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NUTRITION AND SAFETY
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Figure 6.1.13 Potentiometric titration curves for LAL in the absence (H-curve) and presence of various divalent metal ions. The plots show the following relative af nities of metal ions for LAL: Cu > Ni > Hg > Fe. Adapted from Reference 17.
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exerts some of its biological effects through chelation to copper and other metal ions in vivo. 6.1.6.6 Primate Studies
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A short-term feeding study of alkali-treated soy protein diets to Rhesus monkeys revealed no apparent histological changes in kidney tissue of the test animals (15). To obtain additional information on this aspect, we evaluated nutritional and histopathological consequences of feeding toasted and alkalitreated soy ours to baboons (6). The untreated commercial toasted protein isolate contained 5.74 g lysine/16 g N. The corresponding value for LAL was 0.37. The alkali-treated proteins contained 4.96 g lysine/16 g N. The corresponding value for LAL was 1.61. Figure 6.1.10 shows the growth curves for seven preadolescent male baboons each fed soy control and alkali-treated soy diets. There was no difference in growth rates over the 150-day period, since the slopes of the growth curves are not signi cantly different from each other. However, in absolute terms, weight gain of the baboons fed the treated soy diet (containing 370 mg of LAL/100 g air-dry diet = 3700 ppm) was about 20% lower than the gain observed with the control soy diet (containing 80 mg of LAL/100 g = 80 ppm of air-dry diet). The decreased weight gains may be due to the decreased digestibility and utilization of the treated soy protein compared with the control (Table 6.1.6). Histological evaluation of the pancreas and kidney tissues from baboons fed toasted and alkali-treated soy diets indicated that as far as the difference
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DIETARY SIGNIFICANCE OF PROCESSING-INDUCED LYSINOALANINE
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due to soy processing treatment was concerned, this was essentially a negative study. The results of the baboon study show that although feeding alkalitreated soy protein containing a moderate amount of LAL to baboons for about 6 months adversely affected body mass, it apparently did not in uence pancreatic and kidney histology. Short-term feeding of LAL and Maillard product-containing formulas to healthy preterm babies did not appear to induce tubular kidney damage, as determined by urinary excretion of four kidney-derived enzymes (165). The authors concluded that the 10-day feeding study period may have been too short to cause signi cant changes in renal function.
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CONCLUSIONS AND RESEARCH NEEDS
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Although the safety of LAL and related compounds for humans remains unresolved, it is reassuring that the effect on kidneys in rodents was not apparent with primates. Resolution of the safety issue will depend on a better understanding of the fundamental mechanisms of action of these unusual amino acids at the cellular concentration. Mechanistic studies on the formation and biological action and fate of LAL in vivo could perhaps bene t from a proposed method for the synthesis of deuterium- and tritiumlabeled free and protein-bound LAL (166). Such labeling should help ascertain the location of LAL in proteins and its metabolism in animals and humans. Understanding food-processing conditions that govern LAL formation makes it possible to minimize or maximize the LAL content of foods and feeds depending on dietary needs. It may also facilitate the development of new LAL-containing, antimicrobial peptides effective against human pathogens as well as the inhibition of cross-linked amino acid (lysinoalanine, histidinoalanine, and lanthionine) formation in vivo to retard the aging process. Because of its strong af nity for metal ions, free and protein-bound dietary LAL may be of value in the treatment of human diseases associated with retention of excess copper, iron, and mercury. Because baboons gained less weight on an alkali-treated soy protein diet, it may be worthwhile to nd out whether consumption by humans of alkalitreated cereal and legume proteins may help overcome obesity. There is also the need to nd out whether phenylethylamine, histamine, and tyramine in biogenic amine-rich foods react with dehydroalanine moieties during food processing and storage to form phenylethylaminoalanine and histaminoalanine, respectively. Whether lysine or lysinoalanine amino groups react with acrylamide during processing of foods also merits study (167). Research is continuing in this important area of food chemistry, food and microbial safety, nutrition, and medicine (168 172).
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