Esterase Activity from the Germinated Jatropha curcas Seeds in Different Extraction buffers.


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Subramani, T. and Manjunath, K.C. and Siddalinga Murthy, K.R. and Ramachandra Swamy, N. (2012) Esterase Activity from the Germinated Jatropha curcas Seeds in Different Extraction buffers. International Journal of Science and Nature, 03 (01). pp. 173-175. ISSN 2229 – 6441


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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.

Item Type: Article
Uncontrolled Keywords: Phosphate; Citrate;Tris-Hcl;Nacl;Esterases;Jatropha Curcas
Subjects: Faculty of Science > Environmental and Biological Sciences > Biochemistry
Faculty of Science > Pure Sciences > Chemistry
Divisions: Jnana Bharathi / Central College Campus > Department of Biochemistry
Depositing User: Mr. Narayanaswamy B V
Date Deposited: 25 Jun 2016 08:22
Last Modified: 25 Jun 2016 08:22

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