Original scientific paper
https://doi.org/10.15255/CABEQ.2023.2205
Enhanced Esterification Activity and Thermostability of Imprinted Poly(Ethylene Glycol)-Lipase Complex
M. Matsumoto
orcid.org/0000-0001-6879-1150
; Department of Chemical Engineering and Materials Science, Doshisha University, Kyotanabe, Kyoto 610-0321, Japan
Y. Tahara
; Department of Chemical Engineering and Materials Science, Doshisha University, Kyotanabe, Kyoto 610-0321, Japan
Abstract
Although the range of applications for enzymatic reactions in organic solvents is rapidly expanding, this study focused on the enzymatic activity in the esterification of lauric acid with benzyl alcohol, and thermostability of lipase using poly(ethylene glycol) (PEG)-lipase complex and molecular imprinting techniques. The catalytic activity was enhanced through molecular imprinting and the PEG-lipase complex. The imprinting operation was particularly effective for catalytic activity after forming the PEG-lipase complex. The kinetic analysis of the lipase-catalyzed esterification revealed that the increase in esterification rate with imprinted lipases was mainly due to the higher maximum rate achieved by the system. The thermostability of the lipases was significantly improved by imprinting at all temperatures (50~70 °C). After forming a PEG-lipase complex, the imprinted lipase exhibited much higher reactivity and thermostability compared to the native lipase and the imprinted PEG-lipase complex.
This work is licensed under a Creative Commons Attribution 4.0 International License.
Keywords
lipase; imprinting; PEG-lipase complex; thermostability
Hrčak ID:
313511
URI
Publication date:
19.1.2024.
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