Enhanced enzymatic performance of immobilized lipase on metal organic frameworks with superhydrophobic coating for biodiesel production

Zhong, Le; Feng, Yuxiao; Hu, Hongtong; Xu, Jiabao; Wang, Ziyuan; Du, Yingjie; Cui, Jiandong; Jia, Shiru

doi:10.1016/j.jcis.2021.06.017

Cited by 90 publications

(44 citation statements)

References 83 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, Liang et al [43] described enhanced activity of catalase immobilized via one-pot synthesis in a hydrophilic environment when the linker of the MOF was 3methyl-1,2,4-triazole (FCAT@MAF-7) compared to the hydrophobic FCAT-ZIF-8, where the enzyme undergoes inactivation. Lipase, being an enzyme which displays more activity in hydrophobic interfaces, was found to increase its activity in the hydrophobic environment created in the immobilization of lipase onto ZIF-L (AOL@PDMS-ZIF-L) and improves its stability in ZIF-8 (AOL@PDMS-ZIF-8) by the addition of PDMS (polydimethylsiloxane) to provide a hydrophobic environment [44].…”

Section: The Origins and Rising Dominance Of The Enzyme-supporting Mofmentioning

confidence: 99%

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

et al. 2021

View full text Add to dashboard Cite

The industrial use of enzymes generally necessitates their immobilization onto solid supports. The well-known high affinity of enzymes for metal-organic framework (MOF) materials, together with the great versatility of MOFs in terms of structure, composition, functionalization and synthetic approaches, has led the scientific community to develop very different strategies for the immobilization of enzymes in/on MOFs. This review focuses on one of these strategies, namely, the one-pot enzyme immobilization within sustainable MOFs, which is particularly enticing as the resultant biocomposite Enzyme@MOFs have the potential to be: (i) prepared in situ, that is, in just one step; (ii) may be synthesized under sustainable conditions: with water as the sole solvent at room temperature with moderate pHs, etc.; (iii) are able to retain high enzyme loading; (iv) have negligible protein leaching; and (v) give enzymatic activities approaching that given by the corresponding free enzymes. Moreover, this methodology seems to be near-universal, as success has been achieved with different MOFs, with different enzymes and for different applications. So far, the metal ions forming the MOF materials have been chosen according to their low price, low toxicity and, of course, their possibility for generating MOFs at room temperature in water, in order to close the cycle of economic, environmental and energy sustainability in the synthesis, application and disposal life cycle.

show abstract

Section: The Origins and Rising Dominance Of The Enzyme-supporting Mofmentioning

confidence: 99%

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

et al. 2021

View full text Add to dashboard Cite

show abstract

“…As a porous material, the metal–organic framework cannot only immobilize the enzyme and protect the rigid structure of the enzyme but also make the enzyme and the substrate fully in contact. 14 It has been widely used for the research of enzyme immobilization. However, it is difficult to directly use 3D-printing technologies to make complex structures because most of them are synthesized with loose particles.…”

Section: D Printing Materials For Enzyme Immobilizationmentioning

confidence: 99%

Emerging 3D Printing Strategies for Enzyme Immobilization: Materials, Methods, and Applications

et al. 2022

View full text Add to dashboard Cite

As the strategies of enzyme immobilization possess attractive advantages that contribute to realizing recovery or reuse of enzymes and improving their stability, they have become one of the most desirable techniques in industrial catalysis, biosensing, and biomedicine. Among them, 3D printing is the emerging and most potential enzyme immobilization strategy. The main advantages of 3D printing strategies for enzyme immobilization are that they can directly produce complex channel structures at low cost, and the printed scaffolds with immobilized enzymes can be completely modified just by changing the original design graphics. In this review, a comprehensive set of developments in the fields of 3D printing techniques, materials, and strategies for enzyme immobilization and the potential applications in industry and biomedicine are summarized. In addition, we put forward some challenges and possible solutions for the development of this field and some possible development directions in the future.

show abstract

“…They present high activity, good stability, unique selectivity, and specificity. Therefore, they have been widely used in many fields of biotechnology and bioengineering [1][2][3][4][5]. In order to enhance its stability and reusability, lipases can be immobilized on various supports by techniques such as physical adsorption, embedding, covalent binding, and cross-linking [6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

“…The outer surface of the "lid" is relatively hydrophilic, while the inner surface is relatively hydrophobic [1]. While the hydrophobic interface exists, the "lid" moves, and the α-helix is reoriented to expose the active center [4]; thus, the lipase is fixed and adsorbed on the hydrophobic surface in an open form and maintains high activity [12]. Due to the hydrophobic interaction between the hydrophobic surface and the lipase, the enzyme can be activated from an inactive (closed cap) state to an active (open cap) 2 of 12 state, which is called "interface activation" [13][14][15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

“…Due to the hydrophobic interaction between the hydrophobic surface and the lipase, the enzyme can be activated from an inactive (closed cap) state to an active (open cap) 2 of 12 state, which is called "interface activation" [13][14][15][16][17][18]. Moreover, the combination of lipase and a hydrophobic surface is very strong and occurs quickly [4]. The hydrophobic interface reduces hydrogen bond interactions between lipase and water, and the enzyme forms an incomplete hydration layer, while the aliphatic sidechains of hydrophobic substrates fold onto the surface of enzyme molecules to maintain open conformation, and it improves the catalytic efficiency of enzyme reaction [1].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Immobilization of Lipases on Modified Silica Clay for Bio-Diesel Production: The Effect of Surface Hydrophobicity on Performance

Duan

Zou

et al. 2022

Catalysts

View full text Add to dashboard Cite

The hydrophobicity of a support plays a critical role in the catalytic efficiency of immobilized lipases. 3-aminopropyltriethoxysilane (APTES)-modified silica clay (A-SC) was coupled with silane coupling agents of different alkyl chains (methyl triethoxysilane, vinyl triethoxysilane, octyl triethoxysilane, and dodecyl triethoxysilane) to prepare a series of hydrophobic support for lipase immobilization. The lipases were immobilized onto the support by conducting glutaraldehyde cross-linking processes. The results showed that the activity of the immobilized biocatalyst increased with hydrophobicity. The hydrolytic activity of Lip-Glu-C12-SC (contact angle 119.8°) can reach 5900 U/g, which was about three times that of Lip-Glu-A-SC (contact angle 46.5°). The immobilized lipase was applied as a biocatalyst for biodiesel production. The results showed that the catalytic yield of biodiesel with highly hydrophobic Lip-Glu-C12-SC could be as high as 96%, which is about 30% higher than that of Lip-Glu-A-SC. After being recycled five times, the immobilized lipase still maintained good catalytic activity and stability. This study provides a good strategy to improve the efficiency of immobilized lipases, showing great potential for future industrial application on biodiesel production.

show abstract

Enhanced enzymatic performance of immobilized lipase on metal organic frameworks with superhydrophobic coating for biodiesel production

Cited by 90 publications

References 83 publications

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

Emerging 3D Printing Strategies for Enzyme Immobilization: Materials, Methods, and Applications

Immobilization of Lipases on Modified Silica Clay for Bio-Diesel Production: The Effect of Surface Hydrophobicity on Performance

Contact Info

Product

Resources

About