Enzymatic methanolysis reaction of canola oil using capillary channel reactor: Determination of the kinetic constants-involved

Publication date: Available online 29 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Alireza Habibi, Sepideh Fahim, Nooshin Shirvani, Masoud Rahimi Enzymatic methanolysis reaction of canola oil utilizing Candida rugosa lipase in a solvent free system was studied in a shake flask as well as capillary channel reactors. The results demonstrated that pretreatment of the enzyme with the substrate, increased the stability of the enzyme by 21.2% during the methanolysis reaction. Performance of a capillary-channel reactor improved the yield of methanolysis up to 4-fold when compared with the shake flask experiments. Bio-kinetic constants were estimated using the Ping-Pong model by considering the competitive and non-competitive inhibition roles of methanol on enzymatic methanolysis reaction. The results of the kinetics studies showed that the enzymatic methanolysis reaction was best described by the competitive inhibition Ping-Pong model with the maximum enzyme activity of 170368μmolmin−1 genzyme −1, the inhibition constant of methanol 0.826molgenzyme −1, the dissociation constant of canola oil 0.137molgenzyme −1, and methanol dissociation constant 1.081molgenzyme −1. Graphical abstract
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research
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