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A kinetic study on the Novozyme 435-catalyzed esterification of free fatty acids with octanol to produce octyl esters
Published in John Wiley and Sons Inc.
PMID: 26334440
Volume: 31
Issue: 6
Pages: 1494 - 1499
Octyl esters can serve as an important class of biolubricant components replacing their mineral oil counterparts. The purpose of the current work was to investigate the enzymatic esterification reaction of free fatty acids (FFA, from waste cooking oil) with octanol in a solvent-free system using a commercial lipase Novozyme 435. It was found that the esterificaton reaction followed the Ping-pong bi-bi kinetics with no inhibition by substrates or products within the studied concentration range. The maximum reaction rate was estimated to be 0.041 mol L-1 g-1 h-1. Additionally, the stability of Novozyme 435 in the current reaction system was studied by determining its activity and final conversion of FFA to esters after 12 successive utilizations. Novozyme 435 exhibited almost 100% enzyme activity up to 7 cycles of reaction and gradually decreased (by 5%) thereafter. The kinetic parameters evaluated from the study shall assist in the design of reactors for large-scale production of octyl esters from a cheap biomass source. The enzyme reusability data can further facilitate mass production by curtailing the cost of expensive enzyme consumption. © 2015 American Institute of Chemical Engineers Biotechnol. Prog., 31:1494-1499, 2015 © 2015 American Institute of Chemical Engineers.
About the journal
JournalData powered by TypesetBiotechnology Progress
PublisherData powered by TypesetJohn Wiley and Sons Inc.
Open AccessNo