TY - JOUR
T1 - Regulation of Microenvironments of Hydrogen-Bonded Organic Frameworks for Enhanced Enzyme Activity of Phosphotriesterase
AU - Wu, Feier
AU - Li, Peiyan
AU - Guo, Yixuan
AU - Du, Changsheng
AU - Li, Peng
N1 - Publisher Copyright:
© 2026 by the authors.
PY - 2026/5
Y1 - 2026/5
N2 - The microenvironment of the porous channels in enzyme immobilization carriers critically determines the catalytic performance of immobilized enzymes. In this study, we systematically tuned the hydrophobicity/hydrophilicity of the channel microenvironment of hydrogen-bonded organic frameworks (HOFs) by introducing four different substituents (-CH3, -Cl, -F, -NH2) at the 2-position of the phenyl ring of the HOF-101 monomer. These HOF-101 derivatives, which are isostructural to the parent HOF-101, were used to immobilize phosphotriesterase (PTE). The enzyme loading efficiencies ranged from 64.7% to 70.7%, indicating that the substituents had little effect on PTE binding, which primarily relies on carboxyl-residue interactions. Kinetic studies revealed that the hydrophilic -NH2-functionalized HOF-101 (PTE@HOF-101-NH2) exhibited the highest catalytic efficiency (1.43 × 108 M−1 s−1), 2.27 times that of free PTE, while the hydrophobic -CH3 analogue showed reduced activity. Notably, PTE@HOF-101-F demonstrated superior acid resistance (70% relative activity at pH 2) and long-term thermal stability (70% activity retention after 6 h at 70 °C), outperforming other derivatives. In contrast, PTE@HOF-101-NH2 showed the highest activity under mild conditions but suffered from framework dissolution under prolonged harsh treatments. This work demonstrates that fine-tuning the HOF channel microenvironment is an effective strategy to enhance enzyme activity and stability, providing a platform for designing advanced immobilized enzyme systems.
AB - The microenvironment of the porous channels in enzyme immobilization carriers critically determines the catalytic performance of immobilized enzymes. In this study, we systematically tuned the hydrophobicity/hydrophilicity of the channel microenvironment of hydrogen-bonded organic frameworks (HOFs) by introducing four different substituents (-CH3, -Cl, -F, -NH2) at the 2-position of the phenyl ring of the HOF-101 monomer. These HOF-101 derivatives, which are isostructural to the parent HOF-101, were used to immobilize phosphotriesterase (PTE). The enzyme loading efficiencies ranged from 64.7% to 70.7%, indicating that the substituents had little effect on PTE binding, which primarily relies on carboxyl-residue interactions. Kinetic studies revealed that the hydrophilic -NH2-functionalized HOF-101 (PTE@HOF-101-NH2) exhibited the highest catalytic efficiency (1.43 × 108 M−1 s−1), 2.27 times that of free PTE, while the hydrophobic -CH3 analogue showed reduced activity. Notably, PTE@HOF-101-F demonstrated superior acid resistance (70% relative activity at pH 2) and long-term thermal stability (70% activity retention after 6 h at 70 °C), outperforming other derivatives. In contrast, PTE@HOF-101-NH2 showed the highest activity under mild conditions but suffered from framework dissolution under prolonged harsh treatments. This work demonstrates that fine-tuning the HOF channel microenvironment is an effective strategy to enhance enzyme activity and stability, providing a platform for designing advanced immobilized enzyme systems.
KW - catalytic efficiency
KW - enzyme immobilization
KW - hydrogen-bonded organic frameworks
KW - microenvironment regulation
KW - phosphotriesterase
UR - https://www.scopus.com/pages/publications/105040242138
U2 - 10.3390/molecules31101651
DO - 10.3390/molecules31101651
M3 - 文章
C2 - 42197205
AN - SCOPUS:105040242138
SN - 1420-3049
VL - 31
JO - Molecules
JF - Molecules
IS - 10
M1 - 1651
ER -