Abstract
Characterization of three cactus proteins (native and denatured) from Machaerocereus gummosus (Pitahaya agria), Lophocereu schottii (Garambullo), and Cholla opuntia (Cholla), was based on electrophoretic, fluorescence, CD (circular dichroism), DSC (differential scanning calorimetry), and FT-IR (Fourier transform infrared) measurements. The obtained results of intrinsic fluorescence, DSC, and CD were dissimilar for the three species of cactus, providing evidence of differences in secondary and tertiary structures. Cactus proteins may be situated in the following order corresponding to their relative stability: Machaerocereus gummosus (Pitahaya agria) > Cholla opuntia (Cholla) > Lophocereu schottii (Garambullo). Thermodynamic properties of proteins and their changes upon denaturation (temperature of denaturation, enthalphy, and the number of ruptured hydrogen bonds) were correlated with the secondary structure of proteins and disappearance of α-helix.
Similar content being viewed by others
REFERENCES
Arntfield, S. D., Ismond M. A. H., and Murray, E. D. (1987). Int. J. Pept. Prot. Res. 29, 9–20.
Biliaderis, C. G. (1983). Food Chem. 10, 239–265.
Bora, P. S., Brekke, C. J., Powers, J. R. (1994). J. Food Sci. 59, 594–596.
Bradford, M. M. (1976). Anal. Biochem. 72, 248–254.
Brazner, J., Aberdeen, V., and Starmer, W. T. (1984). Ecol. Entomol. 9, 375–381.
Bruhn, J. G. (1973). Plant Med. 24, 315–319.
Chen, R. F., Edelhoch, H., and Steiner, R. F. (1969). In Physical Principles and Techniques in Protein Chemistry, Part A (Leach, S. J., ed.), Academic Press, New York, p. 172.
Chen, Y., Yang, J. T., and Martinez, H. M. (1972). Biochemistry 11, 4120–4131.
Gorinstein, S., Zemser, M., Friedman, M., and Chang, Sh. M. (1995a). Int. J. Peptide Protein Res. 45, 248–256.
Gorinstein, S., Zemser, M., Vargas-Albores, F., and Ochoa, J.-L. (1995b). Biosci. Biotech. Biochem. 59, 2022–2027.
Gorinstein, S., Zemser, M., Friedman, M., Rodrigues, W. A., Martins, P. S., Vello, N. A., Tosello, G. A., and Paredes-Lopez, O. (1996). Food Chem. 56, 131–138.
Kaiden, K., Matsui, T., and Tanaka, S. (1987). Appl. Spectrosc. 42, 180–184.
Khan, S. M., Darnall, D. W., and Birnbaum, E. R. (1980). Biochim. Biophys. Acta 624, 1–12.
Kato, K., Mansui, T., and Tanaka, S. (1987). Appl. Spectrosc. 41, 861–865.
Keeley, J. E., and Keeley, S.C. (1989). Plant Cell Environ. 12, 331–336.
Laemmli, U. K. (1970). Nature 227, 680–685.
Lilley, G. G. (1986). J. Sci. Food Agric. 37, 895–907.
Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J. (1951). J. Biol. Chem. 193, 265–270.
Ma, C. Y., and Harwalkar, V. R. (1988). J. Food Sci. 53, 531–534.
Marcone, M. F., and Yada, R. Y. (1992). J. Agric. Food Chem. 40, 385–389.
Matsuura, J. E., and Manning, M. C. (1994). J. Agric. Food Chem. 42, 1650–1656.
Nagano, T., Mori, H., and Nishinari, K. (1994). J. Agric. Food Chem. 42, 1415–1419.
Noel, P. H., Pugh, J. A., Larme, A. C., and Marsh, G. (1997). Phytother. Res. 11, 512–517.
Otto, A., Thiede, B., Muller, E.-Ch., Scheler, Ch., Wittmann-Liebold, B., and Jungblut, P. (1996). Electrophoresis 17, 1643–1650.
Rodriguez-Felix, A., and Cantwell, M. (1988). Plant Foods Hum. Nutr. 38, 83–93.
Sarkar, P. K., and Doty, P. (1966). Proc. Natl. Acad. Sci. USA 55, 961–989.
Sirohi, S. K., Karim, S. A., and Misra, A. K. (1997). J. Arid Environ. 36, 161–166.
Somers, D. L., Giroux, R. W., and Filion, W. G. (1991). Genome 34, 940–943.
Teles, F. F. F., Stull, J. W., Brown, W. H., and Whiting, F. M. (1984). J. Sci. Food Agric. 35, 421–425.
Trejo-Gonzalez, A., Gabriel-Ortiz, G., Puebla-Perez, A. M., Huizar-Contreras, M. D., Munguia-Mazariegos, M. R., Mejia-Arreguin, S., and Calva, E. (1996). J. Ethnopharmacol. 55, 27–33.
Valencia, M. E., Atondo, J. L., and Hernandez, G. (1985). Ecol. Food Nutr. 17, 165–174.
Velez Boza, F., and Chavez, P. J. F. (1980). Rev. Fac. Farm. Univ. Cent. Ven. 47, 43–90.
Wagner, J. R., and Anon, M. C. (1985). J. Food Sci. 50, 1547–1550.
Wang, D.-H., and Damodaran, S. (1991). J. Agric. Food Chem. 39, 433–438.
Zemser, M., Friedman, M., Katzhendler, J., Greene, L. J., Minsky, A., and Gorinstein, S. (1994). J. Protein Chem. 13, 261–274.
Zenteno, E., Debray, H., and Montreuil, J. (1988). FEBS Lett. 238, 95–100.
Zenteno, E., Ochoa, J. L., Montano, L. F., Debray, H., and Montreuil, J. (1991). Plant Sci. 77, 11–20.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Gorinstein, S., Zemser, M., Vargas-Albores, F. et al. Stability of Some Cactaceae Proteins Based on Fluorescence, Circular Dichroism, and Differential Scanning Calorimetry Measurements. J Protein Chem 18, 239–247 (1999). https://doi.org/10.1023/A:1020640409179
Published:
Issue Date:
DOI: https://doi.org/10.1023/A:1020640409179