Fast multipoint immobilization of lipase through chiral<scp>l</scp>-proline on a MOF as a chiral bioreactor

Lirio, Stephen; Shih, Yung Han; So, Pamela Berilyn; Liu, Li Hao; Yen, Yun Ting; Furukawa, Shuhei; Liu, Wan Ling; Huang, Hsi Ya; Lin, Chia Her

doi:10.1039/d0dt04081a

Cited by 14 publications

(5 citation statements)

References 52 publications

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“…As an alternative, our previous studies demonstrated the anchoring of small dye molecules (FITC-fluorescein isothiocyanate or NBD-4-chloro-7-nitrobenzofurazan, molecular size < 2 nm) onto larger biomolecules to form a host-guest complex, which were subsequently immobilized onto the microporous MOFs (MOFs' micropores as host and dye as guest) to afford dye-tagged-enzyme@MOF bioreactors with high catalytic performance, reusability, and stability [17,18]. In the same way, we were also able to demonstrate the encapsulation of a small chiral molecule (Lproline) for the multipoint immobilization of lipase onto microporous MOFs, giving rise to a reusable and stable chiral catalyst [25]. Considering the diverse types and characteristics of commonly used enzymes for industrial application as well as the versatility of microporous MOFs, in this work, we sought to develop a simple strategy of immobilizing enzyme fragments into microporous MOFs materials for practical application.…”

Section: Introductionmentioning

confidence: 66%

Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors

Liu

Chiu

et al. 2021

Materials

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This work presents an efficient and facile strategy to prepare an α-amylase bioreactor. As enzymes are quite large to be immobilized inside metal-organic frameworks (MOFs), the tertiary and quaternary structures of α-amylase were first disrupted using a combination of urea, dithiothreitol (DTT), and iodoacetamide (IAA). After losing its tertiary structure, the unfolded proteins can now penetrate into the microporous MOFs, affording fragmented α-amylase@MOF bioreactors. Among the different MOFs evaluated, UiO-66 gave the most promising potential due to the size-matching effect of the α-helix of the fragmented α-amylase with the pore size of UiO-66. The prepared bioreactor exhibited high yields of small carbohydrate (maltose) even when reused up to 15 times (>80% conversion).

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Section: Introductionmentioning

confidence: 66%

Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors

Liu

Chiu

et al. 2021

Materials

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“…In another study reported by Lirio et al., the active site of lipase was opened by the co-immobilization of l -proline in MOF–1,4-NDC (Al) ( Figure 1 A), leading to an improved enzymatic activity. 23 This can be attributed to the enhanced enantioselectivity provided by the chiral environment of the amino acid.…”

Section: Recent Advances In Enhancing Enzymatic Activity In Enzyme–mo...mentioning

confidence: 99%

Section: Recent Advances In Enhancing Enzymatic Activity In Enzyme–mo...mentioning

confidence: 99%

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

Weng,

Chen,

Hui

et al. 2024

Chem Bio Eng.

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Enzymes, as highly efficient biocatalysts, excel in catalyzing diverse reactions with exceptional activity and selective properties under mild conditions. Nonetheless, their broad applications are hindered by their inherent fragility, including low thermal stability, limited pH tolerance, and sensitivity to organic solvents and denaturants. Encapsulating enzymes within metal−organic frameworks (MOFs) can protect them from denaturation in these harsh environments. However, this often leads to a compromised enzyme activity. In recent years, extensive research efforts have been dedicated to enhancing enzymatic activity within MOFs, leading to the development of new enzyme− MOF composites that not only preserve their catalytic potential but also outperform their free counterparts. This Review provides a comprehensive review on recent developments in enzyme−MOF composites with a specific emphasis on their enhanced enzymatic activity compared to free enzymes.

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“…19,20 Moreover, introducing polymers into MOFs was proved to enhance the catalytic performance of MOF-immobilized enzymes by creating mesopores inside MOFs via competitive coordination or serving as a protective layer to reduce the influence of unfavorable interfacial interactions on enzyme conformations. 21,22 Furthermore, several research groups have revealed that the introduction of amino acids within MOFs could greatly improve the properties of MOF-immobilized enzymes by inducing an active enzyme conformation, 23,24 accelerating the encapsulation process, 25,26 or changing the morphology of MOFs. 27 In this work, we aimed to develop an efficient immobilization system for haloalkane dehalogenase DhaA from Rhodococcus rhodochrous.…”

Section: ■ Introductionmentioning

confidence: 99%

A Hydrophilic Metal Azolate Coordination Polymer for In Situ Encapsulation of Haloalkane Dehalogenase with Enhanced Enzymatic Performance

Wu,

Sun

2024

ACS Appl. Mater. Interfaces

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Encapsulating enzymes within metal−organic frameworks such as zeolitic imidazolate framework-8 (ZIF-8) has been demonstrated to enhance enzymatic performance under harsh conditions. However, by computer-aided analysis, we revealed that highly hydrophobic organic ligands and unfavorable metal ions could greatly impair the activity of haloalkane dehalogenase DhaA by directly interacting with the catalytic sites, causing an extremely low activity of DhaA after encapsulating within ZIF-8. We also found that the presence of a protecting polymer could protect DhaA from the damage of organic ligands and metal ions and that a positively charged amino acid could increase the DhaA activity. Based on the simulations and experimental observations, we have designed to coencapsulate DhaA with poly(vinylpyrrolidone) (PVP) and lysine (Lys) within the amorphous Co-based metal azolate coordination polymer (CoCP). The as-prepared immobilized enzyme (DhaA/PVP/Lys@CoCP) exhibited significantly increased activity (91.5 times higher than that of DhaA@ZIF-8), dramatically enhanced thermostability at 50−70 °C, greatly improved catalytic performance in several organic solvent solutions, and good recyclability (over 75% of the initial activity after 10 cycles). The superiority of the immobilized enzyme was also demonstrated with a substrate frequently detected in the real world. In addition to the protective effect of PVP and positive effect of Lys, experimental and computational investigations unveiled other two favorable aspects that contributed to the enhanced enzymatic performance: (1) high hydrophilicity of the immobilization material and (2) the use of Co 2+ with a minimal negative effect on DhaA. The research has thus provided a promising immobilized DhaA with favorable catalytic performance and great potential in industrial applications.

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Fast multipoint immobilization of lipase through chirall-proline on a MOF as a chiral bioreactor

Abstract: Successful co-immobilization of Pro and PPL on microporous MOF-1,4-NDC(Al) (PPL-Pro@MOF-1,4-NDC(Al)) has been demonstrated.

Cited by 14 publications

References 52 publications

Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors

Fragmented α-Amylase into Microporous Metal-Organic Frameworks as Bioreactors

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

A Hydrophilic Metal Azolate Coordination Polymer for In Situ Encapsulation of Haloalkane Dehalogenase with Enhanced Enzymatic Performance

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