Metal-organic frameworks (MOFs) for enzyme immobilization

Vaidya, Leena B.; Nadar, Shamraja S.; Rathod, Virendra K.

doi:10.1016/b978-0-12-816984-1.00024-x

Cited by 13 publications

(5 citation statements)

References 97 publications

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“…The underutilization of the internal space of MOFs and the exposure of surface‐bound lipases to the external environment may lead to a comparatively low enzyme loading and the denaturation of lipases in unfavorable conditions. Furthermore, enzyme denaturation/deactivation, low enzyme loading efficiency, and increased mass transfer resistance are the other shortcomings that were observed during MOF‐lipase immobilization (Sun, Wu, et al., 2023; Vaidya et al., 2020b). Vaidya et al.…”

Section: Immobilization Advantages and Shortcomingsmentioning

confidence: 99%

“…The underutilization of the internal space of MOFs and the exposure of surface-bound lipases to the external environment may lead to a comparatively low enzyme loading and the denaturation of lipases in unfavorable conditions.Furthermore, enzyme denaturation/deactivation, low enzyme loading efficiency, and increased mass transfer resistance are the other F I G U R E 9 Synthesis of lipase@Cu-BTC, its storage stability assay as well as application in resolving N-HMVL (Reproduced from Cheng et al, 2023 with permission from Springer Nature, Copyright 2023). N-HMVL, N-hydroxymethyl vince lactam.shortcomings that were observed during MOF-lipase immobilization(Sun, Wu, et al, 2023;Vaidya et al, 2020b) Vaidya et al (2020a). revealed that the lipase's residual activity decreased during the course of six cycles because the enzyme was deactivated in the reaction media.…”

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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: Immobilization Advantages and Shortcomingsmentioning

confidence: 99%

mentioning

confidence: 99%

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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“…Their structure is based on a porous network composed of metal ions and organic ligands [ 24 ]. The selection of adequate synthesis precursors has a huge impact on the chemical surface, biocompatibility and stability [ 25 ]. The flexibility and versatility of their use has prompted their application in different fields, including biosensing, bioimaging and drug-delivery systems [ 26 , 27 , 28 ].…”

Section: Introductionmentioning

confidence: 99%

Super-Stable Metal–Organic Framework (MOF)/Luciferase Paper-Sensing Platform for Rapid ATP Detection

Martínez-Pérez-Cejuela

Calabretta

Bocci

et al. 2023

Biosensors

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Adenosine triphosphate (ATP) determination has been used for many decades to assess microbial contamination for hygiene monitoring in different locations and workplace environments. Highly sophisticated methods have been reported, yet commercially available kits rely on a luciferase–luciferin system and require storage and shipping at controlled temperatures (+4 or −20 °C). The applicability of these systems is limited by the need for a secure cold chain, which is not always applicable, especially in remote areas or low-resource settings. In this scenario, easy-to-handle and portable sensors would be highly valuable. Prompted by this need, we developed a bioluminescence paper biosensor for ATP monitoring in which a new luciferase mutant was combined with a metal–organic framework (MOF); i.e., zeolitic imidazolate framework-8 (ZIF-8). A paper biosensor was developed, ZIF-8@Luc paper sensor, and interfaced with different portable light detectors, including a silicon photomultiplier (SiPM) and smartphones. The use of ZIF-8 not only provided a five-fold increase in the bioluminescence signal, but also significantly improved the stability of the sensor, both at +4 and +28 °C. The ATP content in complex biological matrices was analyzed with the ZIF-8@Luc paper sensor, enabling detection down to 7 × 10−12 moles of ATP and 8 × 10−13 moles in bacterial lysates and urine samples, respectively. The ZIF-8@Luc sensor could, therefore, be applied in many fields in which ATP monitoring is required such as the control of microbial contamination.

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“…As an emerging class of porous materials with a broad spectrum of applications which are ever-expanding, MOFs have gained increasing attention and interests (Yuan et al 2018). In particular, MOFs have been recognized as novel matrices for efficient enzyme immobilization due to their fascinating structural and functional tunability, easy immobilization processing, and excellent catalytic performance presented by the enzyme-MOF hybrid composites (for reviews see (Vaidya et al 2020;Liang et al 2020)). Among them is HKUST-1, a highly porous metal coordination polymer with a molecular formula of [Cu 3 (BTC) 2 (H 2 O) n ] (BTC = benzene-1,3,5-tricarboxylate), which was first reported by Chui et al (1999).…”

Section: Introductionmentioning

confidence: 99%

Tyrosinase@HKUST-1: a super stable biocatalyst efficient for catecholic product synthesis

Feng

et al. 2021

Bioresour. Bioprocess.

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Although metal–organic frameworks (MOFs) have been considered as promising matrices for enzyme immobilization, HKUST-1, constructed from copper acetate (CuAc2) and benzene 1,3,5-tricarboxylate (BTC), has rarely been explored for this application. In this study, mushroom tyrosinase (EC 1.14.18.1) was immobilized in the form of tyrosinase@HKUST-1 following a simple reaction procedure by mixing BTC with the enzyme prior to addition of CuAc2. The resultant biocatalyst was characterized in both structural features and catalytic properties. Upon incorporation into the HKUST-1 frameworks, the enzyme gained a prominent enhancement in stability against pH, temperature and storage: When incubated at 50 °C and pH 6.0, tyrosinase@HKUST-1 presented a half-life of 32.6 h, which is 77-fold and over tenfold higher than that of the free enzyme and its other immobilization forms, respectively; and the catalyst fully maintained its activity for at least 2 months when stored at 30 °C. The applicability of this new biocatalyst was demonstrated by employing it as catalyst for regioselective ortho-hydroxylation reactions to produce catecholic products with huge pharmacological effects, i.e., hydroxytyrosol and l-DOPA, with excellent yields and productivities. This study has thus offered a facile immobilization method to prepare a novel biocatalyst with super stability, and tyrosinase@HKUST-1 so formed from crude mushroom extract provides an efficient catalyst which can be applied to the production of catecholic products with health benefits. Graphical Abstract

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Metal-organic frameworks (MOFs) for enzyme immobilization

Cited by 13 publications

References 97 publications

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

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

Super-Stable Metal–Organic Framework (MOF)/Luciferase Paper-Sensing Platform for Rapid ATP Detection

Tyrosinase@HKUST-1: a super stable biocatalyst efficient for catecholic product synthesis

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