Acta Microbiologica et Immunologica Hungarica
Volume/Issue:
Volume 53: Issue 2
Enhancement of Ethyl Propionate Synthesis by poly (AAc-co-HPMA-cl-MBAm)-immobilized  Pseudomonas aeruginosa MTCC-4713, Exposed to Hg2+ and NH4+ Ions
Authors: S. S. Kanwar 1 , H. K. Verma 2 , S. Pathak 3 , R. K. Kaushal 4 , Y. Kumar 5 , M. L. Verma 6 , S. S. Chimni 7 , and G. S. Chauhan 8
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  • 1 Department of Biotechnology, Himachal Pradesh University Summer Hill, Shimla-171 005, India
  • 2 Department of Biotechnology, Himachal Pradesh University Summer Hill, Shimla-171 005, India
  • 3 Department of Biotechnology, Himachal Pradesh University Summer Hill, Shimla-171 005, India
  • 4 Department of Biotechnology, Himachal Pradesh University Summer Hill, Shimla-171 005, India
  • 5 Department of Chemistry, Himachal Pradesh University Summer Hill, Shimla-171 005, India
  • 6 Department of Biotechnology, Himachal Pradesh University Summer Hill, Shimla-171 005, India
  • 7 Department of Chemistry, Guru Nanak Dev University Amritsar-143 005, India
  • 8 Department of Chemistry, Himachal Pradesh University Summer Hill, Shimla-171 005, India
DOI:
https://doi.org/10.1556/amicr.53.2006.2.6
Page Count:
195–207
Publication Date:
01 Jun 2006
Online Publication Date:
20 Jul 2006
Article Category:
Research Article
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A purified alkaline thermo-tolerant bacterial lipase from Pseudomonas aeruginosa MTCC-4713 was immobilized on a poly (AAc-co-HPMA-cl-MBAm) hydrogel. The hydrogel-bound lipase achieved 93.6% esterification of ethanol and propionic acid (300 mM: 100 mM) into ethyl propionate at temperature 65oC in 3 h in the presence of a molecular sieve (3 Å). In contrast, hydrogel-immobilized lipase pre-exposed to 5 mM of HgCl2 orNH4Cl resulted in approximately 97% conversion of reactants in 3 h into ethyl propionate under identical conditions. The salt-exposed hydrogel was relatively more efficient in repetitive esterification than the hydrogel- bound lipase not exposed to any of the cations. Moreover, bound lipase exposed Hg2+ or NH4+ ions showed altered specificity towards p-nitrophenyl esters and was more hydrolytic towards higher C-chain p-nitrophenyl esters (p-nitrophenyl laurate and p-nitrophenyl palmitate with C 12 and C 16 chain) than the immobilized lipase not exposed to any of the salts. The later showed greater specificity towards p-nitrophenyl caprylate (C 8).

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Cover Acta Microbiologica et Immunologica Hungarica
Acta Microbiologica et Immunologica Hungarica A Quarterly of the Hungarian Academy of Sciences
Print ISSN:
1217-8950
Online ISSN:
1588-2640
Keywords:
thermo-tolerant lipase; P. aeruginosa; immobilization; poly (AAc-co-HPMA-cl-MBAm) hydrogel; Hg2+ and NH4+ ions promoted ethyl propionate synthesis

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