Stability of some cactaceae proteins based on fluorescence, circular dichroism, and differential scanning calorimetry measurements

Shela Gorinstein*, Marina Zemser, Francisco Vargas-Albores, Jose Luis Ochoa, Octavio Paredes-Lopez, Christian Scheler, Sevil Aksu, Johann Salnikow

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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.

Original languageEnglish
Pages (from-to)239-247
Number of pages9
JournalJournal of Protein Chemistry
Volume18
Issue number2
DOIs
StatePublished - 1999

Keywords

  • Cactaceae
  • Calorimetry
  • Denaturation
  • Electrophoresis
  • Fluorescence
  • Proteins
  • Spec troscopy

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