The paper is from J. Am. Chem. Soc. 2024, completed by Professor Gangfeng Ouyang from Sun Yatsen University and coworkers.

Abstract 
1) The article discusses the use of nanocarriers for immobilizing fragile enzymes, enhancing their stability and recyclability compared to free enzymes.
2) It acknowledges the common issue where immobilized enzymes lose catalytic activity due to mass transfer limitations and conformational changes.
3) Introduces a synergistic approach using metal-organic frameworks (MOFs) to enhance both stability and activity of the enzyme lipase by trapping it within a hierarchically porous structure.
4) Highlights the use of fatty acids to modify the mesopore channels, activating the enzyme through hydrophobic interactions.
5) Demonstrates that the modified enzyme shows 1.57 and 2.46 times the activity of native lipase in ester hydrolysis and enantioselective catalysis, respectively.

Background
1) Industry Problems: The paper addresses the challenge of enzyme immobilization, which often results in reduced catalytic activity due to mass transfer issues and conformational changes.
2) Previous Research: Other scholars have proposed various immobilization methods, such as adsorption, covalent bonding, and embedding, with MOFs being a favored choice due to their structural advantages.
3) Innovations by Authors: The authors propose a novel strategy of pore compartmentalization and hydrophobization in MOFs to overcome the limitations of enzyme immobilization, offering a dual benefit of stability and activity enhancement.

Experimental Details
1) Selection of MOF: The authors chose the zirconium-based NU-1003 MOF for its water stability, large mesopores suitable for hosting the enzyme, and feasibility for chemical microenvironment engineering.
2) Immobilization Method: Enzyme was loaded into the MOF through a postpermeation strategy, retaining the crystallinity and allowing for precise chemical modification of the pore walls.
3) Activity Assessment: The hydrolytic activity of the immobilized enzyme was evaluated using p-nitrophenyl palmitate (p-NPP) as a substrate, showing improved accessibility and activity compared to enzymes immobilized in single-pore structures.

Test and Analysis
1) Powder X-ray Diffraction (PXRD): Confirmed the successful synthesis of NU-1003 and its modified versions, maintaining crystallinity post-modification.
2) Scanning Electron Microscopy (SEM): Showed that all modified MOFs retained their rod-like nanostructures.
3) Fourier Transform Infrared Spectroscopy (FT-IR): Demonstrated successful enzyme loading and chemical modification on the MOF pore walls.
4) Nitrogen Adsorption/Desorption Isotherms: Indicated the presence of hierarchical pores and the effect of enzyme loading on pore volume.
5) Thermogravimetric Analysis (TGA): Provided evidence of the presence of modified fatty acids by observing weight loss due to pyrolysis.

Conclusion
1) The paper concludes that the MOF pore-engineering strategy effectively enhances the stability and activity of the enzyme.
2) The immobilized enzyme demonstrated superior performance in ester hydrolysis and enantioselective catalysis compared to native enzymes.
3) The biocatalyst's potential for kinetic resolution of enantiomers was validated, showing higher efficiency than native enzymes.
4) The paper could further explore the long-term stability of the immobilized enzyme under various conditions.

A Synergetic Pore Compartmentalization and Hydrophobization Strategy for Synchronously Boosting the Stability and Activity of Enzyme
Lihong Guo, Rongwei He, Guosheng Chen*, Huangsheng Yang, Xiaoxue Kou, Wei Huang, Rui Gao*, Shuyao Huang*, Siming Huang*, Fang Zhu, and Gangfeng Ouyang*
DOI：10.1021/jacs.4c03286
Link: https://pubs.acs.org/doi/10.1021/jacs.4c03286