In vivo (rat) and in vitro (caco-2 cells) absorption of amino acids from legume protein isolates as compared to lactalbumin or casein

Archives of Animal Nutrition

Volumn 63, Issue 5, 2009, Pages 413-426

  Rubio, Luis A ^a   Clemente, Alfonso ^a  

^a CSIC   (Spain)

Author keywords

Absorption; Amino acids; Cicer arietinum; In vitro; Lupinus angustifolius; Protein isolates; Rats

Indexed keywords

ANIMALIA; CICER ARIETINUM; LUPINUS ANGUSTIFOLIUS; RATTUS;

AMINO ACID; CASEIN; LACTALBUMIN; PROTEIN INTAKE;

ANALYSIS; ANIMAL; ANIMAL FOOD; CACO-2 CELL LINE; CHEMISTRY; CICER; DIET; HUMAN; KINETICS; LUPIN; MALE; METABOLISM; PROTEIN INTAKE; RAT; VETERINARY; WISTAR RAT;

AMINO ACIDS; ANIMAL FEED; ANIMALS; CACO-2 CELLS; CASEINS; CICER; DIET; DIETARY PROTEINS; HUMANS; KINETICS; LACTALBUMIN; LUPINUS; MALE; RATS; RATS, WISTAR;

EID: 70350312508     PISSN: 1745039X     EISSN: 14772817     Source Type: Journal    
DOI: 10.1080/17450390903169237     Document Type: Article

References (37)

1. Aubry M, Boucrot P. 1986. Etude comparee de la digestion des viciline et lectine radiomarquees de Pisum sativum chez le rat. Ann Nutr Metab. 30:175-182.
2. Backwell FRC, Hipolito-Reis M, Wilson D, Bruce LA, Buchan W, MacRae JC. 1997. Quantification of circulating peptides and assessment of peptide uptake across the gastrointestinal tract of sheep. J Anim Sci. 75:3315-3322.
3. van Barneveld RJ. 1999. Understanding the nutritional chemistry of lupin (Lupinus spp.) seed to improve livestock production efficiency. Nutr Res Rev. 12:203-230.
4. Batterham ES, Andersen LM, Burnham BV, Taylor GA. 1986a. Effect of heat on the antinutritional value of lupin (Lupinus angustifolius)-seed meal for growing pigs. Brit J Nutr. 55:169-177.
5. Batterham ES, Andersen LM, Lowe RF, Darnell RE. 1986b. Nutritional value of lupin (Lupinus albus)-seed meal for growing pigs: Availability of lysine, effect of autoclaving and net energy content. Brit J Nutr. 56:645-659.
6. Benevenga NJ, Gahl MJ, Blemings KP. 1993. Role of protein synthesis in amino acid catabolism. J Nutr. 123:332-336.
7. Bloch KJ, Wright JA, Bishara SM, Bloch MB. 1988. Uptake of polypeptide fragments of proteins by rat intestine in vitro and in vivo. Gastroenterology. 95:1272-1278.
8. Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrere B. 1997. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Nat Acad Sci USA. 94:14930-14936.
9. Caligari S, Chiesa G, Camisassi D, Johnson SK, Gilio D, Marchesi M, Parollini C, Rubio LA, Sirtori CR. 2006. Lupin (Lupinus albus) protein isolate has adequate nutritional value and reduces large intestinal weight in rats after restricted and ad libitum feeding. Ann Nutr Metab. 50:528-537.
10. Clemente A, Vioque J, Sanchez-Vioque R, Pedroche J, Bautista J, Millan F. 1999. Protein quality of chickpea protein hydrlysates. Food Chem. 67:269-274.
11. Cohen SA, Meys M, Tarvin TL. 1989. The Pico Tag Method. A manual of advanced techniques for amino acid analysis. Bedford (MA): Millipore Corporation.
12. D'Almeida MS, Gaudin C, Lebrec D. 1995. Validation of 1- and 2-mm transit-time ultrasound flow probes on mesenteric artery and aorta of rats. Am J Physiol. 268:H1368-1372.
13. van Dael P, Kastenmayer P, Clough J, Jarret A-R, Barclay DV, Maire J-C. 2005. Substitution of casein by b-casein or of whey protein isolate by a-lactalbumin does not affect mineral balance in growing rats. J Nutr. 135:1438-1443.
14. DeSesso JM, Jacobson CF. 2001. Anatomical and physiological parameters affecting gastrointestinal absorption in humans and rats. Food Chem Toxicol. 39:209-228.
15. Galibois I, Simoes Nunes C, Rerat A, Savoie L. 1989. Net appearance of amino acids in portal blood during the ingestion of casein or rapeseed proteins in the pig. Can J Physiol Pharmaco. 67:1409-1417.
16. Glahn RP, Wien EM, van Campen DR, Miller DD. 1996. Caco-2 cell iron uptake from meat and casein digests parallels in vivo studies: Use of a novel in vitro method for rapid estimation of iron bioavailability. J Nutr. 126:332-339.
17. Goena M, Santidrian S, Cuevillas F, Larralde J. 1988. Muscle and liver protein synthesis and degradation in growing rats fed a raw field bean (Vicia faba L.) diet. Rev Esp Fisiol. 44:345-352.
18. Lquari H, Vioque J, Pedroche J, Millan F. 2002. Lupinus angustifolius protein isolates: Chemical composition, functional properties and protein characterization. Food Chem. 76:349-356.
19. Macierzanka A, Sancho AI, Mills ENC, Rigby NM, Mackie AR. 2009. Emulsification alters simulated gastrointestinal proteolysis of b-casein and b-lactoglobulin. Soft Matter. 5:538-550.
20. Montoya CA, Leterme P, Beebe S, Souffrant WB, Molle D, Lalles JP. 2008a. Phaseolin type and heat treatment influence the biochemistry of protein digestion in the rat intestine. Brit J Nutr. 99:531.
21. Montoya CA, Gomez AS, Lalles JP, Souffrant WB, Beebe S, Leterme P. 2008b. In vitro and in vivo protein hydrolysis of beans (Phaseolus vulgaris) genetically modified to express different phaseolin types. Food Chem. 106:1225-1233.
22. Moreno FJ, Rubio LA, Olano A, Clemente A. 2006. Non-degradative transcellular transport of 2S albumin allergens, Ber e 1 and Ses i 1, across human intestinal epithelial Caco-2 cell monolayers. J Agric Food Chem. 54:8631-8639.
23. Muzquiz M, Hill GD, Cuadrado C, Pedrosa MM, Burbano C. 2004. Recent advances of research in antinutritional factors in legume seeds and oilseeds. The Netherlands: Wageningen Academic Publishers.
24. National Research Council (NRC). 1995. Nutrients requirements of laboratory animals. Washington (DC): National Academy Press.
25. Prior RL. 1993. Time after feeding and dietary arginine deficiency alter splanchnic, and hepatic amino acid flux in rats. J Nutr. 123:1538-1553.
26. Remesy C, Demigne C. 1983. Changes in availability of glucogenic, and ketogenic substrates, and liver utilization in fed or starved rats. Ann Nutr Metab. 27:57-70.
27. Rerat A, Simoes Nunes C, Mendy P, Roger L. 1987. Absorption kinetics of amino acids from amino acid mixtures of the same composition perfused into the small intestine in the free form or as enzymic milk protein hydrolysates in the conscious pig. Proc Nutr Soc. 46:104a.
28. Rubio LA, Grant G, Bardocz S, Dewey P, Pusztai A. 1991. Nutritional response of growing rats to faba beans (Vicia faba), and faba bean fractions. Brit J Nutr. 66:533-542.
29. Rubio LA, Grant G, Caballe C, Martinez-Aragon A, Pusztai A. 1994. High in vivo (rat) digestibility of faba bean (Vicia faba), lupin (Lupinus angustifolius), and soybean (Glycine max) globulins. J Sci Food Agric. 66:289-292.
30. Rubio LA, Grant G, Scislowsky P, Brown D, Annand M, Pusztai A. 1995. The utilization of lupin (Lupinus angustifolius) and faba bean globulins by rats is poorer than that of soybean globulins or lactalbumin but the nutritional value of lupin seed meal is lower only than that of lactalbumin. J Nutr. 125:2145-2155.
31. Rubio LA, Grant G, Daguid T, Brown D, Bardocz S, Pusztai A. 1998. The nutritional utilization by rats of chickpea (Cicer arietinum) meal, and its isolated globulin proteins is poorer than that of defatted soybean or lactalbumin. J Nutr. 128:1042-1047.
32. Rubio LA, Muzquiz M, Burbano C, Cuadrado C, Pedrosa MM. 2002. High apparent ileal digestibility of amino acids in raw or germinated faba bean- (Vicia faba) or chickpea- (Cicer arietinum) based diets for rats. J Sci Food Agric. 72:1710-1717.
33. Rubio LA, Seiquer I. 2002. Transport of amino acids from in vitro digested legume proteins or casein in caco-2 cell cultures. J Agric Food Chem. 50:5202-5206.
34. Sanchez-Vioque R, Clemente A, Vioque J, Bautista J, Millan F. 1999. Protein isolates from chickpea (Cicer arietinum L.): Chemical composition, functional properties and protein characterization. Food Chem. 64:237-243.
35. Seal CJ, Parker DS. 1991. Isolation and characterization of circulating low molecular weight peptides in steer, sheep and rat portal and peripheral blood. Comp Biochem Physiol. 99B:679-685.
36. Webb KE. 1990. Intestinal absorption of protein hydrolysis products: A review. J Anim Sci. 68:3011-3022.
37. Wu G. 1998. Intestinal mucosal amino acid catabolism. J Nutr. 128:1249-1252.