Acetone powder from dormant seeds of Ricinus communis L: lipase activity and presence of toxic and allergenic compounds.
The influence of several factors on the hydrolytic activity of lipase, present in the acetone powder from dormant castor seeds (Ricinus communis) was evaluated. The enzyme showed a marked specificity for short-chain substrates. The best reaction conditions were an acid medium, Triton X-100 as the emulsifying agent and a temperature of 30 degrees C. The lipase activity of the acetone powder of different castor oil genotypes showed great variability and storage stability of up to 90%. The toxicology analysis of the acetone powder from genotype Nordestina BRS 149 showed a higher ricin (toxic component) content, a lower 2S albumin (allergenic compound) content, and similar allergenic potential compared with untreated seeds.
Cavalcanti
Elisa D C
ED
Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
Maciel
Fábio M
FM
Villeneuve
Pierre
P
Lago
Regina C A
RC
Machado
Olga L T
OL
Freire
Denise M G
DM
D055516:2S Albumins, Plant; D000096:Acetone / Q000737:chemistry*; D000485:Allergens / Q000737:chemistry*; D052179:Antigens, Plant / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D008049:Lipase / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011208:Powders; D012276:Ricin / Q000737:chemistry*; D012278:Ricinus / Q000201:enzymology*; D012639:Seeds / Q000201:enzymology*
D055516:2S Albumins, Plant; C541551:2S storage protein, Ricinus communis; D000485:Allergens; D052179:Antigens, Plant; D010940:Plant Proteins; D011208:Powders; D000096:Acetone; D012276:Ricin; D008049:Lipase