Abstract

by Vijay
(Shimal, India)

Original Text: Abstract

The synthesis of benzyl acetate by transesterification catalyzed by non-commercial immobilized lipase from Rhizopus oryzae NRRL 3562 was studied in solvent free condition. The effect of different transesterification variables namely acyl donor, molarity of alcohol, reaction time, temperature, agitation, addition of water and enzyme amount on molar conversion (%) was investigated. The maximum molar conversion of 96% was obtained with the transesterification variables of 0.5 M benzyl alcohol in vinyl acetate, reaction time of 12 h, agitation speed of 200 rpm, with 12% immobilized enzyme at 40 oC. The immobilized lipase has withstands more than 98 % relative activity up to six recycles and reduces to 50 % relative activity after 12 recycles. The Km and Vmax values were determined to be 310 mM and 0.10 mmol h-1g-1, respectively, for n-benzyl acetate.

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Revised Text:

The synthesis of benzyl acetate by transesterification catalyzed by non-commercial immobilized lipase from Rhizopus oryzae NRRL 3562 was studied in a solvent free condition. The effect of different transesterification variables, namely acyl donor, molarity of alcohol, reaction time, temperature, agitation, addition of water and enzyme amount on molar conversion (%), was investigated.

The maximum molar conversion of 96% was obtained with the transesterification variables of 0.5 M benzyl alcohol in vinyl acetate, reaction time of 12 h, agitation speed of 200 rpm, with 12% immobilized enzyme at 40 oC. The immobilized lipase withstands more than 98% relative activity up to six recycles and reduces to 50% relative activity after 12 recycles.

The Km and Vmax values were determined to be 310 mM and 0.10 mmol h-1g-1, respectively, for n-benzyl acetate.

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