Rapid In Situ Immobilization of Enzymes in Metal–Organic Framework Supports under Mild Conditions

Gascón, Victoria; Carucci, Cristina; Jiménez, Mayra B.; Blanco, Rosa M.; Sánchez‐Sánchez, Manuel; Magner, Edmond

doi:10.1002/cctc.201601342

Cited by 66 publications

(83 citation statements)

References 34 publications

(17 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although enzyme immobilization can sometimes result in decreased catalytic activity, the obtained specific activities of the immobilized lipases are comparable to that of the free lipase. The highest specific activity was obtained for Lip@ZIF‐zni (Figure ).…”

Section: Resultssupporting

confidence: 59%

Lipase and Laccase Encapsulated on Zeolite Imidazolate Framework: Enzyme Activity and Stability from Voltammetric Measurements

et al. 2018

Self Cite

View full text Add to dashboard Cite

Lipase (Pseudomonas fluorescens) and laccase (Trametates versicolor) were encapsulated on two zeolite imidazolate framework, ZIF‐8 and ZIF‐zni, materials using a one‐pot synthesis‐immobilization method in aqueous solution at room temperature. The synthesized immobilized biocatalysts (Lip@ZIF‐8, Lip@ZIF‐zni, Lac@ZIF‐8, and Lac@ZIF‐zni) were characterized by X‐ray diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy, and thermogravimetric analysis. The enzymatic activities of the four immobilized biocatalysts were characterized via the electrochemical detection of the substrates, p‐nitrophenyl butyrate and 2,2‐azinobis‐3‐ethylbenzthiazoline‐6‐sulfonic acid. For Lip@ZIF‐8 the specific activity was 91.9 U mg−1 and 123.1 U mg−1 for Lip@ZIF‐zni, while for Lac@ZIF‐8 and Lac@ZIF‐zni, the activity was 51 U mg−1 and 163 U mg−1, respectively, confirming that laccase retains a higher level of activity when immobilized onto ZIF‐zni than on ZIF‐8. Lac@ZIF‐8 was the most stable system on storage (15 days at 5 °C), retaining 94 % of initial activity, while Lip@ZIF‐zni biocatalyst had the optimal level of reusability, retaining 40 % of initial activity after five reaction cycles.

show abstract

Section: Resultssupporting

confidence: 59%

Lipase and Laccase Encapsulated on Zeolite Imidazolate Framework: Enzyme Activity and Stability from Voltammetric Measurements

et al. 2018

Self Cite

View full text Add to dashboard Cite

show abstract

“…The peak intensity decreased with increasing concentration of bovine serum albumin (BSA) . The XRD patterns of AK@ZIF‐8 and RM@ZIF‐8 samples showed different peak intensities (Figure A–B), suggesting an interaction between the enzyme molecules and the ZIF‐8 material . These findings demonstrate that the formation of pure ZIF‐8 and lipase@ZIF‐8 structures in aqueous solution is a complex process.…”

Section: Resultsmentioning

confidence: 87%

“…This was previously observed for other enzyme@ZIF‐8 . The decrease in surface area for lipase@ZIF‐8 (Table ) is likely due to enzyme encapsulation into the ZIF‐8 structure . The N 2 adsorption/desorption isotherms obtained for the samples synthesized with the low Zn/L (1:4) ratio (Figure D) are significantly different.…”

Section: Resultsmentioning

confidence: 99%

“…Between 230–500 °C, the decomposition of the enzymes occurs with mass losses of 7.3 % and 11.4 % for AK@ZIF‐8 LR and RM@ZIF‐8 LR , respectively. The diversity in shape in Figure C–D are due to the different synthesis conditions …”

Section: Resultsmentioning

confidence: 99%

“…Very recently, Gascòn et al. immobilized lipase B from Candida antarctica on Basolite F‐300 like materials . Cao et al.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Lipase Encapsulation onto ZIF‐8: A Comparison between Biocatalysts Obtained at Low and High Zinc/2‐Methylimidazole Molar Ratio in Aqueous Medium

et al. 2018

Self Cite

View full text Add to dashboard Cite

Lipase AK from Pseudomonas fluorescens and Lipase RM from Rhizomucor miehei were encapsulated into a zeolite imidazolate framework (ZIF‐8) by a “one‐pot” synthesis to obtain AK@ZIF‐8 and RM@ZIF‐8 biocatalysts. The effect of a high (1:40) and low (1:4) Zn/2‐methylimidazole molar ratio on the biocatalysts synthesis was investigated. The different Zn/ligand (L) ratios affected both the surface area, the loading, and the specific activity of the biocatalysts. Samples synthesized by using a high Zn/L ratio had high values of surface area whereas those obtained by using a low Zn/L ratio had higher loadings and specific activities. The decrease of pH (from 11.6 to 9.4) during the synthesis at high Zn/L ratio produced ZIF‐8 samples with features similar to those observed for low Zn/L ratio samples. The low Zn/L (1:4) ratio AK@ZIF‐8 biocatalyst retained 99 % activity after storage for 15 days at 5 °C and 40 % activity after five reaction cycles.

show abstract

Boosted Enzyme Activity via Encapsulation within Metal–Organic Frameworks with Pores Matching Enzyme Size and Shape

Liu,

Chen,

Wang

et al. 2024

Advanced Science

View full text Add to dashboard Cite

A novel and versatile approach called “physical imprinting” is introduced to modulate enzyme conformation using mesoporous materials, addressing challenges in achieving improved enzyme activity and stability. Metal–organic frameworks with tailored mesopores, precisely matching enzyme size and shape, are synthesized. Remarkably, enzymes encapsulated within these customized mesopores exhibit over 1670% relative activity compared to free enzymes, maintaining outstanding efficiency even under harsh conditions such as heat, exposure to organic solvents, wide‐ranging pH extremes from acidic to alkaline, and exposure to a digestion cocktail. After 18 consecutive cycles of use, the immobilized enzymes retain 80% of their initial activity. Additionally, the encapsulated enzymes exhibit a substantial increase in catalytic efficiency, with a 14.1‐fold enhancement in kcat/KM compared to native enzymes. This enhancement is among the highest reported for immobilized enzymes. The improved enzyme activity and stability are corroborated by solid‐state UV–vis, electron paramagnetic resonance, Fourier‐transform infrared spectroscopy, and solid‐state NMR spectroscopy. The findings not only offer valuable insights into the crucial role of size and shape complementarity within confined microenvironments but also establish a new pathway for developing solid carriers capable of enhancing enzyme activity and stability.

show abstract

Rapid In Situ Immobilization of Enzymes in Metal–Organic Framework Supports under Mild Conditions

Cited by 66 publications

References 34 publications

Lipase and Laccase Encapsulated on Zeolite Imidazolate Framework: Enzyme Activity and Stability from Voltammetric Measurements

Lipase and Laccase Encapsulated on Zeolite Imidazolate Framework: Enzyme Activity and Stability from Voltammetric Measurements

Lipase Encapsulation onto ZIF‐8: A Comparison between Biocatalysts Obtained at Low and High Zinc/2‐Methylimidazole Molar Ratio in Aqueous Medium

Boosted Enzyme Activity via Encapsulation within Metal–Organic Frameworks with Pores Matching Enzyme Size and Shape

Contact Info

Product

Resources

About