Encapsulation of lipase using magnetic fluorescent calix[4]arene derivatives; improvement of enzyme activity and stability

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.

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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

Ascioglu

2021

ChemCatChem

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“…Racemic resolution is considered a major challenge in the chemical and pharmaceutical industries; among different chemical processes, biocatalysis is a promising method for the immediate extraction of single isomer chiral drug 31‐34 . Lipases can be employed for racemic resolution due to their regio‐, chemo‐, and enantioselectivity in manufacture of drugs and their intermediates 31,35‐37 …”

Section: Introductionmentioning

confidence: 99%

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

J of Chemical Tech & Biotech

Çağlar

2021

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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).

Preparation of regenerable magnetic nanoparticles for cellulase immobilization: Improvement of enzymatic activity and stability

Alhiali

Çağlar

2021

Biotechnol Progress

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To obtain regenerable magnetic nanoparticles, triethoxy(3-isocyanatopropyl)silane and iminodiacetic acid (IZ) were used as the starting material and immobilized on Fe 3 O 4 nanoparticles. Copper ions (Cu 2+ ions) were loaded on the Fe-IZ nanoparticles and used for cellulase immobilization. The support was characterized by spectroscopic methods (FTIR, NMR) and thermogravimetric analysis, transmission electron microscopy, scanning electron microscope, X-ray diffraction, energy dispersive X-ray analysis, and vibrating sample magnetometer techniques. As a result of experiments, the amount of protein bound to immobilized cellulase (Fe-IZ-Cu-E) and cellulase activity was found to be 33.1 mg/g and 154 U/g at pH 5, 50 C, for 3 h. The results indicated that the free cellulase had kept only 50% of its activity after 2 h, while the Fe-IZ-Cu-E was observed to be around 77%, at 60 C. It was found that the immobilized cellulase maintained 93% of its initial catalytic activity after its sixth use. Furthermore, the Fe-IZ-Cu-E retained about 75% of its initial activity after 28 days of storage. To reuse the support material (Fe-IZ-Cu), it was regenerated by thorough washing with ammonia or imidazole.