Protein Characterization of Protein Bodies from Cotyledons of Mucuna pruriens (L.) DC

• Published in: Plant foods for human nutrition (Dordrecht) Vol. 68; no. 1; pp. 47 - 51
• Main Authors: Bellani, Lorenza, Giglioni, Stefania, Muccifora, Simonetta
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01-03-2013; Springer
• Subjects: Albumins - analysis; Albumins - metabolism; Biological and medical sciences; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Cotyledon - chemistry; Cotyledon - metabolism; Dietary Proteins - analysis; Ecology; Feeding. Feeding behavior; Food Science; Fundamental and applied biological sciences. Psychology; Globulins - analysis; Globulins - metabolism; Glutens - analysis; Glutens - metabolism; Microscopy, Electron, Scanning; Molecular Weight; Mucuna - chemistry; Mucuna - metabolism; Nutrition; Original Paper; Phenylpropanolamine - analysis; Phenylpropanolamine - metabolism; Plant Physiology; Seed Storage Proteins - analysis; Seed Storage Proteins - metabolism; Vertebrates: anatomy and physiology, studies on body, several organs or systems; SDS-PAGE; Protein bodies; (L.) DC; Seed proteins; Seeds; Nutrition; Biochemical compound; Mucuna; Mucuna pruriens (L.)DC; Protein; Characterization; Leguminosae; Dicotyledones; Seed; Angiospermae; Plant origin; Spermatophyta
• ISSN: 0921-9668; 1573-9104
• DOI: 10.1007/s11130-012-0331-z

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.