Calix[4]arene tetracarboxylic acid-treated lipase immobilized onto metal-organic framework: Biocatalyst for ester hydrolysis and kinetic resolution

Özyılmaz, Elif; Ascioglu, Sebahat

doi:10.1016/j.ijbiomac.2021.02.003

Cited by 36 publications

(20 citation statements)

References 69 publications

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“…The encapsulated Fe 3 O 4 @Calix‐ZIF‐8@CRL biocomposite structure was designed. Our approach allows the zeolitic imidazolate frameworks to be encapsulated with CRL‐Calix complex and Fe 3 O 4 on the inside [20,33] …”

Section: Resultsmentioning

confidence: 99%

“…Our group has used calix[4]arene derivative for the first time in ZIF‐lipase encapsulation synthesis . [20] The results indicate that immobilized lipase (CRL@Calix‐ZIF‐8) was higher activity and stability compared to the CRL@ZIF‐8.…”

Section: Introductionmentioning

confidence: 95%

“…Magnetizing MOF is one of the effective ways in this process. Recently, magnetic MOFs with specific functional properties have been designed for enzyme immobilization [6,10,18–20] . Moreover, the potential application of magnetic porous MOFs as the support for enzyme immobilization needs to be explored.…”

Section: Introductionmentioning

confidence: 99%

“…In our previous study, [20] Candida rugosa lipase was used for the first time in the enantioselective hydrolysis of racemic naproxen methyl ester, after immobilizing to metal organic framework. It was obtained that 38 % conversion and enantioselectivity (E=183) were found.…”

Section: Introductionmentioning

confidence: 99%

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Preparation of One‐Pot Immobilized Lipase with Fe₃O₄ Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

Özyılmaz

Ascioglu

2021

ChemCatChem

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Immobilization of enzyme to magnetic metal‐organic frameworks (MOF) can preserve biological functionality in harsh environments to increase enzymes activity, stability, and improve reusability. The magnetic Fe3O4 nanoparticles were treated with calix[4]arene tetracarboxylic acid (Calix) and Candida rugosa lipase (CRL), and then encapsulated into the zeolitic imidazole framework‐8 (Fe3O4@Calix‐ZIF‐8@CRL). The lipase activity data of Fe3O4@Calix‐ZIF‐8@CRL was 2.88 times higher than that of the Fe3O4@ZIF‐8@CRL (without Calix). The catalytic properties of immobilized lipases were studied on the enantioselective hydrolysis of R/S‐naproxen methyl ester. It was also observed that Fe3O4@Calix‐ZIF‐8@CRL has excellent enantioselectivity (E=371) compared to Fe3O4@ZIF‐8@CRL (E=131). Furthermore, Fe3O4@Calix‐ZIF‐8@CRL was seen to still retain 30 % of the conversion rate after the fifth reuse. This work may also be useful for the pharmaceutical industry due to the increased reusability and stability of enzymes, the enantiomeric selectivity exhibited by MOF‐enzyme biocomposites, and the significant differences in the biological activities of the enantiomers.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Preparation of One‐Pot Immobilized Lipase with Fe₃O₄ Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

Özyılmaz

Ascioglu

2021

ChemCatChem

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“…The hydrolysis capability of native, inactivated, immobilized, or modified lipases against naproxen methyl ester was examined using HPLC 10,42‐44 …”

Section: Methodsmentioning

confidence: 99%

L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

Özyılmaz

Çağlar

2021

J of Chemical Tech & Biotech

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BACKGROUND Chemical modification is a simple, low cost, very fast and easy production that has no limits as to the nature of the groups introduced into the enzymes. Chemical modification may be directed to improve enzyme stability, as well as selectivity, specificity, and activity. RESULTS Candida rugosa lipase (CRL) was immobilized onto a cellulose‐based support. The native, inactivated, and immobilized lipases were modified by the reaction of L‐proline (Prl) in the presence of coupling reagent (EDC). The catalytic properties of the modified lipases were evaluated by hydrolysis of p‐nitrophenylpalmitate and the enantioselective hydrolysis of racemic naproxen methyl ester. It was observed that by chemical modification with proline, the hydrolytic activities of native, inactivated, and immobilized lipases increased 2.4, 11.0, and 2.2‐fold, respectively. The immobilized lipase retained 64% of its activity after 120 min at 60 °C, while immobilized L‐proline modified lipase was found to retain 72%. It was also found that the immobilized inactivated lipase kept 44% of its activity at 60 °C for 2 h, while the immobilized L‐proline modified inactivated lipase retained their activity at 65%. In addition, the attained results of the best enantioselectivity of CRL‐Prl exhibited a 2.2‐fold improvement compared to the native enzyme. CONCLUSION The method is simple, cost‐effective, very fast, and it can obtain stronger biocatalysts. It was understood that a lipase lost its activity and could be reused after being simply modified with L‐proline. This study predicts that such facile chemical modifications will open new avenues to develop industrially important biocatalyst with superior catalytic properties. © 2021 Society of Chemical Industry (SCI).

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Lipase Immobilized onto Metal‐Organic Frameworks for Enantioselective Resolution of Mandelic Acid

Fan

Tang

2022

Chem Eng & Technol

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An immobilized lipase with metal‐organic frameworks (MOFs) was first used for the kinetic resolution of mandelic acid enantiomers by transesterification reaction using vinyl acetate as acyl donor in organic medium. Notably, the biocompatibility of the carrier and catalytic performance of lipase could be significantly improved via modification of NH2‐Ni‐MOF with polyvinylpyrrolidone. After extensively screening the enzymatic process, the optimal enantioselective resolution conditions and excellent outcomes were obtained for the enzyme‐catalyzed transesterification reaction. In addition, the recovered immobilized lipase displayed outstanding reusability after immobilization.

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Calix[4]arene tetracarboxylic acid-treated lipase immobilized onto metal-organic framework: Biocatalyst for ester hydrolysis and kinetic resolution

Cited by 36 publications

References 69 publications

Preparation of One‐Pot Immobilized Lipase with Fe₃O₄ Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

Preparation of One‐Pot Immobilized Lipase with Fe₃O₄ Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

Lipase Immobilized onto Metal‐Organic Frameworks for Enantioselective Resolution of Mandelic Acid

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Calix[4]arene tetracarboxylic acid-treated lipase immobilized onto metal-organic framework: Biocatalyst for ester hydrolysis and kinetic resolution

Cited by 36 publications

References 69 publications

Preparation of One‐Pot Immobilized Lipase with Fe3O4 Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

Preparation of One‐Pot Immobilized Lipase with Fe3O4 Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

L‐proline modified inactivated lipase and its immobilization on cellulose‐based material: stability and enantioselectivity

Lipase Immobilized onto Metal‐Organic Frameworks for Enantioselective Resolution of Mandelic Acid

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Preparation of One‐Pot Immobilized Lipase with Fe₃O₄ Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

Preparation of One‐Pot Immobilized Lipase with Fe₃O₄ Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester