Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning DOI
Xinqi Xu,

Jinchang Zhong,

Bingmei Su

et al.

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 275, P. 133229 - 133229

Published: June 17, 2024

Language: Английский

Cellulase immobilization to enhance enzymatic hydrolysis of lignocellulosic biomass: An all-inclusive review DOI
Chaozhong Xu,

Shanshan Tong,

Liqun Sun

et al.

Carbohydrate Polymers, Journal Year: 2023, Volume and Issue: 321, P. 121319 - 121319

Published: Aug. 22, 2023

Language: Английский

Citations

52

Recent applications and future prospects of magnetic biocatalysts DOI
Rafael Leandro Fernandes Melo, Misael Bessa Sales, Viviane de Castro Bizerra

et al.

International Journal of Biological Macromolecules, Journal Year: 2023, Volume and Issue: 253, P. 126709 - 126709

Published: Sept. 9, 2023

Language: Английский

Citations

37

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers DOI Open Access
Nur Atikah Mohidem, Mardawani Mohamad, Muhammad Usman Rashid

et al.

Journal of Composites Science, Journal Year: 2023, Volume and Issue: 7(12), P. 488 - 488

Published: Nov. 26, 2023

For over a century, enzyme immobilisation has been proven to be superior strategy improve catalytic activity and reusability ensure easy separation, operation, reduced cost. Enzyme allows for an easier separation of the from reaction mixture, thus simplifying downstream processing. This technology protects degradation or inactivation by harsh conditions, making it more robust suitable used in various applications. Recent strategies methods, such as adsorption, cross-linking, entrapment encapsulation, covalent bonding, were critically reviewed. These have shown promising results improving stability, activity, A recent development nanomaterials agrowaste renewable carriers is underlined current review. Furthermore, use gained significant attention due their unique properties, high surface area, mass transfer, biocompatibility, sustainability. materials offer outcomes developing efficient sustainable immobilised enzymes. state-of-the-art better control reactions enhances reusability, leading cost-effective environmentally friendly processes. The also helps reduce waste generation promote utilisation resources, further contributing circular economy.

Language: Английский

Citations

37

Enhancing biocatalyst performance through immobilization of lipase (Eversa® Transform 2.0) on hybrid amine-epoxy core-shell magnetic nanoparticles DOI
Rafael Leandro Fernandes Melo, Tiago Melo Freire, Roberta Bussons Rodrigues Valério

et al.

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 264, P. 130730 - 130730

Published: March 11, 2024

Language: Английский

Citations

12

Nanomaterials for co‐immobilization of multiple enzymes DOI Creative Commons
Jingyu Zhang, Jonathan F. Lovell, Jiafu Shi

et al.

BMEMat, Journal Year: 2024, Volume and Issue: unknown

Published: March 12, 2024

Abstract In order to co‐immobilize multiple enzymes, a wide range of nanomaterials has been designed achieve synergistic enzyme activity and enhance catalytic efficiency. Nanomaterials, as carriers for co‐immobilization, possess various advantages such tunable morphology size, high specific surface area, abundant chemically active sites. They can significantly stability, activity, We overview the commonly used methods strategies co‐immobilization. This review further summarizes latest research advances in co‐immobilization applications over past 5 years. Meanwhile, challenges these well some potential future directions are also discussed.

Language: Английский

Citations

11

Precision Engineering of the Co‐immobilization of Enzymes for Cascade Biocatalysis DOI

Zhiyuan Luo,

Li Qiao, Haomin Chen

et al.

Angewandte Chemie International Edition, Journal Year: 2024, Volume and Issue: 63(22)

Published: April 1, 2024

Abstract The design and orderly layered co‐immobilization of multiple enzymes on resin particles remain challenging. In this study, the SpyTag/SpyCatcher binding pair was fused to N‐terminus an alcohol dehydrogenase (ADH) aldo‐keto reductase (AKR), respectively. A non‐canonical amino acid (ncAA), p ‐azido‐L‐phenylalanine (p‐AzF), as anchor for covalent bonding enzymes, genetically inserted into preselected sites in AKR ADH. Employing two bioorthogonal counterparts azide–alkyne cycloaddition immobilization ADH enabled sequential dual‐enzyme coating porous microspheres. ordered reactor subsequently used synthesize ( S )‐1‐(2‐chlorophenyl)ethanol asymmetrically from corresponding prochiral ketone, enabling situ regeneration NADPH. exhibited a high catalytic conversion 74 % good reproducibility, retaining 80 its initial activity after six cycles. product had 99.9 ee, which that maintained each cycle. Additionally, double‐layer method significantly increased enzyme loading capacity, approximately 1.7 times greater than traditional single‐layer immobilization. More importantly, it simultaneously both purification carriers, thus providing convenient approach facilitate cascade biocatalysis.

Language: Английский

Citations

9

Combined cross-linking of Rhizomucor miehei lipase and Candida antarctica lipase B for the effective enrichment of omega-3 fatty acids in fish oil DOI
Faezeh Ahrari, Mehdi Mohammadi

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 260, P. 129362 - 129362

Published: Jan. 23, 2024

Language: Английский

Citations

8

Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated DOI Creative Commons
Diego Carballares, Pedro Abellanas-Pérez, Diandra de Andrades

et al.

ACS Sustainable Chemistry & Engineering, Journal Year: 2024, Volume and Issue: 12(17), P. 6564 - 6572

Published: April 18, 2024

In the present article, glutaraldehyde was used to covalently coimmobilize lipase Eversa Transform 2.0 and β-galactosidase from Aspergillus oryzae. Both enzymes were adsorbed on amino supports modified with glutaraldehyde. However, first enzyme remained almost fully active under stress conditions, while lost a large percentage of its activity. To prevent necessity discarding both enzymes, immobilized following this immobilization strategy. The biocatalyst reduced eliminate chemical reactivity, then coimmobilized via ion exchange. incubation at high concentrations salt desorbed support. This combi-biocatalyst in three inactivation/rebuilding cycles where inactivated liberated by washing ionic strength replaced fresh enzyme, maintained activity throughout 3 cycles. That way, it possible use strategy reuse build new combi-biocatalysts after inactivation.

Language: Английский

Citations

6

Algal carbohydrate polymers: Catalytic innovations for sustainable development DOI
Sudarshan Sahu, Shalini Sharma, Anupreet Kaur

et al.

Carbohydrate Polymers, Journal Year: 2023, Volume and Issue: 327, P. 121691 - 121691

Published: Dec. 16, 2023

Language: Английский

Citations

14

One-pot biocatalytic upgrading of lignin-derived phenol and catechol to hydroxytyrosol DOI

Rui-Yan Zhao,

Shuangping Huang, Lili Gao

et al.

Green Chemistry, Journal Year: 2024, Volume and Issue: 26(10), P. 6180 - 6189

Published: Jan. 1, 2024

One-pot cascade biocatalysis for the conversion of renewable lignin-derived phenol and catechol into hydroxytyrosol.

Language: Английский

Citations

4