TY - JOUR
T1 - Activation of crosslinked lipases in mesoporous silica via lid opening for recyclable biodiesel production
AU - Zhang, Meiling
AU - Jun, Seung Hyun
AU - Wee, Youngho
AU - Kim, Han Sol
AU - Hwang, Ee Taek
AU - Shim, Jongmin
AU - Hwang, Sang Youn
AU - Lee, Jinwoo
AU - Kim, Jungbae
N1 - Funding Information:
This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MSIT) ( NRF-2020R1A2C3009649 ), and Green Fusion Technology Program funded by Ministry of Environment .
Publisher Copyright:
© 2022 Elsevier B.V.
PY - 2022/12/1
Y1 - 2022/12/1
N2 - Lipases catalyze a wide range of industrially important reactions, including the transesterification of triglycerides with alcohols for biodiesel production, and the stabilization of lipases are critical to achieve their recycled uses. Here, nanoscale enzyme reactor (NER) of lipase from Rhizopus oryzae (LP) was prepared via a simple two-step process, comprising of enzyme adsorption into magnetically-separable mesoporous silica and follow-up crosslinking of adsorbed enzymes. In aqueous phase, the specific hydrolysis activity of NER-LP was 4.7 times lower than that of free LP. On the other hand, however, the specific transesterification activity of NER-LP (130.4 μmol/min/mg LP) in organic phase for biodiesel production was 50 times higher than that of free LP (2.6 μmol/min/mg LP). These results reveal that the enzyme crosslinking for the preparation of NER does not interfere with the interfacial activation of LP molecules, opening the lid of LP active site under an optimal hydrophobic environment provided by the combination of organic solvent and mesoporous silica. Magnetic separation and optimized washing protocol facilitated the recycled uses of NER-LP. Highly stable and active NER-LP in magnetically-separable mesoporous silica has demonstrated its great potentials as an environmentally-friendly nanobiocatalyst for various lipase applications, including plasticizers, biosurfactants, functional fatty acids, as well as recyclable biodiesel production.
AB - Lipases catalyze a wide range of industrially important reactions, including the transesterification of triglycerides with alcohols for biodiesel production, and the stabilization of lipases are critical to achieve their recycled uses. Here, nanoscale enzyme reactor (NER) of lipase from Rhizopus oryzae (LP) was prepared via a simple two-step process, comprising of enzyme adsorption into magnetically-separable mesoporous silica and follow-up crosslinking of adsorbed enzymes. In aqueous phase, the specific hydrolysis activity of NER-LP was 4.7 times lower than that of free LP. On the other hand, however, the specific transesterification activity of NER-LP (130.4 μmol/min/mg LP) in organic phase for biodiesel production was 50 times higher than that of free LP (2.6 μmol/min/mg LP). These results reveal that the enzyme crosslinking for the preparation of NER does not interfere with the interfacial activation of LP molecules, opening the lid of LP active site under an optimal hydrophobic environment provided by the combination of organic solvent and mesoporous silica. Magnetic separation and optimized washing protocol facilitated the recycled uses of NER-LP. Highly stable and active NER-LP in magnetically-separable mesoporous silica has demonstrated its great potentials as an environmentally-friendly nanobiocatalyst for various lipase applications, including plasticizers, biosurfactants, functional fatty acids, as well as recyclable biodiesel production.
KW - Enzyme stabilization
KW - Lipase lid opening
KW - Lipase-catalyzed transesterification
KW - Mesoporous silica
KW - Nanoscale enzyme reactors
UR - http://www.scopus.com/inward/record.url?scp=85139876777&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2022.10.023
DO - 10.1016/j.ijbiomac.2022.10.023
M3 - Article
C2 - 36216105
AN - SCOPUS:85139876777
SN - 0141-8130
VL - 222
SP - 2368
EP - 2374
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -