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Ce cile Bos, PhD, Claire Gaudichon, PhD, and Daniel Tome , PhD INRA, Nutrition humaine et physiologie intestinale, Institut National Agronomique Paris-Grignon, 16, rue Claude Bernard 75005 Paris, FRANCE Key words: dietary protein, quality, bioavailability, indispensable amino acids, requirements, peptides, bioactivity
Dietary protein quality is influenced by several factors and especially amino acid composition as well as the bioavailability of the protein. The method to assess the dietary protein quality recommended by the FAO/WHO (1985, 1990) is based on the ability of the protein to satisfy the indispensable amino acid requirements. The Protein Digestibility Corrected Amino Acid Score (PD-CAAS) has been proposed as a quality index and takes into account both the indispensable amino acid composition and the protein digestibility. This index can easily be used routinely, but some conceptual and methodological limits must be considered, such as the determination of both nitrogen and indispensable amino acid requirements, the bioavailability of dietary protein and the validation of the quality indexes. Another level in the evaluation of protein quality considers more specific activities related to specific protein-derived components. The compounds responsible for these activities include enzymes, immunoglobulins, mediator and hormone-like substances. These actions are linked to native proteins or to peptides cleaved from protein during digestion.
Cows milk represents a major dietary source for young and adult humans, and cow milk proteins are considered to have a high nutritional quality. The nutritional value of dietary proteins is usually related to their ability to achieve N and amino acid requirements for tissue growth and maintenance [1 4]. This ability depends both on the protein content of indispensable amino acids and on the digestibility of the protein and subsequent metabolism of the absorbed amino acids. The bioavailability of each indispensable amino acid represents a major factor of nutritional quality
of the different dietary proteins. The general concept underlying this approach is of interest in implementing standards reflecting the relative nutritional values of different protein sources. The recommendations for dietary protein edited by the FAO/WHO (1990) [5] take into account both the protein composition of indispensable amino acids and its digestibility. In addition, milk proteins are also believe to play a potential functional role by acting on nutrient supply, as protective compounds against aggression or by a regulatory action on different physiological functions.
Address reprint requests to: Daniel Tome , PhD, INRA, Nutrition humaine et physiologie intestinale, Institut National Agronomique Paris-Grignon, 16, rue Claude Bernard 75005 Paris, FRANCE
Journal of the American College of Nutrition, Vol. 19, No. 2, 191S205S (2000) Published by the American College of Nutrition 191S
Table 1. Indispensable Amino Acid Requirements (mg/kg/j) Assessed in Adults with Nitrogen Balance (1) or Amino Acid Oxidation (2) Method
His (1) (2) 12 12 Ile 10 23 Leu 14 40 Val 10 20 Lys 12 30 Met Cys 13 16 Phe Tyr 14 39 Thr 7 15 Trp 3, 5 6
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The Chemical Score and the Protein Digestibility Corrected Amino Acid Score
The initial method of the chemical score [7] is based on the complete analysis of food amino acid content and its comparison to amino acid pattern of a reference protein. The PDCAAS (Protein Digestibility Corrected Amino Acid Score) more recently adopted by the FAO/WHO [5] includes both the amino acid composition and the digestibility of a protein. The accuracy of amino acid analysis constitutes a first limitation for the calculation of the amino acid score. Another important limitation is the calculation of reference profiles for indispensable amino acids based on the determination of the requirements. Reference Profiles for Indispensable Amino Acids. Since 1985, FAO edited an amino acid profile reflecting a virtual ideal protein covering the human amino acid requirements. The relevance of the level of the amino acid requirements is then of major concern. Until relatively recently, the international FAO/ WHO/UNU [7] requirement values were based on the classical N balance studies of Rose and others [12]. Four amino acid reference patterns were first established for infant, pre-school children, school children and adult. The pattern for infants was derived from the human milk protein composition, whereas the other were derived from nitrogen balance studies. In this last case, reference profiles were calculated from an intake of 0.7 g/kg/d of protein and a metabolic efficiency of 70% for dietary nitrogen. The N-balance derived estimates are relatively low, and they would be easily met by nearly every human diet around the world, including diets of relatively poor quality that are consumed in many Third World countries [61]. The N-balance derived requirement estimates have however
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Nitrogen Retention
Another approach of the dietary protein bioavailability is based on the determination of the extent to which the nitrogen absorbed in the intestine is retained and metabolized by the organism. This implies the measurement of fecal and urinary nitrogen losses. On this basis, the dietary nitrogen retention can be calculated. This method allows for a very accurate approach of the protein nutritional value. Such methods may act as reference methods for indices validation. The nitrogen balance indicates the amount of nitrogen that is retained in the body according to the following formula: Nitrogen balance Ingested nitrogen Excreted nitrogen (urine and feces) The Net Protein Utilization (NPU) permits the evaluation of the part of the N ingested that is retained: NPU N retained/N ingested The Biological Value (BV) gives the percentage of absorbed nitrogen that is retained: BV N retained/N absorbed In the same manner as with the digestibility, these values are true or apparent depending on whether the endogenous nitrogen is taken into account. Endogenous losses may be estimated either from a situation of protein-free diet or by using stable isotope tracer methodologies. Thus, it follows that:
NPU BV digestibility
This value includes the true digestibility of the protein. When the measurements involve small animals, it is possible to determine directly the nitrogen retained by analysis of the total nitrogen content from the carcass. If the experiments are made in conditions such as a single amino acid in its limiting amount, the result provides a valuable insight into the bioavailability or the digestibility of this amino acid. The classical approach for the measurement of net nitrogen retention usually originates from nitrogen balance data measured in subjects after adaptation to different protein levels for several days [1,4]. One of the major limitation to this method is the existence of a diurnal cycling for the transition between the fasted and fed states, leading alternately to nitrogen postprandial accretion and postabsorptive loss phases. From these considerations, the retention calculated on a daily basis is lower than that derived from the postprandial phase [66]. Another point of view concerns the deposition of dietary nitrogen during the postprandial phase, which is likely to be the critical step for
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CONCLUSION
Among the available methods for the evaluation of protein quality in food, those based on indices calculations progressively stand out due to their scientific logic and their ease in implementation. However they present limits that have to be taken into account. For instance, some questions are raised by the use of the PD-CAAS, despite its interest. Both the criteria and the methods relative to the assessment of reference requirements for indispensable amino acids have to be further examined. The initial requirement values derived from nitrogen balance studies are generally taken as too low with regard to the new data obtained from the oxidation methods. These latter present as well some shortcomings, and there is not always agreement between results calculated by either direct or indirect methods. A subsequent question concerns nitrogen metabolism in the colon. The possibility of amino acid synthesis available for the organism has to be documented. A second problem lies in the assessment of amino acid digestibility and bioavailability. Ileal digestibility for individual amino acids should probably be considered, but this methodology is difficult. Moreover, this implies the establishment of correlations between methods with a view to defining and validating a fast measurement method reliable in comparison to data collected in humans. It is thus necessary to validate the PD-CAAS values against bioavailability measurements. The limitation of this index at 100% should not only be considered from a theoretical point of view but also in the aim of obtaining the best correlation between calculated and in vivo experimental data. Another level of milk protein evaluation is their potential role as bioactive components. Research conducted during the last 30 years strongly suggested that milk and other dietary proteinderived peptides could play a functional role as specific metabolic regulators of various physiological functions. A clear confirmation of this concept is highly relevant for progression of knowledge in the fields of physiology, nutrition and medical sciences and for an understanding of the complex relationships of the organism with foods. It is also of great innovative interest
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REFERENCES
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