Skip to main content
SpringerLink
Log in

Leaf protein for food use: potential of Rubisco

  • Chapter
New and Developing Sources of Food Proteins

Abstract

Leaf protein was discovered and characterized in 1773 by Rouelle [1] who was demonstrator at the ‘Jardin du Roi’ in Paris. The historical background of these studies was reviewed by Pirie [2]. His pioneering work since World War II threw light on the fairly good nutritive value of leaf protein concentrate (LPC) which can be obtained quite easily from the leaves of a variety of plant sources [2, 3]. This LPC is usually obtained by heat coagulation of the whole protein in the juice produced by pressing disintegrated leaves.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Rouelle, M. (1773) Observations sur les fécules ou parties vertes des plantes, et sur la matière glutineuse ou végéto-animale. J. Med. Chir. Pharm., 40, 59–67.

    Google Scholar 

  2. Pirie, N. W. (1978) Leaf protein and other aspects of fodder fractionation, Cambridge University Press, Cambridge, UK.

    Google Scholar 

  3. Telek, L. and Graham, H. D. (1983) Leaf Protein Concentrates, AVI Publishing Company, Westport, Connecticut.

    Google Scholar 

  4. Singh, N. and Matai, S. (1985) Proceedings of the seminar on prospects and problems of green vegetation research in India, Indian statistical institute, Calcutta, India, 12–13 December.

    Google Scholar 

  5. Mathan, O. (de) (1990) Large scale commercial operations in Europe, in Proceedings of the Third International Conference on Leaf Protein Research, Chiriotti Editori, Pinerolo, Italy, pp. 36–49.

    Google Scholar 

  6. Kohler, G. O. and Knuckles, B. E. (1977) Edible protein from leaves. Food Technol, 31, 191–5.

    Google Scholar 

  7. Nagy, S., Telek L., Hall, N. T. and Berry, R. E. (1978) Potential food uses for protein from tropical and subtropical plant leaves. J. Agric Food Chem, 26, 1016–28.

    CAS  Google Scholar 

  8. Enochian, R. V., Kohler, G. O., Edwards R. H. et al. (1980) Producing Pro-Xan (leaf protein concentrate) from alfalfa: Economics of an emerging technology, U.S. Department of Agriculture, Agricultural Economic Report No 445.

    Google Scholar 

  9. Costes, C. (1981) Protéines foliares et alimentation. Gauthier-Villars, Paris.

    Google Scholar 

  10. Humphries, C. (1982) Towards leaf protein as a human food, in Developments in Food Proteins 1, (ed B. J. F. Hudson), Applied Science Publishers, pp. 263–88.

    Google Scholar 

  11. Edwards, R. H., Kohler, G. O., Miller, R. E. et al. (1982) Wet fractionation of forage to reduce energy requirements of dehydration, US Department of Energy Report No DE-AI01-78CS40090.

    Google Scholar 

  12. Fiorentini, R. and Galoppini, C. (1983) The proteins from leaves. Qual. Plant Plant Foods Hum. Nutr., 32, 335–50.

    CAS  Google Scholar 

  13. Fantozzi, P. and Sensidoni A. (1983) Protein extraction from tobacco leaves: technological, nutritional and agronomical aspects. Qual. Plant Plant Foods Hum. Nutr., 32, 351–68.

    CAS  Google Scholar 

  14. Douillard, R. (1985) Propriétés biochimiques et physicochimiques des protéines des feuilles, in Protéines Végétales, (ed B. Godon), Technique et Documentation (Lavoisier), pp. 211–44.

    Google Scholar 

  15. Sheen, S. J. (1986) Whole-plant utilization: the potential of soybean. Biomass, 10, 195–206.

    CAS  Google Scholar 

  16. Tomassi, G. (1990) Complementary or parallel utilization of foliar products: nutritional aspects. Ital. J. Food Sci., 3, 145–55.

    Google Scholar 

  17. Fantozzi, P. (1990) What is the future of leaf protein in human nutrition? Ital. J. Food. Sci., 1, 3–8.

    Google Scholar 

  18. Kawashima, N. and Wildman, S. G. (1970) Fraction I protein. Ann Rev. Plant Physiol. 21, 325–58.

    CAS  Google Scholar 

  19. Jensen, R. G. and Bahr, J. T. (1977) Ribulose 1,5-bisphosphate carboxylase-oxygenase. Ann. Rev. Plant Physiol., 28, 379–400.

    CAS  Google Scholar 

  20. Lorimer, G. H. (1981) The carboxylation and oxygenation of ribulose 1,5-biphosphate: the primary events in photosynthesis and photo-respiration. Ann. Rev. Plant Physiol., 32, 349–383.

    CAS  Google Scholar 

  21. Ellis R. J. and Gray, J. C. (1986) Ribulose bisphosphate carboxylase-oxygenase. The Royal Society, London.

    Google Scholar 

  22. Barbeau, W. E. and Kinsella, J. E. (1988) Ribulose bisphosphate carboxylase/oxygenase (Rubisco) from green leaves — potential as a food protein. Food Rev. Int., 4, 93–127.

    CAS  Google Scholar 

  23. Wildman, S. G. and Bonner, J. (1947) The proteins of green leaves. I. Isolation, enzymatic properties and auxin content of Spinach cytoplasmic proteins. Arch. Biochem., 14, 381–413.

    CAS  Google Scholar 

  24. Weissbach, A., Horecker, B. L. and Hurwitz, J. (1956) The enzymatic formation of phosphoglyceric acid from ribulose diphosphate and carbon dioxide. J. Biol. Chem., 218, 795–810.

    CAS  Google Scholar 

  25. Ellis, R. J. (1979) The most abundant protein in the world. Trends Biochem. Sci., 4, 241–4.

    CAS  Google Scholar 

  26. Pheloung P. and Brady, C. J. (1979) Soluble and fraction 1 protein in leaves of C3 and C4 grasses. J. Sci. Food Agric., 30, 246–50.

    CAS  Google Scholar 

  27. Douillard, R., Porcheron, A., Lila, M. et al. (1990) Teneur en ribulose-1,5-bisphosphate carboxylase/oxygénase des Feuilles de Luzerne (Medicago sativa L.). Facteurs de variation génétique el agronomique. Agronomie, 10, 273–84.

    Google Scholar 

  28. Ecochard, R., Cavalie, G., Nicco C. et al. (1991) Rubisco content and specific activity in barley (Hordeum vulgare L.). J. Exp. Bot., 42, 39–43.

    CAS  Google Scholar 

  29. Noguchi, H., Maekawa, T., Fujimoto, S et al. (1978) Physico-chemical studies on fraction I protein from alfalfa. Agric. Biol. Chem., 42, 1553–8.

    CAS  Google Scholar 

  30. Yeoh, H. H., Stone, N. E. and Watson, L. (1982) Taxonomic variation in the subunit amino acid composition of RuBP carboxylase from grasses. Phytochemistry, 21, 71–80.

    CAS  Google Scholar 

  31. Bigelow, C. C. (1967) On the average hydrophobicity of proteins and the relation between it and protein structure. J. Theor. Biol., 16, 187–211.

    CAS  Google Scholar 

  32. Barrantes, F. J. (1975) The nicotinic chlorinergic receptor: different compositions evidenced by statistical analysis. Biochem. Biophys. Res. Commun., 62, 407–14.

    CAS  Google Scholar 

  33. Hatch, F. T. and Bruce, A. L. (1968) Amino-acid composition of soluble and membranous lipoproteins. Nature, 218, 1166–8.

    CAS  Google Scholar 

  34. Krebbers, E., Seurinck, J., Herdies, L. et al. (1988) Four genes in two diverged subfamilies encode the ribulose-1,5-biphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana. Plant Mol. Biol., 11, 745–59.

    CAS  Google Scholar 

  35. Zurawski, G., Clegg, M. T., and Brown, A. H. D. (1984) The nature of nucleotide sequence divergence between barley and maize chloroplast DNA. Genetics, 106, 735–49.

    CAS  Google Scholar 

  36. Greenland, A. J., Thomas, M. V. and Walden, R. M. (1987) Expression of two nuclear genes encoding chloroplast proteins during early development of cucumber seedlings. Planta, 170, 99–110.

    CAS  Google Scholar 

  37. Stiekema, W. J., Wimpee, C. F. and Tobin, E. M. (1983) Nucleotide sequence encoding the precursor of the small subunit of ribulose 1,5-bisphosphate carboxylase from Lemna gibba L.G-3. Nucleic Acids Res., 11, 8051–61.

    CAS  Google Scholar 

  38. Adams, C. A., Babcock, M., Leung, F. and Sun, S. M. (1987) Sequence of a ribulose 1,5-bisphosphate carboxylase/oxygenase cDNA from the C4 dicot Flaveria trinervia. Nucleic Acids Res., 15, 1875.

    CAS  Google Scholar 

  39. Hutchinson, K. W., Harvie, P. D., Singer, P. B. et al. (1990) Nucleotide sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase from the conifer Larix laricina. Plant Mol. Biol., 14, 281–4.

    CAS  Google Scholar 

  40. Matsuoka, M., Kano-Murakami, Y., Tanaka, Y. et al. (1987) Nucleotide sequence of cDNA encoding the small subunit of ribulose-1,5-bisphos-phate carboxylase from maize. J. Biochem., 102, 673–6.

    CAS  Google Scholar 

  41. Ren, L., Salnikow, J. and Vater, J. (1988) Ribulose-1,5-bisphosphate carboxylase/oxygenase from zea mays: amino-acid sequence of the small subunit. Biol Chem. Hoppe-Seyler, 369, 609–15.

    CAS  Google Scholar 

  42. Pinck, M., Guilley, E., Durr, A. et al. (1984) Complete sequence of one of the mRNAs coding for the small subunit of ribulose bisphosphate carboxylase of Nicotiana sylvestris. Biochimie, 66, 539–45.

    CAS  Google Scholar 

  43. Bedbrook, J. R., Smith, S. M. and Ellis, R. J. (1980) Molecular cloning and sequencing of cDNA encoding the precursor to the small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase. Nature, 287, 692–7.

    CAS  Google Scholar 

  44. Takruri, I. A. H., Boulter, D. and Ellis, R. J. (1981) Amino acid sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase of Pisum sativum. Phytochem., 20, 413–15.

    CAS  Google Scholar 

  45. Coruzzi, G., Broglie, R., Cashmore, A. and Chua, N.-H. (1983) Nucleotide sequences of two pea cDNA clones encoding the small subunit of ribulose 1,5-bisphosphate carboxylase and the major chlorophyll a/b-binding thylakoid polypeptide. J. Biol. Chem., 258, 1399–402.

    CAS  Google Scholar 

  46. Coruzzi, G., Broglie, R., Edwards, C. and Chua, N.-H. (1984) Tissue-specific and light-regulated expression of the pea nuclear gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase. Embo J., 3, 1671–9.

    CAS  Google Scholar 

  47. Tumer, N. E., Clark, W. G., Tabor, G. J. et al. (1986) The genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase are expressed differentially in Petunia leaves. Nucleic Acids Res., 14, 3325–42.

    CAS  Google Scholar 

  48. Yamamoto, N., Kano-Murakami, Y., Ohashi, Y. and Tanaka, Y. (1988) Nucleotide sequence of a full length cDNA clone of ribulose bisphos-phate carboxylase small subunit gene from green dark-grown Pine (Pinus tubergii) seedling. Nucleic Acids Res., 16, 11830.

    CAS  Google Scholar 

  49. Wolter, F. P., Fritz, C. C., Willmitzer, L. et al. (1988). rcbS genes in Solanum tuberosum: conservation of transit peptide and exon shuffling during evolution. Proc. Natl Acad. Sci. USA, 85, 846–50.

    Google Scholar 

  50. Guidet, F. and Fourcroy, P. (1988) Nucleotide sequence of a radish ribulose 1,5-bisphosphate carboxylase small subunit (rbcS) cDNA. Nucleic Acids Res., 16, 2336.

    CAS  Google Scholar 

  51. Baszczynski, C. L., Fallis, L. and Bellemare, G. (1988) Nucleotide sequence of a full length cDNA clone of a Brassica napus ribulose bisphosphate carboxylase-oxygenase small subunit gene. Nucleic Acids Res., 16, 4732.

    CAS  Google Scholar 

  52. Matsuoka, M., Kano-Murakami, Y., Tanaka, Y. et al. (1988) Classification and nucleotide sequence of cDNA encoding the small subunit of ribulose-1,5-bisphosphate carboxylase from rice. Plant Cell Physiol., 29, 1015–22.

    CAS  Google Scholar 

  53. Xie, Y. and Wu, R. (1988) Nucleotide sequence of a ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit gene (rbcS) in rice. Nucleic Acids Res., 16, 7749.

    CAS  Google Scholar 

  54. Berry-Lowe, S. L., McKnight, T. D., Shah, D. M. and Meagher, R. B. (1982) The nucleotide sequence, expression, and evolution of one member of a multigene family encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in Soybean. J. Mol. Appl Gen., 1, 483–98.

    CAS  Google Scholar 

  55. Grandbastien, M. A., Berry-Lowe, S., Shirley, B. W. and Meagher, R. B. (1986) Two soybean ribulose-1,5-bisphosphate carboxylase small subunit genes share extensive homology even in distant flanking sequences. Plant Mol. Biol., 7, 451–65.

    CAS  Google Scholar 

  56. Martin, P. G. (1979) Amino acid sequence of the small subunit of ribu-lose-1,5-bisphosphate carboxylase from spinach. Aust. J. Plant Physiol., 6, 401–8.

    CAS  Google Scholar 

  57. Waksman, G., Lebrun, M. and Freyssinet, G. (1987) Nucleotide sequence of a gene encoding sunflower ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit (rbcs). Nucleic Acids Res., 15, 7181.

    CAS  Google Scholar 

  58. Müller, K.-D., Salnikow, J. and Vater, J. (1983) Amino acid sequence of the small subunit of d-ribulosebisphosphate carboxylase/oxygenase from Nicotiana tabacum. Biochim. Biophys. Acta, 742, 78–83.

    Google Scholar 

  59. Mazur, B. J. and Chui, C. F. (1985) Sequence of a genomic DNA clone for the small subunit of ribulose Bis-Phosphate Carboxylase-Oxygenase from tobacco. Nucleic Acid Res., 13, 2373–86.

    CAS  Google Scholar 

  60. Pichersky, E., Bernatzky, R., Tanksley, S. D. and Cashmore, A. R. (1986) Evidence for selection as a mechanism in the concerted evolution of Lycopersicon esculentum (tomato) genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. Proc. Natl Acad. Sci. USA, 83, 3880–4.

    CAS  Google Scholar 

  61. Broglie R., Coruzzi, G., Lamppa, G. et al. (1983) Structural analysis of nuclear genes coding for the precursor to the small subunit of wheat ribulose-1,5-bisphosphate carboxylase. Bio/technology, 1, 55–60.

    Google Scholar 

  62. Ellison, N. W., Yu, P. L. and White, D. W. R. (1990) Nucleotide sequence of a white clover ribulose bisphosphate carboxylase small subunit gene. Nucleic Acid Res., 18, 4914.

    CAS  Google Scholar 

  63. Terachi, T., Ogihara, Y. and Tsunewaki, K. (1987) The molecular basis of genetic diversity among cytoplasms of Triticum and Aegilops. VI. Complete nucleotide sequence of the rbcL genes encoding H- and L-type rubisco large subunits in common wheat and Ae. crassa 4x. Jpn J Genet., 62, 375–87.

    CAS  Google Scholar 

  64. Terachi, T., Ogihara, Y. and Tsunewaki, K. (1988) The rcbL genes in wheat and several Aegilops species with divergent chloroplast genomes, in Proceedings of the 7th International Wheat Genetics Symp., Cambridge, pp. 789–95.

    Google Scholar 

  65. Hudson, G. S., Mahon, J. D., Anderson, P. A. et al. (1990) Comparisons of rbcL genes for the large subunit of ribulose-bisphosphate carboxylase from closely related C3 and C4 plant species. J. Biol Chem., 265, 808–14.

    CAS  Google Scholar 

  66. Hipkins, V. D., Tsai, C. H. and Strauss, S. H. (1990) Sequence of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from a gymnosperm, Douglas fir. Plant Mol. Biol., 15, 505-7.

    CAS  Google Scholar 

  67. Aldrich, J., Cherney, B., Merlin, E. and Palmer, J. (1986) Sequence of the rcbL gene for the large subunit of ribulose bisphosphate carboxylase-oxygenase from Alfalfa. Nucleic Acids Res., 14, 9535.

    CAS  Google Scholar 

  68. McIntosh, L., Poulsen, C. and Bogorad, L. (1980) Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize. Nature, 288, 556–60.

    CAS  Google Scholar 

  69. Zurawski, G., Whitfeld, P. R. and Bottomley, W. (1986) Sequence of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from pea chloroplast. Nucleic Acids Res., 14, 3975.

    CAS  Google Scholar 

  70. Aldrich, J., Cherney, B., Merlin, E. and Palmer, J. (1986) Sequence of the rbcL gene for the large subunit of ribulose bisphosphate carboxylase-oxygenase from Petunia. Nucleic Acids Res., 14, 9534.

    CAS  Google Scholar 

  71. Nishizawa, Y. and Hirai, A. (1987) Nucleotide sequence and expression of the gene for the large subunit of rice ribulose-1,5-bisphosphate carboxylase. Jpn. J. Genet., 62, 389–95.

    CAS  Google Scholar 

  72. Zurawski, G., Perrot B., Bottomley, W. and Whitfeld, P. R. (1981) The structure of the gene for the large subunit of ribulose, 1,5-bisphosphate carboxylase from spinach chloroplast DNA. Nucleic Acids Res., 9, 3251–70.

    CAS  Google Scholar 

  73. Amiri, I, Salnikow, J. and Vater, J. (1984) Amino-acid sequence of the large subunit of d-ribulosebisphosphate carboxylase/oxygenase from Nicotiana tabacum. Biochim. Biophys. Acta. 784, 116–23.

    CAS  Google Scholar 

  74. Shinozaki, K. and Sugiura, M. (1982) The nucleotide sequence of the tobacco chloroplast Gene for the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. Gene, 20, 91–102.

    CAS  Google Scholar 

  75. Meagher, R. B., Berry-Lowe, S. and Rice, K. (1989) Molecular evolution of the small subunit of ribulose bisphosphate carboxylase: nucleotide substitution and gene conversion. Genetics, 123, 845–63.

    CAS  Google Scholar 

  76. Manzara, T. and Gruissem, W. (1988) Organization and expression of the genes encoding ribulose-1,5-bisphosphate carboxylase in higher plants. Photosynth. Res., 16, 117–39.

    CAS  Google Scholar 

  77. Donnelly, M. I., Hartman, F. C. and Ramakrishnan, V. (1984) The shape of ribulose bisphosphate carboxylase/oxygenase in solution as inferred from small angle neutron scattering. J. Biol. Chem., 259, 406–11.

    CAS  Google Scholar 

  78. Pilz, I., Schwarz, E., Pal, G. P. and Saenger, W. (1987) Small angle X-ray study on the structure of active and inactive ribulose-1,5-bisphosphate carboxylase-oxygenase from spinach. Evidence for a configurational change. Z. Naturfosch., 42c, 1089–91.

    Google Scholar 

  79. Abuja, P. M. and Pilz, I. (1988) Investigation of ribulose-1,5-bisphosphate carboxylase-oxygenase from tobacco by small angle X-ray scattering: a structural model for the enzyme insolution. Z. naturforsch., 43C, 373–6.

    Google Scholar 

  80. Steer, M. W., Gunning, B. E. S., Graham, T. A. and Carr, D. J. (1968) Isolation, properties, and structure of fraction I protein from Avena saliva L. Planta, 79, 254–67.

    CAS  Google Scholar 

  81. Chapman, M. S., Suh, S. W., Cascio, D. et al. (1987) Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO. Nature, 329, 354–6.

    CAS  Google Scholar 

  82. Chapman, M. S., Suh, S. W., Curmi, P. M. G. et al. (1988) Tertiary structure of plant RuBisCO: domains and their contacts. Science, 241, 71–4.

    CAS  Google Scholar 

  83. Knight, S., Andersson, I. and Brändén, C. I. (1989) Re-examination of the three-dimensional structure of the small subunit of RuBisCo from higher plants. Science, 244, 702–5.

    CAS  Google Scholar 

  84. Knight, S., Andersson, I. and Brändén, C. I. (1990) Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution. Subunit interactions and active site. J. Mol. Biol., 215, 113–60.

    CAS  Google Scholar 

  85. Schneider, G., Knight, S., Andersson, I. et al. (1990) Comparison of the crystal structures of L2 and L8S8 rubisco suggests a functional role for the small subunit. EMBO J., 9, 2045–50.

    CAS  Google Scholar 

  86. Kawashima, N. and Wildman, S. G. (1971) Studies on Fraction I protein. II Comparison of physical, chemical, immunological and enzymatic properties between spinach and tobacco Fraction I proteins. Biochem. Biophys. Acta, 229, 749–60.

    CAS  Google Scholar 

  87. Miller, S. (1989) The structure of interfaces between subunits of dimeric and tetrameric proteins. Prot. Engng., 3, 77–83.

    CAS  Google Scholar 

  88. Georgi, S., Radunz, A. and Schmid, G. H. (1990) Characterization of RuBP carboxylase/oxygenase of the N. tabacum mutant series ‘Consolation’ with homologous and non-homologous antisera. Z. Naturforsch., 45c, 749–56.

    Google Scholar 

  89. Chen, K., Kung, S. D., Gray, J. C. and Wildman, S. G. (1976) Subunit polypeptide composition of fraction I protein from various plant species. Plant Sci. Lett., 7, 429–34.

    CAS  Google Scholar 

  90. Kung, S. D. (1984) Genetic analysis of tobacco RuBPCASE. CRC Crit. Rev. Plant Sci., 1, 227–67.

    CAS  Google Scholar 

  91. Dean, C., van den Elzen, P, Tamaki, S. et al. (1985) Linkage and homology analysis divides the eight genes for the small subunit of petunia ribulose 1,5-bisphosphate carboxylase into three gene families. Proc. Natl Acad. Sci. USA, 82, 4964–8.

    CAS  Google Scholar 

  92. Lin, C. M., Liu, Z. Q., and Kung, S. D. (1986) Nicotiana chloroplast genome: X. Correlation between the DNA sequences and the isoelectric focusing patterns of the LS of rubisco. Plant Mol. Biol., 6, 81–7.

    CAS  Google Scholar 

  93. Sugita, M. and Gruissem, W. (1987) Developmental, organ specific, and light-dependent expression of the tomato ribulose-1,5 bisphosphate carboxylase small subunit gene family. Proc. Natl Acad. Sci. USA, 84, 7104–8.

    CAS  Google Scholar 

  94. Foyer, C. H. (1985) Stromal protein phosphorylation in spinach (Spinacia oleracea) chloroplasts. Biochem. J., 231, 97–103.

    CAS  Google Scholar 

  95. Bahr, J. T., Bourque, D. P. and Smith, H. J. (1977) Solubility properties of fraction I proteins of maize, cotton, spinach, and tobacco. J. Agric. Food Chem., 25, 783–9.

    CAS  Google Scholar 

  96. Reger, B. J., Ku, M. S. B., Potter, J. W. and Evans, J. J. (1983) Purification and characterization of maize ribulose-1,5-bisphosphate carboxylase. Phytochemistry, 22, 1127–32.

    CAS  Google Scholar 

  97. Matsumoto, C., Sugiyama, T. and Akazawa, T. (1969) Structure and function of chloroplast proteins IX. Further comparative studies on Chlorella and Spinach leaf ribulose-1,5-bisphosphate carboxylase. Arch. Biochem. Biophys. 135, 282–7.

    CAS  Google Scholar 

  98. Miziorko, H. M., Nowak, T. and Mildvan, A. S. (1974) Spinach leaf phosphoenolpyruvate carboxylase: purification, properties, and kinetic studies. Arch. Biochem. Biophys., 163, 378–89.

    CAS  Google Scholar 

  99. Iwanij, V., Chua, N. H. and Siekevitz, P. (1974) The purification and some properties of ribulosebisphosphate carboxylase and of its subunits from the green alga Chlamdyomonas reinhardtii. Biochim. Biophys. Acta, 358, 329–40.

    CAS  Google Scholar 

  100. Daday, H. V. and Whitecross, M. I. (1983) Isoelectric focusing of ribulose bisphosphate carboxylase from lucerne and spinach. Sci. Tools, 30, 11–14.

    CAS  Google Scholar 

  101. Douillard, R. and Songrilay Kongphet, T. (1990) Propriétés tension-actives de la ribulose-1,5-bisphosphate carboxylase/oxygenase de Luzerne native et maltosylée. Sci. Aliments. 10, 175–87.

    CAS  Google Scholar 

  102. Kachru, R. B. and Anderson, L. E. (1974) Chloroplast and cytoplasmic enzymes. V. Pea-leaf carbonic anhydrases. Planta, 118, 235–40.

    CAS  Google Scholar 

  103. Rabinowitz, H., Reisfeld, A., Sagher, D. and Edelman, M. (1975) Ribulose diphosphate carboxylase from autotrophic Euglena gracilis. Plant Physiol., 56, 345–50.

    CAS  Google Scholar 

  104. Trown, P. W. (1965) An improved method for the isolation of carboxy-dismutase. Probable identity with fraction I protein and the protein moiety of protochlorophyll holochrome. Biochemistry, 4, 908–18.

    CAS  Google Scholar 

  105. Paulsen, J. M. and Lane, M. D. (1966) Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme. Biochemistry, 5, 2350–7.

    CAS  Google Scholar 

  106. Pon, N. G. (1967) Some physical properties of purified fraction I protein from spinach chloroplasts. Arch. Biochem. Biophys., 119, 179–93.

    CAS  Google Scholar 

  107. Johal, S., Bourque, D. P., Smith, W. W. et al. (1980) Crystallization and characterization of ribulose 1,5-bisphosphate carboxylase/oxygenase from eight plant species. J. Biol. Chem., 255, 8873–80.

    CAS  Google Scholar 

  108. Tomimatsu, Y. (1980) Macromolecular properties and subunit interactions of ribulose-1,5-bisphosphate carboxylase from alfalfa. Biochim. Biophys. Acta, 622, 85–93.

    CAS  Google Scholar 

  109. Peñarrubia, L. and Moreno, J. (1988) Ribulose 1,5-bisphosphate carboxylase/oxygenase from citrus leaves. Phytochemistry, 27, 1999–2004.

    Google Scholar 

  110. Gill, S. C. and von Hippel P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem., 182, 319–26.

    CAS  Google Scholar 

  111. Hood, L. L., Cheng, S. G., Koch, U. and Brunner, J. R. (1981) Alfalfa proteins: isolation and partial characterization of the major component — Fraction I protein. J. Food Sci., 46, 1843–50.

    CAS  Google Scholar 

  112. Christeller, J. T. (1981) The effects of bivalent cations on ribulose bisphosphate carboxylase/oxygenase. Biochem. J., 193, 839–44.

    CAS  Google Scholar 

  113. Parry, M. A. J., Schmidt, C. N. G., Keys, A. J. and Gutteridge, S. (1983) Activation of ribulose 1,5-bisphosphate carboxylase by Ca2+. FEBS Lett., 159, 107–11.

    CAS  Google Scholar 

  114. Styring, S. and Brändén, R. (1985) Identification of ligands to the metal ion in copper(II)-activated ribulose-1,5-bisphosphate carboxylase/oxygenase by the use of electron paramagnetic resonance spectroscopy and 17O-labeled ligands. Biochemistry, 24, 6011–19.

    CAS  Google Scholar 

  115. Nilsson, T., Brändén, R. and Styring, S. (1984) Distortion of the activator metal coordination during the turnover of cobalt-activated ribulosebisphosphate carboxylase/oxygenase. Biochim. Biophys. Acta, 788, 274–280.

    CAS  Google Scholar 

  116. Bränden, R., Janson, K., Nilsson, P. and Aasa, R. (1987) Intermediates formed by the Co++-activated ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach studied by electron paramagnetic resonance spectroscopy. Biochim. Biohys. Acta, 916, 298–303.

    Google Scholar 

  117. Bhagwat, A. S. and Verma, N. C. (1988) Effect of activation by Mg2+ on the conformation of ribulose-1,5-bisphosphate carboxylase/oxygenase: a fluorescence study. Indian J. Biochem. Biophys., 25, 244–8.

    CAS  Google Scholar 

  118. Grebanier, A. E., Champagne, D. and Roy, H. (1978) Effects of Mg2+ and substrates on the conformation of ribulose-1,5-bisphosphate carboxylase. Biochemistry, 17, 5150–55.

    CAS  Google Scholar 

  119. Bränden, R., Janson, K. and Nilsson, P. (1989) Studies of the Co++-activated ribulose-1,5-bisphosphate carboxylase/oxygenase by the use of spectrophotometry. Biochim. Biophys. Acta, 995, 75–81.

    Google Scholar 

  120. Tomimatsu, Y. and Donovan, J. W. (1981) Effects of pH, Mg++, CO2 and mercurials on the circular dichoism, thermal stability and light scattering of ribulose-1,5-bisphosphate carboxylases from alfalfa, spinach and tobacco. Plant Physiol., 68, 808–13.

    CAS  Google Scholar 

  121. Buchanan, B. B. and Schürmann, P. (1973) Regulation of ribulose 1,5-diphosphate carboxylase in the photosynthetic assimilation of carbon dioxide. J. Biol. Chem., 248, 4956–64.

    CAS  Google Scholar 

  122. Ashton, A. R. (1982) A role for ribulose-1,5-bisphosphate carboxylase as a metabolite buffer. FEBS Lett., 145, 1–7.

    CAS  Google Scholar 

  123. Ogren, W. L., Salvucci, M. E. and Portis, A. R. Jr. (1986) The regulation of rubisco activity. Phil. Trans. R. Soc. Lond. B, 313, 337–46.

    CAS  Google Scholar 

  124. Woodrow, I. E. and Berry, J. A. (1988) Enzymatic regulation of photo-synthetic CO2 fixation in C3 plants. Ann Rev. Plant Physiol. Plant Mol. Biol., 39, 533–94.

    CAS  Google Scholar 

  125. Beck, E.; Scheibe, R. and Reiner, J. (1989) An assessment of the Rubisco inhibitor. 2-carboxyarabinito-l-phosphate and d-hamamelonic acid 21-phosphate are identical compounds. Plant Physiol., 90, 13–16.

    CAS  Google Scholar 

  126. Wardrop, A. J. and Polya, G. M. (1980) Co-purification of pea and bean leaf soluble auxin-binding proteins with ribulose 1,5-bisphosphate carboxylase. Plant Physiol, 66, 105–11.

    CAS  Google Scholar 

  127. Parry, M. A. J., Schmidt, C. N. G., Cornelius, M. J. et al. (1985) Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme. J. Exp. Bot., 36, 1396–404.

    CAS  Google Scholar 

  128. Gontero, B., Cárdenas, M. L. and Ricard, J. (1988) A functional five-enzyme complex of chloroplast involved in the Calvin cycle. Eur. J. Biochem., 173, 437–43.

    CAS  Google Scholar 

  129. Sainis, J. K., Merriam, K. and Harris, G. C. (1989) The association of d-ribulose-1,5-bisphosphate carboxylase/oxygenase with phosphoribulo-kinase. Plant Physiol., 89, 368–74.

    CAS  Google Scholar 

  130. Sainis, J. K. and Harris, G. C. (1986) The association of ribulose-1,5-bisphosphate carboxylase with phosphoriboisomerase and phospho-ribulokinase. Biochem. Biophys. Res. Commun., 139, 947–54.

    CAS  Google Scholar 

  131. Rosichan, J. L. and Huffaker, R. C. (1984) Source of endoproteolytic activity associated with purified ribulose bisphosphate carboxylase. Plant Physiol., 75, 74–7.

    CAS  Google Scholar 

  132. Hazlewood, G. P., Horsnell, J. M., Mangan, J. L. (1983) Trypsin isoinhibitors of lucerne: association with leaf fraction 1 protein. Phytochemistry, 22, 1107–11.

    CAS  Google Scholar 

  133. Sheen, S. J. and Sheen, V. L. (1985) Functional properties of fraction-1-protein from tobacco leaf. J. Agric. Food Chem., 33, 79–83.

    CAS  Google Scholar 

  134. Barbeau, W. E. and Kinsella, J. E. (1983) Factors affecting the binding of chlorogenic acid to fraction 1 leaf protein. J. Agric. Food Chem., 31, 993–8.

    CAS  Google Scholar 

  135. Kleinkopf, G. E., Huffaker, R. C. and Matheson, A. (1970) A simplified purification and some properties of ribulose 1,5-bisphosphate carboxylase from barley. Plant Physiol., 46, 204–7.

    CAS  Google Scholar 

  136. Douillard, R. (1986) Purification et Caractérisation électrophorétique de la Ribulose-1,5-Bisphosphate Carboxylase/Oxygénase de Luzerne. Sci. Aliments, 6, 81–9.

    CAS  Google Scholar 

  137. Hall, N. P., McCurry, D. and Tolbert, N. E. (1981) Storage and maintaining activity of ribulose bisphosphate carboxylase/oxygenase. Plant Physiol., 67, 1220–3.

    CAS  Google Scholar 

  138. Chan, P. H., Sakano, K., Singh, S. and Wildman, S. G. (1972) Crystalline fraction I protein: preparation in large yield. Science, 176, 1145–6.

    CAS  Google Scholar 

  139. Baker, T. S., Eisenberg, D., Eiserling, F. A. and Weissman, L. (1975) The structure of form I crystals of d-ribulose-1,5-diphosphate carboxylase. J. Mol. Biol. 91, 391–9.

    CAS  Google Scholar 

  140. Baker, T. S., Suh, S. W. and Eisenberg, D. (1977) Structure of ribulose-1,5-bisphosphate carboxylase-oxygenase form III crystals. Proc. Nat. Acad. Sci. USA, 74, 1037–41.

    CAS  Google Scholar 

  141. Suh, S. W., Cascio, D., Chapman, M. S. and Eisenberg, D. (1987) A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state. J. Mol Biol., 197, 363–5.

    CAS  Google Scholar 

  142. Johal, S. and Bourque, D. P. (1982) Preparation of crystalline RuBPCase from higher plants, in Methods in chloroplast molecular biology, (ed M. Edelman, R. B. Hallick and N. H. Chua), Elsevier Biomedical Press, Amsterdam, pp. 783–92.

    Google Scholar 

  143. Bourque, D. P. (1982) Purification of protein extracted from leaves. European patent 0 048 633 A3, 33 pp.

    Google Scholar 

  144. Pagliaro, L. and Johal, S. (1985) Crystals of CO2/Mg2+-activated and deactivated spinach ribulosebisphosphate carboxylase. Biochim. Biophys. Acta, 831, 34–9.

    CAS  Google Scholar 

  145. Sheen, S. J. and Sheen, V. L. (1987) Characteristics of fraction-1-protein degradation by chemical and enzymatic treatments. J. Agric. Food Chem., 35, 948–52.

    CAS  Google Scholar 

  146. Li, L. R., Li, C. F. and Xu, R. B. (1988) Dissociation and reconstitution of immobilized ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco. Sci. Sin., 31, 1204–12.

    CAS  Google Scholar 

  147. Voordouw, G., van der Vies, S. M. and Bouwmeister, P. P. (1984) Dissociation of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach by urea. Eur. J. Biochem., 141, 313–18.

    CAS  Google Scholar 

  148. Sarkar, S. K., Howarth, R. E., Hikichi, M. and McArthur, J. M. (1975) Soluble proteins of alfalfa (Medicago sativa) herbage. Fractionation by ammonium sulfate and gel chromatography. J. Agric. Food Chem., 23, 626–30.

    CAS  Google Scholar 

  149. Incharoensakdi, A., Takabe, T., Takabe, T. and Akazawa, T. (1986) Isolation of the catalytic competent small subunit of ribulose bisphosphate carboxylase/oxygenase from spinach under an extremely alkaline condition. Biochem. Biophys. Res. Commun., 138, 118–24.

    CAS  Google Scholar 

  150. Rintamäki, E. (1989) Formation of disulphide cross-linked aggregates of large subunits from higher plant ribulose-1,5-bisphosphate carboxylase-oxygenase. J. Exp. Bot., 40, 1305–13.

    Google Scholar 

  151. Andrews, T. J. and Lorimer, G. H. (1985) Catalytic properties of a hybrid between cyanobacterial large subunits and higher plant small subunits of ribulose bisphosphate carboxylase-oxygenase J. Biol. Chem., 260, 4632–6.

    CAS  Google Scholar 

  152. Makino, A., Mae, T. and Ohira, K. (1983) Purification and storage of ribulose-1,5-bisphosphate carboxylase from rice leaves. Plant Cell Physiol. 24, 1169–73.

    CAS  Google Scholar 

  153. Suelter, C. H. and Deluca, M. (1983) How to prevent losses of protein by adsorption to glass and plastic. Anal. Biochem., 135, 112–19.

    CAS  Google Scholar 

  154. Mächler, F., Keys, A. J. and Cornelius, M. J. (1980) Activation of ribulose bisphosphate carboxylase purified from wheat leaves. J. Exp. Bot., 31, 7–14.

    Google Scholar 

  155. Burova, T. V., Soshsinsky, A. A., Danilenko, A. N. et al. (1989) Conformation stability of ribulose diphosphate carboxylase of alfalfa green leaves according to the data of differential scanning microcalorimetry. Biofizika, 34, 545–9.

    CAS  Google Scholar 

  156. Peñarrubia, L. and Moreno, J. (1987) Spontaneous and shear-induced inactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase in vitro.Biochim. Biophys. Acta, 916, 227–35.

    Google Scholar 

  157. Douillard, R. and Teissié, J. (1991) Surface pressure and fluorescence study of ribulose-1,5-bisphosphate carboxylase/oxygenase adsorption at an air/buffer interface. J. Colloid Interface Sci., 143, 111–19.

    CAS  Google Scholar 

  158. Barbeau, W. E. and Kinsella, J. E. (1986) Physical behavior and functional properties: relationship between surface rheology and foam stability of ribulose 1,5-bisphosphate carboxylase. Colloids Surf., 17, 169–83.

    CAS  Google Scholar 

  159. de Fremery, D., Miller, R. E., Edwards, R. H. et al. (1973) Centrifugal separation of white and green protein fractions from alfalfa juice following controlled heating. J. Agr. Food Chem., 21, 886–9.

    Google Scholar 

  160. Knuckles, B. E., Edwards, R. H., Kohler, G. O. and Whitney, L. F. (1980) Flocculants in the separation of green and soluble white protein fractions from alfalfa. J. Agric. Food Chem., 28, 32–6.

    CAS  Google Scholar 

  161. Bray, W. J. and Humphries, C. (1979) Preparation of white leaf protein concentrate using a polyanionic flocculant. J. Sci. Food Agric., 30, 171–6.

    CAS  Google Scholar 

  162. Merodio, C., Martin, M. and Sabater, B. (1983) Improved separation of green and soluble leaf proteins by pH shift. J. Agric. Food Chem., 31, 957–9.

    CAS  Google Scholar 

  163. Eakin, D. E., Singh, R. P., Kohler, G. O. and Knuckles, B. (1978) Alfalfa protein fractionation by ultrafiltration. J. Food Sci., 43, 544–52.

    CAS  Google Scholar 

  164. Gwiazda, S. and Saio, K. (1981) Preparation of white leaf protein concentrates using calcium salts. Agric. Biol. Chem., 45, 2659–60.

    CAS  Google Scholar 

  165. Bray, W. J. and Humphries, C. (1978) Solvent fractionation of leaf juice to prepare green and white protein products. J. Sci. Food Agric., 29, 839–46.

    CAS  Google Scholar 

  166. Edwards, R. H., Miller, R. E., de Fremery, D. et al. (1975) Pilot plant production of an edible white fraction leaf protein concentrate from alfalfa. J. Agric. Food Chem., 23, 620–6.

    CAS  Google Scholar 

  167. Burghofer, C., Costes, C., Rambourg, J. C. et al. (1987) Amélioration du procédé industriel d’extraction de la protéine blanche de luzerne. Caractérisation de l’isolat obtenu destiné à l’alimentation humaine. Sci. Aliments, 7, 111–34.

    Google Scholar 

  168. Merodio, C. and Sabater, B. (1988) Preparation of a white protein fraction in high yield from sugar beet (Beta vulgaris L) leaves. J. Sci. Food Agric., 44, 237–43.

    CAS  Google Scholar 

  169. Miller, R. E., de Fremery, D., Bickoff, E. M. and Kohler, G. O. (1975) Soluble protein concentrate from alfalfa by low-temperature acid precipitation. J. Agric. Food Chem., 23, 1177–9.

    CAS  Google Scholar 

  170. Knuckles, B. E., de Fremery, D., Bickoff, E. M. and Kholer, G. O. (1975) Soluble protein from alfalfa juice by membrane filtration. J. Agric. Food Chem., 23, 209–12.

    CAS  Google Scholar 

  171. Knuckles, B. E., Edwards, R. H., Miller, R. E. and Kohler, G. O. (1980) Pilot scale ultrafiltration of clarified alfalfa juice. J. Food Sci., 45, 730–4.

    CAS  Google Scholar 

  172. Wildman, S. G. and Kwanyuen, P. (1982) Process for isolation of proteins from plant leaves, US Patent No. 4374324.

    Google Scholar 

  173. Duméry, B. (1983) Procédé d’extraction des protéines foliares à partir d’une matière végétale et plus particulièrement d’une plante genre Nicotiana. French patent 8302097, 14 pp.

    Google Scholar 

  174. Duméry, B., Albo, J. P. and Chouteau, J. (1981) Approche analytique des protéines de tabac. Implications technologiques. Ann. Tabac, Sect. 2, 17, 105–32.

    Google Scholar 

  175. Lowe, R. H. (1977) Crystallization of fraction I protein from tobacco by a simplified procedure. FEBS Lett., 78, 98–100.

    CAS  Google Scholar 

  176. Knuckles, B. E., Kohler, G. O. and de Fremery, D. (1979) Processing of fresh tobacco leaves for protein fractions. J. Agric. Food Chem., 27, 414–18.

    CAS  Google Scholar 

  177. Kung, S. D., Chollet, R. and Marsho, T. V. (1980) Crystallization and assay procedures of tobacco ribulose-1,5-bisphosphate carboxylase-oxygenase. Methods Enzymol., 69, 326–36.

    CAS  Google Scholar 

  178. Kung, S. D. and Tso, T. C. (1978) Tobacco as a potential food source and smoke material: soluble protein content, extraction, and amino acid composition. J. Food Sci., 43, 1844–52.

    CAS  Google Scholar 

  179. Knuckles, B. E. and Kohler, G. O. (1982) Functional properties of protein concentrate from alfalfa. Agric. Food Chem., 30, 748–52.

    CAS  Google Scholar 

  180. Jones, W. T. and Mangan, J. L. (1976) Large-scale isolation of fraction 1 leaf protein (18S) from lucerne (Medicago sativa L). J. Agric. Sci., 86, 495–501.

    Google Scholar 

  181. Vidal, J., Godbillon, G. and Gadal, P. (1982) Estimation of Sorghum leaf phosphoenolpyruvate carboxylase protein using an immunoadsorbent column. Phytochemistry, 21, 2829–30.

    CAS  Google Scholar 

  182. Latzko, E. and Kelly, G. J. (1983) The many-faceted function of phosphoenolypyruvate carboxylase in C3 plants. Physiol Vég., 21, 805–15.

    CAS  Google Scholar 

  183. Kitabatake, N., Indo, K. and Doi, E. (1989) Changes in interfacial properties of the hen egg ovalbumin caused by freeze-drying and spray-drying. J. Agric. Food Chem., 37, 905–10.

    CAS  Google Scholar 

  184. Betschart, A. A. (1974) Nitrogen solubility of alfalfa protein concentrate as influenced by various factors. J. Food Sci., 39, 1110–15.

    CAS  Google Scholar 

  185. Sheen, S. J. (1989) Thermal modification of the structural and functional properties of fraction-1-protein. J. Agric. Food Chem., 37, 605–10.

    CAS  Google Scholar 

  186. Wang, C. H. and Damodaran, S. (1990) Thermal gelation of globular proteins: weight-average molecular weight dependence of gel strength. J. Agric. Food Chem., 38, 1157–64.

    CAS  Google Scholar 

  187. Sheen, S. J. and Sheen, V. T. (1988) Effect of chemical and enzymatic degradation on the functional properties of fraction-l-protein. J. Agric. Food Chem., 36, 445–50.

    CAS  Google Scholar 

  188. Douillard, R. and Songrilay Kongphet, T. (1990) Properties of rubisco from alfalfa leaves: surface activity before and after maltosylation. In: Proceedings of the third international conference on leaf protein research. Chiriotti editori, Pineralo, Italy, pp. 295–8.

    Google Scholar 

  189. Margosiak, S. A., Dharma, A., Bruce-Carver, M. R. et al. (1990) Identification of the large subunit of ribulose 1,5-bisphosphate carbosylase/oxygenase as a substrate for transglutaminase in Medicago sativa L. (Alfalfa). Plant Physiol., 92, 88–96.

    CAS  Google Scholar 

  190. Nio, N., Motoki, M. and Takinami, K. (1986) Gelation of protein emulsion by transglutaminase. Agric. Biol. Chem., 50, 1409–12.

    CAS  Google Scholar 

Download references

Authors
  1. R. Douillard
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. O. de Mathan
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Department of Food Science and Technology, University of Reading, UK

    B. J. F. Hudson

Rights and permissions

Reprints and permissions

Copyright information

© 1994 Springer Science+Business Media Dordrecht

About this chapter

Cite this chapter

Douillard, R., de Mathan, O. (1994). Leaf protein for food use: potential of Rubisco. In: Hudson, B.J.F. (eds) New and Developing Sources of Food Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2652-0_10

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-2652-0_10

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6139-8

  • Online ISBN: 978-1-4615-2652-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation