Abstract
Effects of feeding alkaline (0.1 N NaOH) and heat treated (75° C for 3 h) proteins (lactalbumin and soybean protein isolate, SPI) on growth, and protein and mineral status of rats have been determined. The untreated and alkaline/heat treated lactalbumin contained 0.10 and 4.42 g lysinoalanine (LAL)/100 g protein, respectively. Similarly, the un-treated and treated SPI contained 0.03 and 1.94 g LAL/100 g protein, respectively. The formation of LAL in the treated proteins was accompanied with a loss of cystine (73–77%), threonine (35–45%), serine (18–30%) and lysine (19–20%). The alkaline/heat treatments caused significant (P < 0.05) reductions in protein digestibility of lactalbumin (99 vs. 73%) and SPI (96 vs. 68%). The processing treatments also caused a drastic negative effect on protein quality, as measured by rat growth methods such as relative protein efficiency ratio (RPER) and relative net protein ratio (RNPR). The RPER and RNPR values of untreated lactalbumin and SPI were 89–91 and 56–64%, respectively. But the RPER and RNPR values of the treated lactalbumin and SPI were 0%. The mineral status of rats was also compromised by feeding alkaline/heat treated proteins. Liver iron levels in male rats (165–180 µg/g dry weight) and female rats (306–321 µg/g dry weight) fed the treated proteins were about half the levels in male rats (229–257 µg/g dry weight) and female rats (578–697 µg/g dry weight) fed the untreated proteins. The kidney iron contents of rats fed the treated proteins were also lower than that of rats fed the untreated proteins. Liver copper levels of male and female rats fed the treated proteins were up to three fold higher than those found in rats fed the untreated proteins. The data suggested that LAL, an unnatural amino acid derivative formed during processing of foods, may produce adverse effects on growth, protein digestibility, protein quality and mineral bioavailability and utilization. The antinutritional effects of LAL may be more pronounced in sole-source foods such as infant formulas and formulated liquid diets which have been reported to contain significant amounts (up to 2400 ppm of LAL in the protein) of LAL.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Association of Official Analytical Chemists. Official methods of Analysis, 15th Ed., AOAC, Arlington, VA., 1990.
Baker, D.H. Utilization of isomers and analogs of amino acids and other sulfur-containing compounds. Prog. Food Nut. Sci. 1986, 10, 133.
Codex Alimentarius Commission. Working group’s report, on Lysinoalanine Toxicity, to the second session of Codex Committee on vegetable Proteins (CCVP), FAO, Rome, Italy & WHO, Geneva, Switzerland. 1982.
DeGroot, A.P.; Slump, P.; Feron, W.J.; Van Beek, L. Feeding of alkali-treated proteins: feeding studies with free and protein-bound lysinoalanine in rats and other animals. J. Nutr. 1976, 106, 1527–15
Friedman, M. Formation, nutritional value and safety of D-amino acids. In Nutritional and Toxicological Consequences of Food Processing, Friedman, M. Ed.; Plenum Press: New York, N.Y. 1991, pp 447–481
Friedman, M.; Gumbmann, M.R. The utilization and safety of isomeric sulfur-containing amino acids in mice. J. Nutr. 1984, 144, 2301.
Friedman, M.; Gumbmann, M.R.; Masters, RM. Protein-alkali reactions: chemistry, toxicology, and nutritional consequences. In Nutritional and Toxicological Aspects of Food Safety J. Friedman, M., Ed.; Plenum Press: New York, N.Y. 1984; pp 367–412.
Friedman, M.; Zahnley, J.C.; Masters, P.M. Relationship between in vitro digestibility of casein and its content of lysinoalanine and D-amino acids. J. Food Sci. 1981, 46, 127–131.
Gould, D.H.; MacGregor J.T. Biological effects of alkali-treated protein and lysinoalanine: an overview. In Protein Crosslinking: Nutritional and Medical Consequences; Friedman, M., Ed; Plenum Press: New York, N.Y. 1977; pp 29–48.
Hayashi, R. Lysinoalanine as a metal chelator. J. Biol. Chem. 1982, 257, 13896–13898.
International Life Sciences Institute. Processed protein foods and lysinoalanine. Nutr. Rev. 1976, 34(4), 120–122.
International Life Sciences Institute. Mechanism of toxicity of lysinoalanine. Nutr. Rev. 1989, 47(11), 362–364.
Karayiannis, N.; MacGregor, J.T.; Bjeldanes, L.F. Biological effects of alkali-treated soy protein and lactalbumin in the rat and mouse. Food Cosmet. Toxicol. 1979, 17, 591–604.
Kawamura, Y; Hayashi, R. Lysinoalanine-degrading enzymes of various animal kidneys. Agric. Biol. Chem. 1987, 51, 2289–2290.
L’Abbé, M.R.; Fischer, P.F.W. The effects of dietary zinc on the activity of copper-requiring metalloenzymes in the rat. J. Nutr. 1984, 114, 823–828.
L’Abbé, M.R.; Sarwar, G.; Trick, K.; Botting, H.G.; Ma, C.Y Dietary lysinoalanine formed during processing of proteins exerts adverse effects on mineral status of rats. Lancet 1998 (submitted for publication).
Paquet, A.; Thresher, W.C.; Swaisgood, H.E. Further studies on in vitro digestibility of some epimeric tripeptides. Nutr. Res. 1987, 7, 581.
Paquet, A.; Thresher, W.C.; Swaisgood, H.E.; Catignani, G.L. Synthesis and digestibility determinations of some epimeric tripeptides occurring in dietary proteins. Nutr. Res. 1985, 5, 893–904.
Pearce, K.N.; Friedman, M. The binding of copper (II) and other metals by lysinoalanine and related compounds and its significance for food safety. J. Agric. Food Chem. 1988, 36, 707–717.
Reeves, P.G.; Nielsen, F.H.; Fehey, G.C., Jr. AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J. Nutr. 1993, 123, 1939–1951.
Robbins, K.R.; Baker, D.H.; Finley, J.W. Studies on the utilization of lysinoalanine and lanthionine. J. Nutr. 1980, 110, 907–915.
Sarwar, G. The protein digestibility-corrected amino acid score method overestimates quality of proteins containing antinutritional factors and of poorly digestible proteins supplemented with limiting amino acids in rats. J. Nutr. 1997, 127, 758–764.
Sarwar, G.; Botting, H.G.; Peace, R. W. Complete amino acid analysis in hydrolysates of foods and feeds by liquid chromatography of precolumn phenylisothiocyanate derivatives. J. Assoc.Off. Anal. Chem. 1988, 71, 1172–1175.
Sarwar, G.; Paquet, A.; Peace, R.W. Bioavailability of methionine in some tripeptides occurring in dietary proteins as determined by rat growth. Nutr. Res. 1985, 5. 905–912.
Slump, P. Lysinoalanine in alkali treated proteins and factors influencing its biological activity. Annales de la Nutr. et de l’Alimentation. 1978, 32, 271–279.
Sternberg, M.; Kim C.Y.; Schwende, F.J. Lysinoalanine: presence in foods and food ingredients. Science 1975, 190, 992–994.
Struthers, B.J.; Dahlgren, R.R.; Hopkins, D.T.; Raymond, M.L. Lysinoalanine: biological effects and significance. In Soy Protein and Human Nutrition; Wilcke, H.L.; Hopkins, D.T.; Waggle, D.H., Ed; Academic Press, New York, N.Y. 1979; pp 235–260.
Woodard, J.C. Renal toxicity of N e-DL (2-amino-2-carboxyethyl)-L-lysine, lysinoalanine. Vet. Path. 1975, 12, 65–66.
Wood-Rethwill, J.C; Warthesen, J.J. Lysinoalanine determination in proteins using high-pressure liquid chromatography. J. Food Sci. 1980, 45, 1637–1640.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Springer Science+Business Media New York
About this chapter
Cite this chapter
Sarwar, G., L’Abbé, M.R., Trick, K., Botting, H.G., Ma, C.Y. (1999). Influence of Feeding Alkaline/Heat Processed Proteins on Growth and Protein and Mineral Status of Rats. In: Jackson, L.S., Knize, M.G., Morgan, J.N. (eds) Impact of Processing on Food Safety. Advances in Experimental Medicine and Biology, vol 459. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4853-9_11
Download citation
DOI: https://doi.org/10.1007/978-1-4615-4853-9_11
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7201-1
Online ISBN: 978-1-4615-4853-9
eBook Packages: Springer Book Archive