Synthesis of 4-nitrophenyl acetate using molecular sieve-immobilized lipase from Bacillus coagulans.
Extracellular lipase from Bacillus coagulans BTS-3 was immobilized on (3 A x 1.5 mm) molecular sieve. The molecular sieve showed approximately 68.48% binding efficiency for lipase (specific activity 55 IU mg(-1)). The immobilized enzyme achieved approx 90% conversion of acetic acid and 4-nitrophenol (100 mM each) into 4-nitrophenyl acetate in n-heptane at 65 degrees C in 3 h. When alkane of C-chain length other than n-heptane was used as the organic solvent, the conversion of 4-nitrophenol and acetic acid was found to decrease. About 88.6% conversion of the reactants into ester was achieved when reactants were used at molar ratio of 1:1. The immobilized lipase brought about conversion of approximately 58% for esterification of 4-nitrophenol and acetic acid into 4-nitrophenyl acetate at a temperature of 65 degrees C after reuse for 5 cycles.
Raghuvanshi
Shilpa
S
Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla, 171 005, India.
Gupta
Reena
R
D019342:Acetic Acid / Q000378:metabolism; D001407:Bacillus / Q000145:classification / Q000201:enzymology* / Q000254:growth & development; D001709:Biotechnology / Q000379:methods; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004952:Esters / Q000378:metabolism; D009596:Nitrophenols / Q000378:metabolism*; D013696:Temperature
D004800:Enzymes, Immobilized; D004952:Esters; D009596:Nitrophenols; C008642:4-nitrophenyl acetate; D019342:Acetic Acid