Renewable, sustainable, and natural lignocellulosic carriers for lipase immobilization: A review

Girelli, Anna Maria; Chiappini, Viviana

doi:10.1016/j.jbiotec.2023.02.003

Cited by 19 publications

(15 citation statements)

References 168 publications

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“…Enzymes are a kind of biomacromolecule that could catalyze a variety range of chemical reactions. , Immobilization could afford a facile and feasible strategy to promote the industrialization of enzymes in pharmaceuticals, biosensing, biosynthesis, and so on. − In the last few years, efforts have been made to explore polymeric materials, inorganic materials, and hybrid materials for the development of immobilization carriers. − However, the activity enhancement and sustainable applications of immobilized enzymes remain a challenge for current enzyme immobilization platforms. − In general, the enzyme immobilization carriers should have features of good enzyme-compatibility, excellent structural stability, regular and tunable pore structure, etc.…”

Section: Introductionmentioning

confidence: 99%

Bioactive Covalent Organic Framework Capsules for Lactate Synthesis

Meng

Shi

et al. 2023

ACS Sustainable Chem. Eng.

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Capsular covalent organic frameworks (COFs) offer unique and highly tunable spaces for enzyme immobilization. Herein, a kind of bioactive covalent organic framework (bio-COF) capsule was fabricated through a sacrificial templating method for the synthesis of lactate from pyruvate. The synthesis time of COF and the amount of enzyme were optimized during the preparation of bio-COF capsules. The enzymes were entrapped in the capsule wall with a thickness of ∼240 nm and a major pore size of ∼1.8 nm. The porous structure of bio-COF capsules ensured rapid diffusion of substrates through the capsule wall. Thereby, the bio-COF capsule retained 70% of its initial activity under reaction conditions at pH 6 and 35 °C. The confinement of the capsule wall toward enzymes remarkably improved the operational stability and organic solvent tolerance. After treatment under pH 4 and 60 °C for 120 min, the bio-COF capsules still retained the relative activities of 79 and 60%, respectively. Furthermore, the bio-COF capsules exhibited superior recyclability, retaining over 85% relative activity after 8 cycles. Our study offers a general platform for immobilizing enzymes and expands the potential application of COFs in the green biomanufacturing field.

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Section: Introductionmentioning

confidence: 99%

Bioactive Covalent Organic Framework Capsules for Lactate Synthesis

Meng

Shi

et al. 2023

ACS Sustainable Chem. Eng.

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“…Bilirubin can act as an agonist activate the (melastatinlike transient receptor potential 2) TRPM2 channel to exacerbate neurotoxicity [26].The structure of bilirubin was presented in Figure 1b. The combination of substances can be achieved in a variety of ways such as self-assembly [27,28], co-precipitation [29,30] and immobilization [31,32]. The combination of bilirubin to albumin can proceed spontaneously and the binding of bilirubin and albumin has long been explored by scientists, which possess a variety of physiological functions in human body [33][34][35].…”

Section: Introductionmentioning

confidence: 99%

The Impact of Bilirubin on 7α- and 7β- Hydroxysteroid Dehydrogenases: Spectra and Docking Analysis

Ji¹,

Chen²,

Zhu³

et al. 2023

Preprint

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7α- and 7β-hydroxysteroid dehydrogenases (HSDH) are a pair of enzymes that can catalyze the isomerization of hydroxyl group at site 7 of bile acids. In previous study, we found that the activities of 7α- and 7β-HSDH can be inhibited by bilirubin. In order to clarify the impact, the effects of bilirubin on enzymes were studied by kinetics, spectrum and docking analysis. Relative activity of 7α-HSDH remained less than 40 % under 1 mM bilirubin, for 7β-HSDH, only 18 % activity left at the same condition. Using taurochenodeoxycholic acid (TCDCA) as substrate, the Km of 7α-HSDH was up to 0.63 mM from 0.24 mM after binding with bilirubin, the Km of 7β-HSDH rose from 1.14 mM to 1.87 mM for the catalysis of tauroursodeoxycholic acid (TUDCA). The affinity of 7α- and 7β-HSDH to substrate decreased with the effect of bilirubin. The binding of bilirubin with 7α- or 7β-HSDH were analyzed by UV–Vis spectra, Fluorescence spectra and Circular dichroism (CD) spectra. The results reflected that bilirubin caused a slight change in the secondary structure of 7α- or 7β-HSDH, and the changes were correlated with the ratio of bilirubin to enzyme. 10 candidate molecular docking results were presented to reflect the binding of bilirubin with 7α- or 7β-HSDH and to explore the inhibition mechanism. This research not only provides the more in-depth understanding of 7α- and 7β-HSDH, but also reminds us to avoid the inhibition of bilirubin on hydroxysteroid dehydrogenases.

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“…1 However, free lipase exhibits low stability during long operational times and is difficult to reuse and separate from the products, which greatly limits the development of enzyme-based industries. 1,2 To address these challenges, enzyme immobilization technology has been designed and is becoming increasingly popular. Compared with free enzymes, immobilized enzymes generally exhibit superior stability, operability, reusability, and controllability due to their physical or chemical interaction with supports.…”

Section: Introductionmentioning

confidence: 99%

“…For example, if hydrophobic products of lipase block hydrophobic channels or deposit on the surface of the hydrophobic support, the activity of immobilized lipase will be isolated from substrates and show low activity . To overcome these drawbacks, support materials should be designed with fewer blockages of mass transfer channels, high immobilization capacity, and good stability in reaction environments to improve the practicability and reusability of immobilized enzymes. , For instance, when designing supports to immobilize lipases, strategies to prevent membrane fouling, such as forming richer pores in the supports as mass transfer channels to reduce blockages caused by compounds, and changing the surface properties of supports to reduce compound deposition can be referenced. − …”

Section: Introductionmentioning

confidence: 99%

“…24 To overcome these drawbacks, support materials should be designed with fewer blockages of mass transfer channels, high immobilization capacity, and good stability in reaction environments to improve the practicability and reusability of immobilized enzymes. 2,16 For instance, when designing supports to immobilize lipases, strategies to prevent membrane fouling, such as forming richer pores in the supports as mass transfer channels to reduce blockages caused by compounds, and changing the surface properties of supports to reduce compound deposition can be referenced. 25−28 Lipases (EC 3.1.1.3) are the most popular industrial enzymes in in vitro biocatalysis due to their broad specificity and excellent stability in different solvents.…”

Section: Introductionmentioning

confidence: 99%

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Fe₃O₄ Nanoparticle-Polyacrylonitrile Composite Magnetic Beads Decorated with Candida antarctica Lipase B for Long-Term Reusability in the Hydrolysis of Esters

Lu,

Li,

et al. 2023

ACS Appl. Nano Mater.

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The reusability of immobilized lipases, including their hydrolysis activity, is greatly affected by lipase leakage, mass transfer channel blockage, and compound deposition on the outside surface. In this study, Candida antarctica lipase B (CALB) was immobilized on Fe3O4 nanoparticle-polyacrylonitrile (PAN) composite magnetic beads through phase inversion (L/FP). The hydrolysis activity of lipase was investigated using p-nitrophenyl palmitate (p-npp) as a model ester. To overcome the limitations of immobilized lipase in ester hydrolysis, three modification strategies were employed. First, lipase was covalently immobilized on Fe3O4 nanoparticles modified with methallyl (M9) and chloro (M13) silane modifiers, which exhibited faster immobilization with reduced lipase leaching and higher activity expression and stability. Second, poly(ethylene glycol) (PEG6000) and polylactic acid (PLA) were added to the precursors to physically modify the composite structures of L/FP, resulting in modified beads with larger specific surface area (15.26 m2·g–1) and smaller average pore size (19 nm). The modified beads, L/FP-9-M and L/FP-13-M, demonstrated superior reusability in long-term hydrolysis activity over 250 cycles. L/FP-9-M retained 63 and 34% of the initial activity at the 100th cycle and the 250th cycle, respectively. L/FP-13-M retained 55 and 36% of the initial activity at the 100th cycle and the 250th cycle, respectively. Furthermore, even after 250 repeated uses, the unit activities (U·gsupport –1) of both L/FP-9-M and L/FP-13-M remained higher than the initial activity of Novo 435.

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Renewable, sustainable, and natural lignocellulosic carriers for lipase immobilization: A review

Cited by 19 publications

References 168 publications

Bioactive Covalent Organic Framework Capsules for Lactate Synthesis

Bioactive Covalent Organic Framework Capsules for Lactate Synthesis

The Impact of Bilirubin on 7α- and 7β- Hydroxysteroid Dehydrogenases: Spectra and Docking Analysis

Fe₃O₄ Nanoparticle-Polyacrylonitrile Composite Magnetic Beads Decorated with Candida antarctica Lipase B for Long-Term Reusability in the Hydrolysis of Esters

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Renewable, sustainable, and natural lignocellulosic carriers for lipase immobilization: A review

Cited by 19 publications

References 168 publications

Bioactive Covalent Organic Framework Capsules for Lactate Synthesis

Bioactive Covalent Organic Framework Capsules for Lactate Synthesis

The Impact of Bilirubin on 7α- and 7β- Hydroxysteroid Dehydrogenases: Spectra and Docking Analysis

Fe3O4 Nanoparticle-Polyacrylonitrile Composite Magnetic Beads Decorated with Candida antarctica Lipase B for Long-Term Reusability in the Hydrolysis of Esters

Contact Info

Product

Resources

About

Fe₃O₄ Nanoparticle-Polyacrylonitrile Composite Magnetic Beads Decorated with Candida antarctica Lipase B for Long-Term Reusability in the Hydrolysis of Esters