The buffer solution plays a major role in protein stability and activity, thereby making the selection of a buffer to achievemaximum activity for a protein will be a formidable challenge. The present work constitutes
an extension of this investigation to esterases from germinated Jatrophacurcas seeds. The 0.1 M NaCl solution, 0.1 M phosphate buffer pH7.0, 0.1 M citrate buffer pH 5.0 and 0.1 M Tris-HCl buffer pH 8.5, 0.1 M NaOH and distill water were used to extract protein from germinated Jatrophacurcas
seeds. The esterase activity and specific activity for NaCl solution, phosphatebuffer, citrate buffer, Tris-HCl buffer, NaOH and Distilled water was 9.07, 8.6, 8.2, 6.46, 0.07 and 4.98 μmoles/min/gm
and 0.09258, 0.0905, 0.088, 0.0715 0.0003 and 0.081 IU/mg, respectively.The Native-PAGE analysis showed the esterase
enzyme activity in different extraction buffer.Among 13 esterase bands, 8 esterolytic bands were major bands
(band no 1,3, 6, 7, 8, 11, 12 and 13)and remaining were minor bands.The amount of proteins and esterase activity were found to bethe highest when extracted with 0.1 M NaCl solution
