poultry carcass rinse, and large animal carcass sponge. The method has been independently evaluated for total coliform in whole milk, skim milk, chocolate milk, and heavy cream. The method was also independently evaluated for E. coli and coliform in ground beef, filtered bottled water, and sponge rinse from stainless steel surfaces. In inclusivity and exclusivity studies, the method detected 57 of 58 different strains of coliform and E. coli at 32 ± 1°C and 35 ± 1°C in and excluded 31 of 32 different noncoliform strains consisting of Gram-negative and Gram-positive bacteria. In the matrix study, each matrix was assessed separately at each contamination level in comparison to an appropriate reference method. Colony counts were determined for each level and then log10 transformed. The transformed data were evaluated for repeatability, log-mean comparison between methods with 95% confidence interval, and r2. A 95% confidence interval range of −0.5 to 0.5 on the mean difference was used as the acceptance criterion to establish significant statistical difference between methods. The evaluations demonstrate that the Peel Plate EC method provides no statistical differences across most of the matrixes. The coliform r2 values were greater than 0.9 except in the case of skim milk (r2 = 0.77 and 0.69), sheep milk (0.84), and chocolate (0.81). In the case of skim milk, the three highest concentrations were significantly biased low compared with the reference method, whereas in the case of chocolate, the highest concentration was significantly biased high. The E. coli r2 values were greater than 0.9 except in the case of hog rinse (0.89), flume water (0.82), and chocolate (0.77). The lower values were generally from only a 1 log difference between highest and lowest concentrations except in the case of chocolate, in which the highest concentration was biased high compared with the reference method. Within-method repeatability of Peel Plate EC was similar to the reference method, with relative SDs generally less than 5% when log10 means were ≥1.5. QC data support that the Peel Plate EC is stable for 1 year when refrigerated. Incubation temperature ranges, 30–36°C, and times, 22–26 and 48 h for yogurt, were not significantly different in paired t-test comparison. The method is selective without the need for confirmation, although confirmation of coliform and E. coli was performed as part of the validation work.


2012 ◽  
Vol 108 (S2) ◽  
pp. S333-S336 ◽  
Author(s):  
Gertjan Schaafsma

PDCAAS is a widely used assay for evaluating protein quality. It is a chemical score, which is derived from the ratio between the first limiting amino acid in a test protein and the corresponding amino acid in a reference amino acid pattern and corrected for true faecal N digestibility. Chemical scores exceeding 100 % are truncated to 100 %. The advantages of the PDCAAS are its simplicity and direct relationship to human protein requirements. The limitations are as follows: the reference pattern is based on the minimum amino acid requirements for tissue growth and maintenance and does not necessarily reflect the optimum intake. Truncated PDCAAS of high-quality proteins do not give any information about the power of these proteins to compensate, as a supplement, for low levels of dietary essential amino acids in low-quality proteins. It is likely that faecal N digestibility does not take into account the loss from the colon of indispensable amino acids that were not absorbed in the ileum. Anti-nutritional factors, such as lectins and trypsin inhibitors, in several plant protein sources can cause heightened endogenous losses of amino acids, an issue which is particularly relevant in animal feedstuffs. The assumption that amino acid supplementation can completely restore biological efficiency of the protein source is incorrect since the kinetics of digestion and absorption between supplemented free amino acids and amino acids present in dietary proteins, are different.


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