Metal-Organic Frameworks Conjugated Lipase with Enhanced Bio-catalytic Activity and Stability
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Metal-Organic Frameworks Conjugated Lipase with Enhanced Bio-catalytic Activity and Stability Bin Zou 1,3 & Liming Zhang 1 & Jiaojiao Xia 2,3 Xinyi Wang 1 & Idowu Onyinye Adesanya 1
1
1
& Pengyun Wang & Yan Yan &
Received: 3 October 2019 / Accepted: 13 February 2020/ # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract
Covalent immobilization of lipase onto a solid carrier is an effective way to enhance stability. Immobilization inhibits the activity of lipase due to decreased flexibility of enzyme structure via the covalent bond. In this study, monomer of the metal-organic frameworks (MOFs) material ZIF-8 (2-methyl imidazole-4-carboxylic acid) was innovatively used as a chemical modifier of Candida nrugosa lipase (CRL). The circular dichroism spectra results show that the CRL molecule was altered by chemical modification and thus its catalytic activity was 1.3 times higher than that of the free CRL. The modified CRL molecule was further immobilized in the “skeleton” of ZIF-8 through the monomer while in situ forming the cell skeleton of the MOFs, which prevent the active center from being destroyed. The results show that conjugation of chemical modification and immobilized enzymes ensure that there was no obvious reduction in the activity of CRL after immobilization and the stability of CRL was improved. Especially, the organic solvent stability of the modified immobilization CRL in isopropanol was significantly improved and retained more than 148% of its activity. Keywords Lipase . Metal-organic frameworks . Chemical modification . Immobilization . Stabilities
* Jiaojiao Xia [email protected]
1
School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China
2
School of Chemistry and Chemical Engineering, Jiangsu University, No.301 Xuefu Road, Zhenjiang 212013, China
3
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China
Applied Biochemistry and Biotechnology
Introduction Lipases are presumed to provide a green synthetic pathway with low pollution and energy consumption due to their mild reaction conditions and high catalytic efficiency [1]. However, large-scale application of lipases in the industry is still limited because catalytic reactions usually conducting in organic solvents, high temperatures, and extreme pH are not natural lipase-catalyzed environments [2]. Therefore, it is imperative to alter the lipase molecule and thus enhance its catalytic performance. Presently the commonly used lipase molecular transformation methods may be subdivided into molecular biology methods (rational design and directed evolution), and in vitro modification methods (chemical modification and immobilization [3, 4]). Molecular biology methods in lipase transformation are liable for a huge screening scale and complex operation. Although molecular biology methods are much more precise than modification, in vitro modification methods have the advantages of lower cost, shorter cycle, and easy development of new enzymatic p
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