Protein characterization of protein bodies from cotyledons of Mucuna pruriens (L.) DC

Plant Foods Hum Nutr. 2013 Mar;68(1):47-51. doi: 10.1007/s11130-012-0331-z.

Abstract

Seeds of Mucuna pruriens (L.) DC. (Fabaceae) were analyzed for protein composition of protein bodies isolated from cotyledons. Protein bodies were successfully separated by Lympholyte and those of dry seeds, observed by scanning electron microscope, were elliptical or spherical in shape with a diameter of 5-12 μm. Protein content in dry seed protein bodies was 10.6 mg/g dry weight. Globulin was the largest protein fraction isolated (62.5 %), followed by albumin (18.3 %), glutelin (15.8 %) and prolamin (3.4 %). The prolamin fraction and high glutelin content are uncommon in legumes. SDS-PAGE of albumins, globulins, prolamins and glutelins provided different band numbers and molecular weights under reducing and non reducing conditions and suggested that the albumin fraction is rich in disulphide bonds.

MeSH terms

  • Albumins / analysis*
  • Albumins / metabolism
  • Cotyledon / chemistry*
  • Cotyledon / metabolism
  • Dietary Proteins / analysis
  • Globulins / analysis*
  • Globulins / metabolism
  • Glutens / analysis*
  • Glutens / metabolism
  • Microscopy, Electron, Scanning
  • Molecular Weight
  • Mucuna / chemistry*
  • Mucuna / metabolism
  • Phenylpropanolamine / analysis*
  • Phenylpropanolamine / metabolism
  • Seed Storage Proteins / analysis*
  • Seed Storage Proteins / metabolism

Substances

  • Albumins
  • Dietary Proteins
  • Globulins
  • Seed Storage Proteins
  • Phenylpropanolamine
  • Glutens