Lipase AK from Pseudomonas fluorescens immobilized on metal organic frameworks for efficient biosynthesis of enantiopure (S)− 1-(4-bromophenyl) ethanol

Sun, Chenrui; Wu, Shuhui; Wu, Ying; Sun, Bizhu; Zhang, Panliang; Tang, Kewen

doi:10.1016/j.procbio.2022.11.022

Cited by 5 publications

(12 citation statements)

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“…In comparison to both free and immobilized lipase without ILs (PPL‐Fe 3 O 4 @MOF), the immobilized lipase (PPL‐ILs/Fe 3 O 4 @MOF) displayed 2.1‐ and 1.8‐fold greater activity, respectively (Suo et al., 2023). Moreover, the MOF (NH 2 ‐Co‐MOF) was used to create microsphere support, upon which the immobilization of lipase AK from Pseudomonas fluorescens was studied (Sun, Wu, et al., 2023). Covalent bonding was used to immobilize lipase AK to the NH 2 ‐Co‐MOF support.…”

Section: Designing Lipase‐mof Immobilization Platformmentioning

confidence: 99%

“…Covalent bonding was used to immobilize lipase AK to the NH 2 ‐Co‐MOF support. The immobilization yield was 72.3% at a loading capacity of 256.9 mg g −1 (MOF) (Sun, Wu, et al., 2023).…”

Section: Designing Lipase‐mof Immobilization Platformmentioning

confidence: 99%

“…Lipase AK was immobilized from P. fluorescens onto a microsphere substrate built by the MOF of NH 2 ‐Co‐MOF and its catalytic efficiency for the enantiospecific transesterification of 1‐(4‐bromophenyl) ethanol (BPE) with vinyl acetate was investigated (Sun, Wu, et al., 2023). Enantiospecific transesterification of BPE with vinyl acetate was shown to be catalyzed effectively by AK@NH 2 ‐Co‐MOF, with an expressed activity of 4.028 ± 0.21 × 10 −2 mmol (min mg AK@NH 2 ‐Co‐MOF) −1 that was eight times higher than the free lipase (Sun, Wu, et al., 2023). In the other experiment, it was discovered that lipase@Cu‐BTC had an enzyme activity almost five times higher than a free enzyme (Cheng et al., 2023).…”

Section: Immobilization Advantages and Shortcomingsmentioning

confidence: 99%

“…Nowadays, lipases are applied in an array of industries, including those dealing with biodiesel, medicines, emulsifiers, cosmetics, fragrances, the pretreatment of lipid‐rich wastewater, and the production of several organic compounds, including lipophilic antioxidants (Kim et al., 2023; Sampaio et al., 2022). While lipases can be extracted from microorganisms, animals, and plants, the latter are the ones prevalently applied in the industry because of their great diversity, extensive range of catalytic potentials, high lipase production yield, production control, magnification ease, less complex genetic manipulation, and high stability in catalytic performance in the reaction media (Ismail & Baek, 2020; Kim et al., 2023; Sampaio et al., 2022; Sun, Wu, et al., 2023). Lipase has several potential industrial applications, but it has yet to overcome a number of challenges.…”

Section: Introductionmentioning

confidence: 99%

“…They include low stability, separation, and recovery challenges, and limited reusability. As a first step in solving these problems, researchers are looking toward modifying the lipase, with immobilization being one of the most well‐studied and commonly used technologies thus far (Sun, Wu, et al., 2023). Hence, the increasing interest in processes reliant on immobilized lipases has coincided with the development of novel supports.…”

Section: Introductionmentioning

confidence: 99%

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Recent trends in metal‐organic frameworks mediated lipase immobilization: A state‐of‐the‐art review

Patil,

Dong,

Usman

et al. 2023

Food Safety and Health

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Immobilized lipase is a powerful biocatalytic system with numerous applications in industries, particularly in the energy, pharmaceutical, cosmetic, and food industries. Reusability, simple recovery, and high chemical and thermal stability make it an attractive alternative to traditional chemical catalysts in industrial applications. Novel methods and support materials for immobilizing lipases have recently attracted much attention. Metal‐organic frameworks (MOFs) are a promising class of materials for enzyme immobilization carriers due to their appealing features, including a high specific surface area, high specific porosity, a stable framework structure, and a wide variety of functional sites. Due to the protection provided to enzymes by MOFs, several reported MOFs‐lipase composites display exceptional catalytic characteristics relative to free lipases. This includes increased enzyme efficiency, stability, selectivity, and recyclability. Herein, we summarize an updated review of the most recent advances in MOFs immobilizing lipases. This review sheds light on the numerous aspects of lipase‐MOF immobilization, with special emphasis on different techniques of designing lipase‐MOF platforms and the advantages of lipase‐MOF composites. Subsequently, molecular simulation approaches in lipase‐MOF immobilization are briefly introduced. Moreover, practical applications of MOFs‐lipase composites have been outlined. Finally, potential limitations and future directions for MOFs‐lipase immobilization research are highlighted.

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Section: Designing Lipase‐mof Immobilization Platformmentioning

confidence: 99%

Section: Designing Lipase‐mof Immobilization Platformmentioning

confidence: 99%