The protein profile of Theobroma cacao L. seeds as obtained by matrix-assisted laser desorption/ionization mass spectrometry

Rapid Commun Mass Spectrom. 2011 Jul 30;25(14):2035-42. doi: 10.1002/rcm.5080.

Abstract

The water-soluble protein profile of the seeds of green, red, and yellow Theobroma cacao L. fruits has been determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-ToF-MS). The seeds were powdered under liquid nitrogen and defatted. The residues were dialyzed and lyophilized. The obtained samples were suspended in the matrix solution of sinapinic acid. The obtained MALDI mass spectra showed the presence of a wide number of proteins with molecular weight ranging from 8000 to 13,000 Da and a cluster of peaks centered at 21,000 Da that were attributed to albumin. The abundance of this peak was found to depend on the different portion of the seed (husk, apical and cortical parts); however, the MALDI mass spectra obtained from the different varieties of cocoa were practically superimposable. Changes in the protein profiles were also observed after the cocoa seeds were treated by fermentation and roasting, which are processes usually employed for the commercial production of cocoa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cacao / chemistry*
  • Coumaric Acids / chemistry
  • Hot Temperature
  • Plant Extracts / chemistry
  • Plant Proteins / analysis*
  • Plant Proteins / chemistry
  • Seeds / chemistry*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*

Substances

  • Coumaric Acids
  • Plant Extracts
  • Plant Proteins
  • sinapinic acid