Details

Autor(en) / Beteiligte

• Wu, Shuhui
• Zhang, Panliang
• Sun, Bizhu
• Wu, Ying
• Huang, Meiai
• Luo, Zhuolin
• Ma, Yingnan
• Tang, Kewen

Titel

Polyethyleneimine-MOF composite as a support for immobilization of lipase with enhanced activity in kinetic resolution

Ist Teil von

• Applied catalysis. A, General, 2023-07, Vol.661, p.119232, Article 119232

Ort / Verlag

Elsevier B.V

Erscheinungsjahr

2023

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Lipase PS from Pseudomonas cepacia was steadily immobilized on a new support prepared with metal-organic framework (MOF) and polyethyleneimine (PEI) through a PEI-boosted strategy (PS@MOF-5-PEI). Evaluated by the enantioselective transesterification reaction of racemic 1-(4-(trifluoromethyl) phenyl) ethanol (TFMP) with vinyl acetate, PS@MOF-5-PEI expressed more than 10 times of increase in specific activity (U/mg protein) compared with free lipase PS. PS@MOF-5-PEI had an enhanced enzyme-substrate affinity and catalytic efficiency than free lipase PS, as supported by a lower apparent Km value (7.3 vs 11.3 mM) and an increased Vmax/Km value (0.38 vs 0.05 min−1), respectively. Under the optimal conditions involving 45 °C, substrate ratio of 1:18, enzyme dosage of 20 mg and reaction time of 60 min, the ees of 99.8% and c of 50.1% for kinetic resolution of TFMP enantiomers were achieved with PS@MOF-5-PEI, which can be recycled for 10 times without significant loss in activity and with enantioselectivity well maintained. [Display omitted] •Polyethyleneimine-introduced polymer-MOF composite for lipase immobilization.•Sought after products obtained in more than 99% optical purity.•Enhanced activity as compared to the commercial lipase preparation.•Improved tolerance to organic solvents.•Biocatalyst retains 92% of initial conversion after 10 cycles of reuse.