| Literature DB >> 27580160 |
Hongming He1, Haobo Han2, Hui Shi2, Yuyang Tian1, Fuxing Sun1, Yang Song1, Quanshun Li2, Guangshan Zhu1.
Abstract
Enhancing the activity and stability of enzymes and improving their reusability are critical challenges in the field of enzyme immobilization. Here we report a facile and efficient biomimetic mineralization to embed thermophilic lipase QLM in zeolite imidazolate framework-8 (ZIF-8). Systematic characterization indicated that the entrapment of lipase molecules was successfully achieved during the crystal growth of ZIF-8 with an enzyme loading of ∼72.2 ± 1.88 mg/g lipase@ZIF-8, and the enzymes could facilitate the construction of framework building blocks. Then the composite lipase@ZIF-8 was observed to possess favorable catalytic activity and stability in the ester hydrolysis, using the hydrolysis of p-nitrophenyl caprylate as a model. Finally, the composite was successfully applied in the kinetic resolution of (R,S)-2-octanol, with favorable catalytic activity and enantioselectivity during 10 cycle reactions. Thus, the biomimetic mineralization process can be potentially used as an effective technique for realizing the entrapment of biomacromolecules and constructing efficient catalysts for industrial biocatalysis.Entities:
Keywords: biomimetic mineralization; ester hydrolysis; kinetic resolution; metal−organic frameworks; thermophilic lipase
Year: 2016 PMID: 27580160 DOI: 10.1021/acsami.6b05538
Source DB: PubMed Journal: ACS Appl Mater Interfaces ISSN: 1944-8244 Impact factor: 9.229