Self-assembly of activated lipase hybrid nanoflowers with superior activity and enhanced stability

Li, Conghai; Zhao, Juan; Zhang, Zhijin; Jiang, Yanjun; Bilal, Muhammad; Jiang, Yunhong; Jia, Shiru; Cui, Jiandong

doi:10.1016/j.bej.2020.107582

Cited by 72 publications

(19 citation statements)

References 46 publications

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“…However, in a recent study using sonication as an accelerator mechanism, An et al ( 2015) [253] reduced this time to just 5 minutes. Many authors used this method to confirm the proposed protocol's efficiency and efficacy [253,254,[256][257][258]. Figure 7 shows how the process for enzyme immobilization by hybrid nanoflowers occurs: Figure 7.…”

Section: Hybrid Nanoflowersmentioning

confidence: 95%

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

Cavalcante

Sousa

et al. 2021

Catalysts

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The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level.

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Section: Hybrid Nanoflowersmentioning

confidence: 95%

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

Cavalcante

Sousa

et al. 2021

Catalysts

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“…Nanoflowers have been demonstrated as effective biocatalysts and biosensors, particularly with copper phosphate as the inorganic phase. [154][155][156][157][158][159][160][161][162][163][164][165][166] Though the relative mass of protein within the nanoflowers is relatively low (5-30% by mass), the materials assemble in a robust and predictable fashion, the morphology can be modified by synthesis conditions, and there is limited leaching of enzymes from nanoflowers. Additionally, they retain high enzyme activity upon binding, and in some cases, the inorganic phase can serve as a rate enhancer for the immobilized enzyme.…”

Section: Inorganic Nanoflowers and Supraparticlesmentioning

confidence: 99%

Protein Mediated Enzyme Immobilization

Caparco

Dautel

Champion

2022

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Enzyme immobilization is an essential technology for commercializing biocatalysis. It imparts stability, recoverability, and other valuable features that improve the effectiveness of biocatalysts. While many avenues to join an enzyme to solid phases exist, protein‐mediated immobilization is rapidly developing and has many advantages. Protein‐mediated immobilization allows for the binding interaction to be genetically coded, can be used to create artificial multienzyme cascades, and enables modular designs that expand the variety of enzymes immobilized. By designing around binding interactions between protein domains, they can be integrated into functional materials for protein immobilization. These materials are framed within the context of biocatalytic performance, immobilization efficiency, and stability of the materials. In this review, supports composed entirely of protein are discussed first, with systems such as cellulosomes and protein cages being discussed alongside newer technologies like spore‐based biocatalysts and forizymes. Protein‐composite materials such as polymersomes and protein–inorganic supraparticles are then discussed to demonstrate how protein‐mediated strategies are applied to many classes of solid materials. Critical analysis and future directions of protein‐based immobilization are then discussed, with a particular focus on both computational and design strategies to advance this area of research and make it more broadly applicable to many classes of enzymes.

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“…A unique peak at 1092 cm −1 for the vibration of C-O and probably PO 4 3− was observed. The latter originated from traces of phosphate buffer [43,44], used during AOL immobilization on the MNC/PES. The formation of new intermolecular hydrogen bonds between O-H molecules on AOL and functional groups on MNC/PES fibers shifted the O-H stretching vibration from 3450 cm −1 to 3318 cm −1 and increased band intensity [34,44].…”

Section: Protein Content Immobilization Yield and Lipase Activitymentioning

confidence: 99%

“…A unique peak at 1092 cm −1 for the vibration of C-O and probably PO 4 3− was observed. The latter originated from traces of phosphate buffer[43,44], used during AOL immobilization…”

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confidence: 99%

Electrospun Magnetic Nanocellulose–Polyethersulfone-Conjugated Aspergillus oryzae Lipase for Synthesis of Ethyl Valerate

et al. 2021

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A novel greener MNC/PES membrane was developed through an electrospinning technique for lipase immobilization to catalyze the synthesis of ethyl valerate (EV). In this study, the covalent immobilization of Aspergillus oryzae lipase (AOL) onto an electrospun nanofibrous membrane consisting of magnetic nanocellulose (MNC) and polyethersulfone (PES) to produce EV was statistically optimized. Raman spectroscopy, Fourier-transform infrared spectroscopy: attenuated total reflection, field emission scanning electron microscopy, energy dispersive X-ray spectroscopy, thermal gravimetric analysis (TGA), and differential thermal gravimetric (DTG) of MNC/PES-AOL demonstrated that AOL was successfully immobilized onto the fibers. The Taguchi design-assisted immobilization of AOL onto MNC/PES fibers identified that 1.10 mg/mL protein loading, 4 mL reaction volume, 250 rpm stirring rate, and 50 °C were optimal to yield 72.09% of EV in 24 h. The thermal stability of MNC/PES-AOL was improved by ≈20% over the free AOL, with reusability for up to five consecutive esterification cycles while demonstrating an exceptional half-life of 120 h. Briefly, the electrospun MNC/PES fibers that immobilized AOL showed promising applicability in yielding relatively good EV levels. This study suggests that using MNC as fillers in a PES to improve AOL activity and durability for a longer catalytic process could be a viable option.

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Self-assembly of activated lipase hybrid nanoflowers with superior activity and enhanced stability

Cited by 72 publications

References 46 publications

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

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

Protein Mediated Enzyme Immobilization

Electrospun Magnetic Nanocellulose–Polyethersulfone-Conjugated Aspergillus oryzae Lipase for Synthesis of Ethyl Valerate

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