TY - JOUR
T1 - Specific immobilization of lipase on functionalized 3D printing scaffolds via enhanced hydrophobic interaction for efficient resolution of racemic 1-indanol
AU - Zhang, Jingxuan
AU - Gao, Bingbing
AU - Lv, Kai
AU - Kumissay, Lot
AU - Wu, Bin
AU - Chu, Jianlin
AU - He, Bingfang
N1 - Publisher Copyright:
© 2021
PY - 2021/3/26
Y1 - 2021/3/26
N2 - Lipase immobilization with hydrophobic interaction is of interesting exploration, and some functionalized groups on supports are special for activity increasing. To achieved a good performance of cost-effective immobilization on macro-supports for feasible usage and recycle, eco-friendly PLA-based 3D printing macro-scaffolds with fabrication was designed, and phenyl groups with different length of linkers and combined two kinds of groups were anchored for lipase YCJ01 binding with improving payload, the highest enzyme expression of 2227.5 U/g, activity recovery of 137.3%, and increasing specific activity of 815.9 U/mg were attained by using PLA@AMTS-C7-Ph/PLA@AMTS-C9-Ph scaffolds as carries. The immobilized lipase YCJ01 on bifunctionalized 3D printing scaffolds was further applied to the efficient resolution of racemic 1-indanol (267 mM) with high stereoselectivity using a binary solvent system. The immobilized lipase YCJ01 could control the over transesterification of (S)-1-indanol and exhibit good operational stability of repetitive usage for 9 cycles. This is beneficial to obtain the high enantiomerical pure product by feasible separation of immobilized biocatalyst without rigorous operation.
AB - Lipase immobilization with hydrophobic interaction is of interesting exploration, and some functionalized groups on supports are special for activity increasing. To achieved a good performance of cost-effective immobilization on macro-supports for feasible usage and recycle, eco-friendly PLA-based 3D printing macro-scaffolds with fabrication was designed, and phenyl groups with different length of linkers and combined two kinds of groups were anchored for lipase YCJ01 binding with improving payload, the highest enzyme expression of 2227.5 U/g, activity recovery of 137.3%, and increasing specific activity of 815.9 U/mg were attained by using PLA@AMTS-C7-Ph/PLA@AMTS-C9-Ph scaffolds as carries. The immobilized lipase YCJ01 on bifunctionalized 3D printing scaffolds was further applied to the efficient resolution of racemic 1-indanol (267 mM) with high stereoselectivity using a binary solvent system. The immobilized lipase YCJ01 could control the over transesterification of (S)-1-indanol and exhibit good operational stability of repetitive usage for 9 cycles. This is beneficial to obtain the high enantiomerical pure product by feasible separation of immobilized biocatalyst without rigorous operation.
KW - Functionalized 3D-printed scaffolds
KW - Hydrophobic interaction
KW - Lipase
KW - Racemic 1-indanol
KW - Specific immobilization
UR - http://www.scopus.com/inward/record.url?scp=85101794320&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2021.02.003
DO - 10.1016/j.bbrc.2021.02.003
M3 - 文章
C2 - 33582553
AN - SCOPUS:85101794320
SN - 0006-291X
VL - 546
SP - 111
EP - 117
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
ER -