Integration of multienzyme co-immobilization and biomimetic catalysis in magnetic metal–organic framework nanoflowers for α-amylase detection in fermentation samples

Chen, Liangqiang; Hao, Mengdi; Huang, Wanqiu; Yu, Shaoning; Shen, Hao; Yang, Fan; Wang, Li; Tu, Huabin

doi:10.1016/j.foodchem.2024.138773

Cited by 4 publications

(2 citation statements)

References 29 publications

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“…2,3 In particular, there are growing appeals for exploring MOFs as potent supports for enzyme immobilization, endowed by the high surface area, the facile de novo design, and postsynthetic modification. 4,5 To date, different modification strategies have been proposed to regulate the structure and properties of MOFs to exhibit better performance as carrier materials, while various immobilization strategies such as encapsulation and coprecipitation have been proposed to achieve enzyme immobilization within MOFs. 6−8 The hydrophilicity and porosity of MOFs have been demonstrated to significantly affect the activity, selectivity, and stability of the immobilized enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…Metal–organic frameworks, also known as porous coordination polymers, represent an emerging class of three-dimensional ordered porous materials formed by the linkage between organic ligands and metal nodes via ordination bonds . Their natural advantages, such as ultrahigh porosity, large surface area, high structural tunability, and functional designability, lead to a great potential for various applications including gas storage and separations, catalysis, biomedicine, proton conduction, etc. , In particular, there are growing appeals for exploring MOFs as potent supports for enzyme immobilization, endowed by the high surface area, the facile de novo design, and postsynthetic modification. , To date, different modification strategies have been proposed to regulate the structure and properties of MOFs to exhibit better performance as carrier materials, while various immobilization strategies such as encapsulation and coprecipitation have been proposed to achieve enzyme immobilization within MOFs. − The hydrophilicity and porosity of MOFs have been demonstrated to significantly affect the activity, selectivity, and stability of the immobilized enzymes. , In addition to being carrier materials, MOFs can also be used as the template for the construction of enzyme immobilization . However, the difficulty in constructing ordered and interconnected macroporous structures severely limits the application of MOFs in the immobilization of macromolecular enzymes as well as in bulky-molecule reaction systems .…”

Section: Introductionmentioning

confidence: 99%

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Single-Crystalline Ordered Nanoporous Metal–Organic Frameworks for Lipase Immobilization and Structured Lipid Production

Liu,

Li,

Dai

et al. 2024

ACS Appl. Nano Mater.

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Single-crystalline ordered macro-microporous CuBTC shows excellent mass transfer performance and has high fatty acid stability, making it highly promising as an enzyme immobilization carrier. However, its practical application is severely limited by its poor water stability. To address this challenge, we introduced a ligand, 1,2,3-benzotriazole (BTA), known for its hydrophobicity and strong coordination with copper. A series of CuBTCderived dual-ligand SOM-MOFs (SOM-MIXs) was successfully synthesized with enhanced hydrophobicity and improved water stability. The CuBTCderived SOM-MIXs demonstrated superior performance for lipase immobilization, resulting in a maximum increase of 66.9% in specific activity. To address the limitation that excessive addition of 1,2,3-benzotriazole does not further enhance the hydrophobicity of the carrier and may lead to structural damage, a sol−gel method was employed to coat the SOM-MIX with highly hydrophobic PDMS, leading to a further increase of 139.1% in the specific activity. The resulting immobilized lipase exhibited excellent catalytic performance and remarkable reusability, with 90.09% activity retention after five cycles in the synthesis process of 1-oleoyl-2-palmitoyl-3-linoleoylglycerol (OPL) by acidolysis. This work highlights the potential of SOM-MIX@PDMS and provides valuable insights into the rational design and postmodification of metal−organic frameworks (MOFs) for enzyme immobilization in diverse applications.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Single-Crystalline Ordered Nanoporous Metal–Organic Frameworks for Lipase Immobilization and Structured Lipid Production

Liu,

Li,

Dai

et al. 2024

ACS Appl. Nano Mater.

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Immobilized Multi‐Enzyme/Nanozyme Biomimetic Cascade Catalysis for Biosensing Applications

Cai,

Huang,

Zhu

2024

Adv Healthcare Materials

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Multiple enzyme‐induced cascade catalysis has an indispensable role in the process of complex life activities, and is widely used to construct robust biosensors for analyzing various targets. The immobilized multi‐enzyme cascade catalysis system is a novel biomimetic catalysis strategy that immobilizes various enzymes with different functions in stable carriers to simulate the synergistic catalysis of multiple enzymes in biological systems, which enables high stability of enzymes and efficiency enzymatic cascade catalysis. Nanozymes, a type of nanomaterial with intrinsic enzyme‐like characteristics and excellent stabilities, are also widely applied instead of enzymes to construct immobilized cascade systems, achieving better catalytic performance and reaction stability. Due to good stability, reusability, and remarkably high efficiency, the immobilized multi‐enzyme/nanozyme biomimetic cascade catalysis systems show distinct advantages in promoting signal transduction and amplification, thereby attracting vast research interest in biosensing applications. This review focuses on the research progress of the immobilized multi‐enzyme/nanozyme biomimetic cascade catalysis systems in recent years. The construction approaches, factors affecting the efficiency, and applications for sensitive biosensing are discussed in detail. Further, their challenges and outlooks for future study are also provided.

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Developing Catalysts for the Hydrolysis of Glycosidic Bonds in Oligosaccharides Using a Spectrophotometric Screening Assay

Striegler

2024

ACS Catal.

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In a proof-of-concept study, a method for the empirical design of polyacrylate gel catalysts with the ability to cleave 1→4 α-glycosidic bonds in di- and trisaccharides was elaborated. The study included the synthesis of a 300-gel member library based on two different cross-linkers and 10 acrylate monomers, identification of monomodal gels by dynamic light scattering, and a 96-well plate spectrophotometric screening assay to monitor the hydrolysis of chromophore-free maltose into glucose units. The composition of the matrix of the most efficient catalysts in the library was found to enable CH−π, hydrophobic, and H-bond accepting interactions during the hydrolysis as typically seen in glycosylases. The same gel catalysts allowed the hydrolysis of the trisaccharide maltotriose with a catalytic proficiency of 2 × 106 indicating transition state stabilization during the hydrolysis of 5 × 10–7. The results place the developed gels among the most efficient catalysts developed for the hydrolysis of natural saccharides. The elaborated strategy may lead to catalysts that can transform polysaccharides into valuable synthons in the near future.

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Integration of multienzyme co-immobilization and biomimetic catalysis in magnetic metal–organic framework nanoflowers for α-amylase detection in fermentation samples

Cited by 4 publications

References 29 publications

Single-Crystalline Ordered Nanoporous Metal–Organic Frameworks for Lipase Immobilization and Structured Lipid Production

Single-Crystalline Ordered Nanoporous Metal–Organic Frameworks for Lipase Immobilization and Structured Lipid Production

Immobilized Multi‐Enzyme/Nanozyme Biomimetic Cascade Catalysis for Biosensing Applications

Developing Catalysts for the Hydrolysis of Glycosidic Bonds in Oligosaccharides Using a Spectrophotometric Screening Assay

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