Hostname: page-component-848d4c4894-xfwgj Total loading time: 0 Render date: 2024-06-14T20:46:18.191Z Has data issue: false hasContentIssue false

Minimal processed infant formula vs. conventional shows comparable protein quality and increased postprandial plasma amino acid kinetics in rats

Published online by Cambridge University Press:  23 November 2023

Juliane Calvez*
Affiliation:
Université Paris-Saclay, AgroParisTech, INRAE, UMR PNCA, 91123, Palaiseau, France
Anne Blais
Affiliation:
Université Paris-Saclay, AgroParisTech, INRAE, UMR PNCA, 91123, Palaiseau, France
Amélie Deglaire
Affiliation:
STLO, INRAE, Institut Agro, 35042, Rennes, France
Claire Gaudichon
Affiliation:
Université Paris-Saclay, AgroParisTech, INRAE, UMR PNCA, 91123, Palaiseau, France
François Blachier
Affiliation:
Université Paris-Saclay, AgroParisTech, INRAE, UMR PNCA, 91123, Palaiseau, France
Anne-Marie Davila
Affiliation:
Université Paris-Saclay, AgroParisTech, INRAE, UMR PNCA, 91123, Palaiseau, France
*
*Corresponding author: Juliane Calvez, email juliane.calvez@agroparistech.fr

Abstract

During industrial processing, heat treatments applied to infant formulas may affect protein digestion. Recently, innovative processing routes have been developed to produce minimally heat-processed infant formula. Our objective was to compare the in vivo protein digestion kinetics and protein quality of a minimally processed (T−) and a heat-treated (T+++) infant formula. Sixty-eight male Wistar rats (21 d) were fed with either a diet containing 40 % T− (n 30) or T+++ (n 30), or a milk protein control diet (n 8) during 2 weeks. T− and T+++ rats were then sequentially euthanised 0, 1, 2, 3 or 6 h (n 6/time point) after ingestion of a meal containing their experimental diet. Control rats were euthanised 6 h after ingestion of a protein-free meal to determine nitrogen and amino acid endogenous losses. Nitrogen and amino acid true caecal digestibility was high for both T− and T+++ diets (> 90 %), but a tendency towards higher nitrogen digestibility was observed for the T− diet (96·6 ± 3·1 %) compared with the T+++ diet (91·9 ± 5·4 %, P = 0·0891). This slightly increased digestibility led to a greater increase in total amino acid concentration in plasma after ingestion of the T− diet (P = 0·0010). Comparable protein quality between the two infant formulas was found with a digestible indispensable amino acid score of 0·8. In conclusion, this study showed that minimal processing routes to produce native infant formula do not modify protein quality but tend to enhance its true nitrogen digestibility and increase postprandial plasma amino acid kinetics in rats.

Type
Research Article
Copyright
© The Author(s), 2023. Published by Cambridge University Press on behalf of The Nutrition Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Theurich, MA, Davanzo, R, Busck-Rasmussen, M, et al. (2019) Breastfeeding rates and programs in Europe: a survey of 11 national breastfeeding committees and representatives. J Pediatr Gastroenterol Nutr 68, 400407.CrossRefGoogle ScholarPubMed
Martin, CR, Ling, PR & Blackburn, GL (2016) Review of infant feeding: key features of breast milk and infant formula. Nutrients 8, 279.CrossRefGoogle ScholarPubMed
Floris, R, Lambers, T, Alting, A, et al. (2010) 17 - Trends in infant formulas: a dairy perspective. In Improving the Safety and Quality of Milk, pp. 454474 [Griffiths, MW, editor]. Sawston, UK: Woodhead Publishing.CrossRefGoogle Scholar
Brodkorb, A, Croguennec, T, Bouhallab, S, et al. (2016) Heat-induced denaturation, aggregation and gelation of whey proteins. In Advanced Dairy Chemistry: Volume 1B: Proteins: Applied Aspects, pp. 155178 [McSweeney, PLH and O’Mahony, JA, editors]. New York, NY: Springer New York.CrossRefGoogle Scholar
Yu, X, Leconte, N, Mejean, S, et al. (2021) Semi-industrial production of a minimally processed infant formula powder using membrane filtration. J Dairy Sci 104, 52655278.CrossRefGoogle ScholarPubMed
van Lieshout, GAA, Lambers, TT, Bragt, MCE, et al. (2020) How processing may affect milk protein digestion and overall physiological outcomes: a systematic review. Crit Rev Food Sci Nutr 60, 24222445.CrossRefGoogle ScholarPubMed
Dupont, D, Boutrou, R, Menard, O, et al. (2010) Heat treatment of milk during powder manufacture increases casein resistance to simulated infant digestion. Food Digestion 1, 2839.CrossRefGoogle Scholar
Rahaman, T, Vasiljevic, T & Ramchandran, L (2017) Digestibility and antigenicity of beta-lactoglobulin as affected by heat, pH and applied shear. Food Chem 217, 517523.CrossRefGoogle ScholarPubMed
Sánchez-Rivera, L, Ménard, O, Recio, I, et al. (2015) Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder. Food Res Int 77, 132139.CrossRefGoogle Scholar
Halabi, A, Croguennec, T, Bouhallab, S, et al. (2020) Modification of protein structures by altering the whey protein profile and heat treatment affects in vitro static digestion of model infant milk formulas. Food Funct 11, 69336945.CrossRefGoogle ScholarPubMed
Barbe, F, Menard, O, Le Gouar, Y, et al. (2013) The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids. Food Chem 136, 12031212.CrossRefGoogle ScholarPubMed
Lacroix, M, Bon, C, Bos, C, et al. (2008) Ultra high temperature treatment, but not pasteurization, affects the postprandial kinetics of milk proteins in humans. J Nutr 138, 23422347.CrossRefGoogle Scholar
Efigênia, M, Povoa, B & Moraes-Santos, T (1997) Effect of heat treatment on the nutritional quality of milk proteins. Int Dairy J 7, 609612.CrossRefGoogle Scholar
Lacroix, M, Leonil, J, Bos, C, et al. (2006) Heat markers and quality indexes of industrially heat-treated [15N] milk protein measured in rats. J Agric Food Chem 54, 15081517.CrossRefGoogle ScholarPubMed
Gilani, GS & Sepehr, E (2003) Protein digestibility and quality in products containing antinutritional factors are adversely affected by old age in rats. J Nutr 133, 220225.CrossRefGoogle ScholarPubMed
Rutherfurd, SM & Moughan, PJ (2008) Effect of elevated temperature storage on the digestible reactive lysine content of unhydrolyzed- and hydrolyzed-lactose milk-based products. J Dairy Sci 91, 477482.CrossRefGoogle ScholarPubMed
Bavaro, SL, Mamone, G, Picariello, G, et al. (2021) Thermal or membrane processing for infant milk formula: effects on protein digestion and integrity of the intestinal barrier. Food Chem 347, 129019.CrossRefGoogle ScholarPubMed
Halabi, A, Croguennec, T, Ménard, O, et al. (2022) Protein structure in model infant milk formulas impacts their kinetics of hydrolysis under in vitro dynamic digestion. Food Hydrocolloids 126, 107368.CrossRefGoogle Scholar
Reeves, PG, Nielsen, FH & Fahey, GC Jr (1993) AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition writing committee on the reformulation of the AIN-76A rodent diet. J Nutr 123, 19391951.CrossRefGoogle ScholarPubMed
Rutherfurd, SM & Gilani, GS (2009) Amino acid analysis. Comptes rendus hebdomadaires seances l’Academie sciences. Curr Protoc Protein Sci Chapter 11, Unit 11 19.Google Scholar
Guillin, FM, Gaudichon, C, Guerin-Deremaux, L, et al. (2023) Caecal digestibility as an approximation of ileal protein digestibility evaluation in rats. J Nutr Sci 12, e18.CrossRefGoogle ScholarPubMed
FAO (2013) Dietary Protein Quality Evaluation in Human Nutrition. Report of an FAO Expert Consultation. Food and Nutrition Paper n°92. Rome: FAO.Google Scholar
Guillin, FM, Gaudichon, C, Guerin-Deremaux, L, et al. (2021) Multi-criteria assessment of pea protein quality in rats: a comparison between casein, gluten and pea protein alone or supplemented with methionine. Br J Nutr 125, 389397.CrossRefGoogle ScholarPubMed
Rutherfurd, SM, Fanning, AC, Miller, BJ, et al. (2015) Protein digestibility-corrected amino acid scores and digestible indispensable amino acid scores differentially describe protein quality in growing male rats. J Nutr 145, 372379.CrossRefGoogle ScholarPubMed
Ghasemi, A & Zahediasl, S (2012) Normality tests for statistical analysis: a guide for non-statisticians. Int J Endocrinol Metab 10, 486489.CrossRefGoogle Scholar
Gałecki, A & Burzykowski, T (2013) Linear mixed-effects model. In Linear Mixed-Effects Models Using R: A Step-by-Step Approach, pp. 245273 [Casella, G, Finenberg, SE and Olkin, I, editors]. New York, NY: Springer New York.CrossRefGoogle Scholar
Mishra, P, Singh, U, Pandey, CM, et al. (2019) Application of student’s t test, analysis of variance, and covariance. Ann Cardiac Anaesth 22, 407411.CrossRefGoogle ScholarPubMed
Varga, F (1976) Transit time changes with age in the gastrointestinal tract of the rat. Digestion 14, 319324.CrossRefGoogle ScholarPubMed
Buraczewski, S, Porter, JW, Rolls, BA, et al. (1971) The course of digestion of different food proteins in the rat. 2. The effect o feeding carbohydrate with proteins. Br J Nutr 25, 299306.CrossRefGoogle ScholarPubMed
Oberli, M, Douard, V, Beaumont, M, et al. (2018) Lipo-protein emulsion structure in the diet affects protein digestion kinetics, intestinal mucosa parameters and microbiota composition. Mol Nutr Food Res 62, 1700570.CrossRefGoogle ScholarPubMed
Calvez, J, Khodorova, N, Beaubier, S, et al. (2022) Using the dual isotope method to assess cecal amino acid absorption of goat whey protein in rats, a pilot study. Amino Acids 54, 811821.CrossRefGoogle Scholar
Atallah, N, Gaudichon, C, Boulier, A, et al. (2022) Moderate adiposity levels counteract protein metabolism modifications associated with aging in rats. Eur J Nutr 61, 31893200.CrossRefGoogle Scholar
Tessier, R, Khodorova, N, Calvez, J, et al. (2020) 15N and (2)H intrinsic labeling demonstrate that real digestibility in rats of proteins and amino acids from sunflower protein isolate is almost as high as that of goat whey. J Nutr 150, 450457.CrossRefGoogle Scholar
Charton, E, Henry, G, Cahu, A, et al. (2023) Ileal digestibility of nitrogen and amino acids in human milk and an infant formula as determined in neonatal minipiglets. J Nutr 153, 10631074.CrossRefGoogle Scholar
Rutherfurd, SM & Moughan, PJ (1997) Application of a new method for determining digestible reactive lysine to variably heated protein sources. J Agric Food Chem 45, 15821586.CrossRefGoogle Scholar
Cattaneo, S, Stuknyte, M, Masotti, F, et al. (2017) Protein breakdown and release of beta-casomorphins during in vitro gastro-intestinal digestion of sterilised model systems of liquid infant formula. Food Chem 217, 476482.CrossRefGoogle ScholarPubMed
Pinto, MS, Léonil, J, Henry, G, et al. (2014) Heating and glycation of β-lactoglobulin and β-casein: aggregation and in vitro digestion. Food Res Int 55, 7076.CrossRefGoogle Scholar
Rutherfurd, SM & Moughan, PJ (2005) Digestible reactive lysine in selected milk-based products. J Dairy Sci 88, 4048.CrossRefGoogle ScholarPubMed
Maathuis, A, Havenaar, R, He, T, et al. (2017) Protein digestion and quality of goat and cow milk infant formula and human milk under simulated infant conditions. J Pediatr Gastroenterol Nutr 65, 661666.CrossRefGoogle ScholarPubMed
Alegría, A, Barberá, R, Farré, R, et al. (1999) Amino acid contents of infant formulas. J Food Compos and Anal 12, 137146.CrossRefGoogle Scholar
Almeida, CC, Baião, DDS, Leandro, KC, et al. (2021) Protein quality in infant formulas marketed in Brazil: assessments on biodigestibility, essential amino acid content and proteins of biological importance. Nutrients 13, 3933.CrossRefGoogle ScholarPubMed
Welch-Jernigan, RJ, Abrahamse, E, Stoll, B, et al. (2018) Postprandial amino acid kinetics of milk protein mixtures are affected by composition, but not denaturation, in neonatal piglets. Curr Dev Nutr 3, nzy102.CrossRefGoogle Scholar
Moro, G, Minoli, I, Boehm, G, et al. (1999) Postprandial plasma amino acids in preterm infants: influence of the protein source. Acta Paediatr 88, 885889.CrossRefGoogle ScholarPubMed
Lacroix, M, Bos, C, Leonil, J, et al. (2006) Compared with casein or total milk protein, digestion of milk soluble proteins is too rapid to sustain the anabolic postprandial amino acid requirement. Am J Clin Nutr 84, 10701079.CrossRefGoogle ScholarPubMed
Supplementary material: File

Calvez et al. supplementary material

Calvez et al. supplementary material
Download Calvez et al. supplementary material(File)
File 188.9 KB