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.
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http://dx.doi.org/10.1016/j.bbrc.2021.02.003 | DOI Listing |
Biochem Biophys Res Commun
March 2021
School of Pharmaceutical Sciences, Nanjing Tech University, No. 30 Puzhu South Road, Jiangbei New Area, Nanjing, 211800, China; College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, No. 30 Puzhu South Road, Jiangbei New Area, Nanjing, 211800, China. Electronic address:
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.
View Article and Find Full Text PDFRSC Adv
April 2019
College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University Nanjing 211816 China
The lipase YCJ01 from is an organic solvent-stable enzyme and its activity can be activated by a hydrophobic solvent due to the "interface activation" mechanism. The activity of lipase YCJ01 increased by 2.1-fold with -butanol as the precipitant even after cross-linking.
View Article and Find Full Text PDFInt J Biol Macromol
November 2018
School of Pharmaceutical Sciences, Nanjing Tech University, No. 30 South Puzhu Road, Nanjing 211816, People's Republic of China. Electronic address:
Lipases have wide applications using as biocatalyst in numerous biotechnological and bioengineering fields, especially function at hydrophobic or amphiphilic interface. Previously, the lipase from Burkholderia ambifaria YCJ01 was significantly activated when immobilized on the amphiphilic environment. In this work, insights into the functional effect of amphiphilic surface on lipase activation are presented by molecular dynamic simulations.
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