BackgroundEnzyme immobilization is efficient tool to reduce enzymatic processes cost and improve catalyst stability. The enzymatic catalytic transesterification reaction of castor oil was studied for the production of biodiesel. In this research, castor seeds oil was extracted and used along with methanol as substrates for enzymatic transesterification reaction. Porcine pancreatic lipase (PPL) immobilized on calcium alginate (Ca-Alg) and mesoporous SBA-15 supports identified, and its potential was investigated for used as the reaction catalyst.ResultsThe mesoporous SBA-15 supports with a high specific surface area (519.25 m2/g) and the pore diameter (83.2 Å) was suitable for immobilization of the PPL with 4.6⨯2.6⨯1.1 nm3 dimensions. The effect of temperature, biocatalyst concentration, methanol/oil molar ratio and water content on biodiesel conversion were investigated in presents of PPL immobilized on mesoporous SBA-15-OH-NH2-GA. The biodiesel conversion in the presence of PPL immobilized on SBA-15-OH-NH2-GA and Ca-Alg was calculated 88.6% and 77.65% in optimal conditions respectively. Conclusions The result indicate that castor plant has a very high potential for use in the future of the biodiesel industry as a substrate for transesterification reaction. The biodiesel production efficiency is higher when the PPL is immobilized on the SBA-15-OH-NH2-GA toward than conditions that immobilized on the Ca-Alg.