Advertisement

Enhancement of Amino Acid Availability in Corn Grain

  • L. Kriz AlanEmail author
Part of the Biotechnology in Agriculture and Forestry book series (AGRICULTURE, volume 63)

As modern corn hybrids were bred for higher yields, the composition of the grain has inadvertently trended to higher starch content at the expense of protein (Scott et al. 2006). Moreover since corn grain protein is deficient in certain nutritionally essential amino acids, this reduction in grain protein level has further reduced the nutritional quality of the grain. One approach to address this problem is to increase the nutritional quality of corn grain protein, particularly by enhancing the content of essential amino acids, such as lysine and tryptophan.

The most limiting amino acid in corn grain, with respect to the dietary needs of monogastric animals, is lysine. Therefore, enhancement of lysine content is a primary target for improving grain quality. The poor nutritional quality of corn protein is mostly caused by the amino acid composition of endosperm proteins. Corn protein has a lysine content of 2.7%, which is well below the recommendation by FAO (FAO/WHO/UNU 1985) for human nutrition. Although the germ protein has an adequate lysine content (5.4%) in whole grain, this is diluted by the much more abundant endosperm proteins, which have an average lysine content of only about 1.9%. This is because 60–70% of endosperm protein consists of zeins, which contain few or no lysine residues (Coleman and Larkins 1999). Similarly, the absence of tryptophan residues in zein proteins is the reason for the low tryptophan content of corn protein. Therefore, modification of the grain protein profile through approaches such as zein reduction and expression of lysine-rich proteins could significantly improve the balance of amino acids. Alternatively, the lysine content of the grain could be increased by elevating the level of free lysine in the kernel.

Keywords

Lysine Content Quality Protein Maize Maize Endosperm Endosperm Protein Amino Acid Availability 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Arruda P, Kemper EL, Papes F, Leite A (2000) Regulation of lysine catabolism in higher plants. Trends Plant Sci 5:324–330PubMedCrossRefGoogle Scholar
  2. Azevedo RA, Damerval C, Lea PJ, Landry J, Bellato CM, Meinhardt LW, Le Guilluox M, Delhaye S, Toro AA, Gaziola SA, Varisi VA, Gratao PL (2004) Endosperm protein synthesis and lysine metabolism in distinct opaque maize seed mutants. Funct Plant Biol 31:339–348CrossRefGoogle Scholar
  3. Azevedo RA, Lancien M, Lea PJ (2006) The aspartic acid metabolic pathway, an exciting and essential pathway in plants. Amino Acids 30:143–162PubMedCrossRefGoogle Scholar
  4. Belanger FC, Kriz AL (1991) Molecular basis for allelic polymorphism of the maize Globulin-1 gene. Genetics 129:863–872PubMedGoogle Scholar
  5. Bicar EH, Woodman-Clikeman W, Sangtong V, Peterson JM, Yang SS, Lee M, Scott MP (2008) Transgenic maize endosperm containing a milk protein has improved amino acid balance. Transgenic Res 17:59–71PubMedCrossRefGoogle Scholar
  6. Burgoon KG, Hansen JA, Knabe DA, Bockholt AJ (1992) Nutritional value of quality protein maize for starter and finisher swine. J Anim Sci 70:811–817PubMedGoogle Scholar
  7. Coleman CE, Larkins BA (1999) The prolamins of maize. In: Shewry PR, Casey R (eds) Seed proteins. Kluwer, Dordrecht, pp 109–139Google Scholar
  8. Dierks-Ventling C (1981) Storage proteins in Zea mays (L.): interrelationship of albumins, globulins and zeins in the opaque-2 mutation. Eur J Biochem 120:177–182PubMedCrossRefGoogle Scholar
  9. Dierks-Ventling C (1983) Lysine biosynthesis and utilization during seed development of normal and opaque-2 Zea mays L. Planta 157:233–238CrossRefGoogle Scholar
  10. Falco SC, Guida T, Locke M, Mauvais J, Sanders C, Ward RT, Webber P (1995) Transgenic canola and soybean seeds with increased lysine. Biotechnology 13:577–582PubMedCrossRefGoogle Scholar
  11. FAO (1992) Maize in human nutrition. FAO, RomeGoogle Scholar
  12. FAO/WHO/UNU (1985) Energy and protein requirements. Report of a joint FAO/WHO/UNU expert consultation. WHO, GenevaGoogle Scholar
  13. Galili G (2004) New insights into the regulation and functional significance of lysine metabolism in plants. Ann Rev Plant Physiol Plant Mol Biol 53:27–43Google Scholar
  14. Geetha KB, Lending CR, Lopes MA, Wallace JC, Larkins BA (1991) Opaque-2 modifiers increase γ-zein synthesis and alter its spatial distribution in maize endosperm. Plant Cell 3: 1207–1219PubMedCrossRefGoogle Scholar
  15. Gentinetta E, Maggiore T, Salamini F, Lorenzoni C, Piole F, Soave C (1975) Protein studies in 46 opaque-2 strains with modified endosperm texture. Maydica 20:145–164Google Scholar
  16. Gibbon BC, Larkins BA (2005) Molecular genetic approaches to developing quality protein maize. Trends Genet 21:227–233PubMedCrossRefGoogle Scholar
  17. Gibbon BC, Wang X, Larkins BA (2003) Altered starch structure is associated with endosperm modification in Quality Protein Maize. Proc Natl Acad Sci USA 100:15329–15334PubMedCrossRefGoogle Scholar
  18. Gupta D, Kovacs I, Gaspar L (1975) Protein quality traits and their relationship with yield and yield components of opaque-2 and analogous normal maize hybrids and inbred lines. Theor Appl Genet 45:341–348CrossRefGoogle Scholar
  19. Hadjinov MI, Zima KI, Normov AA (1972) Changes in weight, protein and lysine content in opaque-2 kernels of corn during backcrossing. Maize Genet Coop Newsl 46:101–104Google Scholar
  20. Hamada S, Ishiyama K, Sakulsingharoj C, Choi SB Wu Y, Wang C, Singh S, Kawai N, Messing J, Okita TW (2003) Dual regulated RNA transport pathways to the cortical region in developing rice endosperm. Plant Cell 15:2265–2272PubMedCrossRefGoogle Scholar
  21. Hamaker BR, Kirleis AW, Butler LG, Axtell JD, Mertz ET (1987) Improving the in vitro digestibility of sorghum with reducing agents. Proc Natl Acad Sci USA 84:626–628PubMedCrossRefGoogle Scholar
  22. Harper AE, Benton DA, Elvehjem CA (1955) L-leucine, an isoleucine antagonist in the rat. Arch Biochem Biophys 57:1–12CrossRefGoogle Scholar
  23. Harper AE, Benevenga NJ, Wohlhueter RM (1970) Effects of ingestion of disproportionate amounts of amino acids. Physiol Rev 50:428–558PubMedGoogle Scholar
  24. Houmard NM, Mainville, JL, Bonin CP, Huang S, Luethy MH, Malvar TM (2007) High lysine corn generated by endosperm specific suppression of lysine catabolism using RNAi. Plant Biotechnol J 5(5):605–614PubMedCrossRefGoogle Scholar
  25. Huang S, Adams WR, Zhou Q, Malloy KP, Voyles DA, Anthony J, Kriz AL, Luethy MH (2004) Improving nutritional quality of maize proteins by expressing sense and antisense zein genes. J Agric Food Chem 52(7): 1958–1964PubMedCrossRefGoogle Scholar
  26. Huang S, Kruger DE, Frizzi A, D'Ordine RL, Florida CA, Adams WR, Brown WE, Luethy MH (2005) High-lysine corn produced by the combination of enhanced lysine biosynthesis and reduced zein accumulation. Plant Biotechnol J 3:555–569PubMedCrossRefGoogle Scholar
  27. Huang S, Frizzi A, Florida CA, Kruger DE, Luethy MH (2006) High lysine and high tryptophan transgenic maize resulting from the reduction of both 19- and 22-kD α-zeins. Plant Mol Biol 61:525–535PubMedCrossRefGoogle Scholar
  28. Ji Q, Vincken JP, Luc CJM, Suurs LCJM, Visser RGF (2003) Microbial starch-binding domains as a tool for targeting proteins to granules during starch biosynthesis. Plant Mol Biol 51:789–801PubMedCrossRefGoogle Scholar
  29. Johnson LA, Hardy CL, Baumel CP, Yu T-H, Sell JL (2001) Identifying valuable corn quality traits for livestock feed. Iowa State University, Ames Kemper EL, Cord-Neto G, Capella AN, Goncalves-Butruile M, Azevedo RA, Arruda P (1998) Structure and regulation of the bifunctional enzyme lysine-oxoglutarate reductase-saccharopine dehydrogenase in maize. Eur J Biochem 253:720–729Google Scholar
  30. Kim CS, Woo Y, Clore AM, Burnett RJ, Carneior NP, Larkins BA (2002) Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm. Plant Cell 14:655–672PubMedCrossRefGoogle Scholar
  31. Kriz AL (1989) Characterization of embryo proteins encoded by the maize Glb genes. Biochem Genet 27:239–251PubMedCrossRefGoogle Scholar
  32. Kriz AL, Wallace NH (1991) Characterization of the maize Globulin-2 gene and analysis of two null alleles. Biochem Genet 29:241–254PubMedCrossRefGoogle Scholar
  33. Landry J, Moreaux T (1982) Distribution and amino acid composition of protein fractions in opaque-2 maize grains. Biochemistry 21:1865–1869Google Scholar
  34. Landry J, Delhaye S, Damerval C (2002) Effect of the opaque-2 gene on accumulation of protein fractions in maize endosperm. Maydica 47:59–66Google Scholar
  35. Lopes MA, Larkins BA (1991) Gamma-zein content is related to endosperm modification in quality protein maize. Crop Sci 31:1655–1662Google Scholar
  36. Lopes MA, Takasaki K, Bostwick DE, Helentjaris T, Larkins BA (1995) Identification of two opaque2 modifier loci in Quality Protein Maize. Mol Gen Genet 247:603–613PubMedCrossRefGoogle Scholar
  37. Lucas DM, Glenn KC, Bu J-Y (2004) Petition for determination of nonregulated status for lysine maize LY038. http://www.aphis.usda.gov/brs/aphisdocs/04 22901p.pdf
  38. May RC, Piepenbrock N, Kelly RA, Mitch WE (1991) Leucine-induced amino acid antagonism in rats: muscle valine metabolism and growth impairment. J Nutr 121:293–301PubMedGoogle Scholar
  39. Mazur B, Krebbers E, Tingey S (1999) Gene discovery and product development for grain quality traits. Science 285:372–375PubMedCrossRefGoogle Scholar
  40. Mertz ET, Bates LS, Nelson OE (1964) Mutant gene that changes protein composition and increases lysine content of maize endosperm. Science 145:279–280PubMedCrossRefGoogle Scholar
  41. Misra PS, Jambunathan R, Mertz ET, Glover DV, Barbosa HM, McWhirter KS (1972) Endosperm synthesis in maize mutants with increased lysine content. Science 176:1425–1427PubMedCrossRefGoogle Scholar
  42. Nelson OE (1969) Genetic modification of protein quality in plants. Adv Agron 21:171–174CrossRefGoogle Scholar
  43. Nelson OE, Mertz ET, Bates LS (1965) Second mutant gene affecting the amino acid pattern of maize endosperm proteins. Science 150:1469–1470PubMedCrossRefGoogle Scholar
  44. Osborne TB (1908) Our present knowledge of plant proteins. Science 28:417–427PubMedCrossRefGoogle Scholar
  45. Paez AV, Helm JL, Zuber MS (1969) Lysine content of opaque-2 maize kernels having different phenotypes. Crop Sci 9:251–252Google Scholar
  46. Prasanna BM, Vasal SK, Kassahun B, Singh NN (2001) Quality protein maize. Curr Sci 81:1308–1319Google Scholar
  47. Puckett JL, Kriz AL (1991) Globulin gene expression in opaque-2 and floury-2 mutant maize embryos. Maydica 36:161–167Google Scholar
  48. Scott MP, Edwards JW, Bell CP, Schussler JR, Smith JS (2006) Grain composition and amino acid content in maize cultivars representing 80 years of commercial maize varieties. Maydica 51:417–423Google Scholar
  49. Segal G, Song R, Messing J (2003) A new opaque variant of maize by a single dominant RNA-interference-inducing transgene. Genetics 165:387–397PubMedGoogle Scholar
  50. Sodek L, Wilson CM (1971) Amino acid composition of proteins isolated from normal, opaque-2, and floury-2 corn endosperms by a modified Osborne procedure. J Agric Food Chem 19:1144–1150CrossRefGoogle Scholar
  51. Stepansky A, Less H, Angelovici R, Aharon R, Zhu X, Galili G (2006) Lysine catabolism, an effective versatile regulator of lysine level in plants. Amino Acids 30:121–125PubMedCrossRefGoogle Scholar
  52. Sullivan JS, Knabe DA, Bockholt AJ, Gregg EJ (1989) Nutritional value of quality protein maize and food corn for starter and growth pigs. J Anim Sci 67:1285–1292PubMedGoogle Scholar
  53. Torrent M, Alvarez I, Geli MI, Dalcol I, Ludevid D (1997) Lysine-rich modified γ-zeins accumulate in protein bodies of transiently transformed maize endosperms. Plant Mol Biol 34:139–149PubMedCrossRefGoogle Scholar
  54. Tsai CY, Larkins BA, Glover DV (1978) Interaction of the opaque-2 gene with starch-forming mutant genes on the synthesis of zein in maize endosperm. Biochem Genet 16:883–896PubMedCrossRefGoogle Scholar
  55. Wall JS, Paulis JW (1978) Corn and sorghum grain proteins. Adv Cereal Sci Technol 2:135–219Google Scholar
  56. Wallace JC, Galili G, Kawata EE, Cuellar RE, Shotwell MA, Larkins BA (1988) Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes. Science 240:662–664PubMedCrossRefGoogle Scholar
  57. Wang X, Larkins BA (2001) Genetic analysis of amino acid accumulation in opaque-2 maize endosperm. Plant Physiol 125:1766–1777PubMedCrossRefGoogle Scholar
  58. Wu XR, Kenzior A, Willmot D, Scanlon S, Chen Z, Topin A, He SH, Acevedo A, Folk WR (2007) Altered expression of plant lysyl tRNA synthetase promotes tRNA misacylation and translational recoding of lysine. Plant J 50(4): 627–636. doi: 10.111/j.1365-313X.2007.03076.xPubMedCrossRefGoogle Scholar
  59. Yang SH, Moran DL, Jia HW, Bicar EH, Lee M, Scott MP (2002) Expression of a synthetic porcine α-lactalbumin gene in the kernels of transgenic maize. Transgenic Res 11:11–20PubMedCrossRefGoogle Scholar
  60. Yu J, Peng P, Zhang X, Zhao Q, Zhy D, Sun X, Liu J, Ao G (2004) Seed-specific expression of a lysine rich protein sb401 gene significantly increases both lysine and total protein content in maize seeds. Mol Breed 14:1–7CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, B.V 2009

Authors and Affiliations

  1. 1.BASF Plant Science, LLCUSA

Personalised recommendations