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ABSTRACT: Abstract
The present study scrutinizes lipases of different origins, immobilization methods, carriers, and reaction solvents to accelerate the octyl octanoate synthesis. The acylation reaction parameters including temperature, moisture level, shaking speed and enzyme dose were subsequently investigated and optimized following fully rotatable central composite design. The initial screening revealed that lipases of Rhizopus arrhizus, when applied as a biocatalyst (lipase bearing dead mycelia) furnished the highest acylation activity (147 μM L-1 min-1). Validation of reaction conditions disclosed that 250 I.U. of lipase based biocatalyst when incubated with 850 mM of acylating agent and 750 mM of the substrate at 35 °C, 3% moisture level and 150 RPM shakin
SUBMITTER: Rashid A
PROVIDER: S-EPMC6233414 | biostudies-literature | 2018 Dec
REPOSITORIES: biostudies-literature