Comparative effects of limited tryptic hydrolysis on physicochemical and structural features of seed 11S globulins

Int J Biol Macromol. 2006 Nov 15;39(4-5):174-8. doi: 10.1016/j.ijbiomac.2005.12.006. Epub 2006 Jun 19.

Abstract

The effect of the limited proteolysis by trypsin on selected seed storage 11S globulins (broad bean and pea legumins, glycinin and helianthinin) was studied by high-sensitive differential scanning calorimetry, fluorescence spectroscopy and analysis of proteolysis kinetics. Different behaviour of glycinin and helianthinin, on one hand, and broad bean and pea legumins, on the other, were observed: in the first group changes in the physicochemical characteristics of the proteins due to their limited proteolysis are more pronounced in comparison with the second one, in relation with the extent of primary structure modifications. The differences observed have been evaluated in relation with the amino acid sequence features of the four 11S globulin studied and agree with the literature data concerning the protein structural changes in the course of the limited proteolysis.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2S Albumins, Plant
  • Calorimetry, Differential Scanning
  • Chemical Phenomena
  • Chemistry, Physical
  • Globulins / chemistry*
  • Glycine max / chemistry
  • Hydrolysis
  • Legumins
  • Molecular Sequence Data
  • Pisum sativum / chemistry
  • Plant Proteins / chemistry*
  • Protein Denaturation
  • Seed Storage Proteins
  • Seeds / chemistry
  • Soybean Proteins / chemistry
  • Spectrometry, Fluorescence
  • Thermodynamics
  • Trypsin
  • Vicia faba / chemistry

Substances

  • 2S Albumins, Plant
  • Globulins
  • Plant Proteins
  • Seed Storage Proteins
  • Soybean Proteins
  • glycinin
  • Trypsin

Associated data

  • SWISSPROT/P02857
  • SWISSPROT/P04776
  • SWISSPROT/P14594
  • SWISSPROT/P19084
  • SWISSPROT/Q99304