Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Cavalcante, Francisco Sales Ávila; Cavalcante, Antônio Luthierre Gama; Sousa, Isamayra Germano de; Neto, Francisco Simão; Santos, José Cleiton Sousa dos

doi:10.3390/catal11101222

Cited by 93 publications

(57 citation statements)

References 321 publications

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“…In addition, they possess highly interesting characteristics that enable their use as enzyme immobilization matrices for subsequent application in biosensors [18]. Among the characteristics of MOFs that make them a good alternative for enzyme immobilization, their large surface area and adjustable pore sizes can be highlighted [208,209]. In addition, such properties also grant biosensors with greater sensitivity for electrochemical detection [15].…”

Section: Discussionmentioning

confidence: 99%

A Comprehensive Review on the Use of Metal–Organic Frameworks (MOFs) Coupled with Enzymes as Biosensors

et al. 2022

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Several studies have shown the development of electrochemical biosensors based on enzymes immobilized in metal–organic frameworks (MOFs). Although enzymes have unique properties, such as efficiency, selectivity, and environmental sustainability, when immobilized, these properties are improved, presenting significant potential for several biotechnological applications. Using MOFs as matrices for enzyme immobilization has been considered a promising strategy due to their many advantages compared to other supporting materials, such as larger surface areas, higher porosity rates, and better stability. Biosensors are analytical tools that use a bioactive element and a transducer for the detection/quantification of biochemical substances in the most varied applications and areas, in particular, food, agriculture, pharmaceutical, and medical. This review will present novel insights on the construction of biosensors with materials based on MOFs. Herein, we have been highlighted the use of MOF for biosensing for biomedical, food safety, and environmental monitoring areas. Additionally, different methods by which immobilizations are performed in MOFs and their main advantages and disadvantages are presented.

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Section: Discussionmentioning

confidence: 99%

A Comprehensive Review on the Use of Metal–Organic Frameworks (MOFs) Coupled with Enzymes as Biosensors

et al. 2022

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“…Several thorough and comprehensive reviews focused on enzyme immobilization have been recently published, where updated information on the methodologies for enzyme immobilization and related issues, e.g., materials used for immobilization, physical and (bio)chemical characterization methods, impact on catalytic features of the enzyme and interface with reactor operation, can be found [30,36,57,67,70,[144][145][146][147][148][149][150][151][152][153][154][155].…”

Section: Immobilization Of Multimeric Enzymesmentioning

confidence: 99%

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

et al. 2022

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Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.

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“…Lipases (triacylglycerol ester hydrolase, EC 3.1.1.3), ubiquitous in nature, constitute a special class of carboxyl ester hydrolases (EC 3.1.1) obtained from various sources ranging from microbes (fungi, yeast, and bacteria) to mammals (Ali et al., 2015; Sams et al., 2017). They are remarkably effective in versatile reactions, such as esterification, transesterification (Verdasco‐Martína et al., 2016), and C–C bond formation (Cavalcante, Cavalcante, et al., 2021). In nature, lipases act as important regulators in lipid metabolism and release long‐chain fatty acids from naturally water‐insoluble esters (lipids) (Ang et al., 2019; He et al., 2018; Wang et al., 2010).…”

Section: Introductionmentioning

confidence: 99%

“…Lipases have recently emerged as a leading biocatalyst/bioaccelerator (Lima et al., 2017) and served as a potential contributor to this multibillion‐dollar industry, with multifaceted applications in both industries and in situ lipid metabolism (Moreira et al., 2022; Vanleeuw et al., 2019). Lipases have been recently used as a potential biocatalyst in a large number of biotechnological sciences, more specifically, dairy products (cheese recovery, flavor enhancement, and the production of enzyme‐modified cheese), detergents, pharmaceuticals (ibuprofen, naproxen), chemicals, agriculture products (pesticides, insects), and oil chemistry (fat and oil hydrolysis and the synthesis of biodetergents) (Cavalcante, Neto, et al., 2021). Over the past few years, lipase‐catalyzed reactions have been performed in common organic solvents, ionic liquids, and even unconventional solvents with high selectivity and remarkable efficiency (Priyanka et al., 2019; Sharma & Kanwar, 2014).…”

Section: Introductionmentioning

confidence: 99%

Rebuilding the lid region from conformational and dynamic features to engineering applications of lipase in foods: Current status and future prospects

Chen

Khan

He³

et al. 2022

Comp Rev Food Sci Food Safe

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The applications of lipases in esterification, amidation, and transesterification have broadened their potential in the production of fine compounds with high cumulative values. Mostly, the catalytic triad of lipases is covered by either one or two mobile peptides called the “lid” that control the substrate channel to the catalytic center. The lid holds unique conformational allostery via interfacial activation to regulate the dynamics and catalytic functions of lipases, thereby highlighting its importance in redesigning these enzymes for industrial applications. The structural characteristic of lipase, the dynamics of lids, and the roles of lid in lipase catalysis were summarized, providing opportunities for rebuilding lid region by biotechniques (e.g., metagenomic technology and protein engineering) and enzyme immobilization. The review focused on the advantages and disadvantages of strategies rebuilding the lid region. The main shortcomings of biotechnologies on lid rebuilding were discussed such as negative effects on lipase (e.g., a decrease of activity). Additionally, the main shortcomings (e.g., enzyme desorption at high temperatre) in immobilization on hydrophobic supports via interfacial action were presented. Solutions to the mentioned problems were proposed by combinations of computational design with biotechnologies, and improvements of lipase immobilization (e.g., immobilization protocols and support design). Finally, the review provides future perspectives about designing hyperfunctional lipases as biocatalysts in the food industry based on lid conformation and dynamics.

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Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Cited by 93 publications

References 321 publications

A Comprehensive Review on the Use of Metal–Organic Frameworks (MOFs) Coupled with Enzymes as Biosensors

A Comprehensive Review on the Use of Metal–Organic Frameworks (MOFs) Coupled with Enzymes as Biosensors

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

Rebuilding the lid region from conformational and dynamic features to engineering applications of lipase in foods: Current status and future prospects

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