Activated magnetic lipase-inorganic hybrid nanoflowers: A highly active and recyclable nanobiocatalyst for biodiesel production

Zhong, Le; Jiao, Xiaobo; Hu, Hongtong; Shen, Xuejian; Zhao, Juan; Feng, Yuxiao; Li, Conghai; Du, Yingjie; Cui, Jiandong; Jia, Shiru

doi:10.1016/j.renene.2021.02.155

Cited by 72 publications

(19 citation statements)

References 48 publications

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“…Later on, Zhong et al immobilized the surfactant-activated lipase from Aspergillus oryzae on Fe 3 O 4 magnetic nanoparticles and embedded the enzyme-functionalized nanoparticles into hybrid nanoflowers (MhNFs) for biodiesel production. 134 The MhNFs produced biodiesel in 88% yield, which was greater than the yield with free lipase (69%). They were able to recycle the MhNF with 76% retained activity after six cycles.…”

Section: Enzyme Immobilization On Various Functionalized Solid Surfac...mentioning

confidence: 85%

“…However, the outcomes may not meet our requirements in many cases because of the limitations and disadvantages of enzyme immobilization mentioned before. 4,14,22,23 In addition to optimization of support materials and immobilization protocols, combination of other techniques such as enzyme activation by chemicals, surfactants, 60,134 and lower-intensity ultrasonic irradiation 71 with enzyme immobilization could convey new opportunities.…”

Section: Enzyme Immobilization On Various Functionalized Solid Surfac...mentioning

confidence: 99%

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Recent Advances in Enzyme Immobilization Utilizing Nanotechnology for Biocatalysis

T.sriwong

Matsuda

2022

Org. Process Res. Dev.

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Enzyme immobilization has been extensively employed in research and industry to improve enzyme stability and allow enzyme recycling. Broad ranges of chemicals and support materials have been utilized for enzyme immobilization. Recent breakthroughs in nanotechnology and materials science have influenced enzyme immobilization technology. Novel approaches for enzyme immobilization have enabled us to access more benefits, for example, excellent activity and stability, cost effectiveness, and the establishment of continuous flow processes. Herewith, this review provides an update on the enzyme immobilization strategies that have been attracting expanding interest in biocatalysis. Organic–inorganic nanocrystal formation, metal–organic frameworks, enzyme immobilization on graphene-based nanomaterials, and enzyme immobilization on functionalized solid surfaces are discussed in detail.

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Section: Enzyme Immobilization On Various Functionalized Solid Surfac...mentioning

confidence: 85%

Section: Enzyme Immobilization On Various Functionalized Solid Surfac...mentioning

confidence: 99%

Recent Advances in Enzyme Immobilization Utilizing Nanotechnology for Biocatalysis

T.sriwong

Matsuda

2022

Org. Process Res. Dev.

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“…Considering that immobilized lipases are highly efficient and environmentally friendly biocatalysts for biodiesel production, developing high-performance lipases is necessary, and many strategies have been developed. − Especially, several oriented enzyme immobilization strategies have been proposed, such as the use of molecular biology to introduce biotags to proteins and the introduction of chemical tags. ,− It is worth noting that such approaches generally require genetic engineering or complicated material fabrication. Nevertheless, the operational complexity and difficulty of these immobilization approaches are not expected.…”

Section: Introductionmentioning

confidence: 99%

Site-Specific and Covalent Immobilization of Lipase on Natural Polyphenol-Modified Magnetic Nanoparticles for Effective Biodiesel Production

Tang

Zhang

et al. 2022

ACS Sustainable Chem. Eng.

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Site-specific and covalent attachment is the most desirable immobilization strategy, but classic methods typically require genetic engineering or complicated material fabrication, resulting in operational complexity and difficulty. Herein, a novel site-specific and covalent immobilization strategy based on accurately selected immobilization sites on lipase was developed. Specifically, computer-aided structural analysis of functional groups on lipase revealed that lysine residues with free amino groups were far away from the catalytic pocket and lid, which were suitable to be chosen as the best immobilization sites to effectively reduce the loss in its activity. Meanwhile, natural polyphenol-modified magnetic nanoparticles could increase the active immobilization sites, and lipase can be immobilized on them directly via a covalent reaction. This site-specific immobilization system exhibited significant enhancement in activity recovery (71.3%) compared to random immobilization (42.5 and 55.9%). As expected, experimental and computational analyses revealed that tailor-made site-specific immobilization carriers were beneficial to maintain the native catalytic pocket conformation and enhance the rigidity of the immobilized lipase, which exhibited a higher biodiesel yield (92.1%) than free and randomly immobilized lipases. Besides, the site-specifically immobilized lipase could maintain as high as 75.3% biodiesel yield after eight cycles, making it an ideal nanocatalyst for efficient production of biodiesel. Overall, the site-specific enzyme immobilization technology can provide stable catalytic activity advantages over the randomly covalent immobilization strategy, which can significantly promote green manufacturing and sustainable production.

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“…In the last decade, the production of hybrid enzyme nanoflowers proved to be an immobilization method able to improve some enzyme features, such as enzyme stability and activity [ 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 ]. In some cases, this technique has been applied to immobilize lipases [ 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 , 88 , 89 ].…”

Section: Introductionmentioning

confidence: 99%

Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts

et al. 2022

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Four commercial immobilized lipases biocatalysts have been submitted to modifications with different metal (zinc, cobalt or copper) phosphates to check the effects of this modification on enzyme features. The lipase preparations were Lipozyme®TL (TLL-IM) (lipase from Thermomyces lanuginose), Lipozyme®435 (L435) (lipase B from Candida antarctica), Lipozyme®RM (RML-IM), and LipuraSelect (LS-IM) (both from lipase from Rhizomucor miehei). The modifications greatly altered enzyme specificity, increasing the activity versus some substrates (e.g., TLL-IM modified with zinc phosphate in hydrolysis of triacetin) while decreasing the activity versus other substrates (the same preparation in activity versus R- or S- methyl mandelate). Enantiospecificity was also drastically altered after these modifications, e.g., LS-IM increased the activity versus the R isomer while decreasing the activity versus the S isomer when treated with copper phosphate. Regarding the enzyme stability, it was significantly improved using octyl-agarose-lipases. Using all these commercial biocatalysts, no significant positive effects were found; in fact, a decrease in enzyme stability was usually detected. The results point towards the possibility of a battery of biocatalysts, including many different metal phosphates and immobilization protocols, being a good opportunity to tune enzyme features, increasing the possibilities of having biocatalysts that may be suitable for a specific process.

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Activated magnetic lipase-inorganic hybrid nanoflowers: A highly active and recyclable nanobiocatalyst for biodiesel production

Cited by 72 publications

References 48 publications

Recent Advances in Enzyme Immobilization Utilizing Nanotechnology for Biocatalysis

Recent Advances in Enzyme Immobilization Utilizing Nanotechnology for Biocatalysis

Site-Specific and Covalent Immobilization of Lipase on Natural Polyphenol-Modified Magnetic Nanoparticles for Effective Biodiesel Production

Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts

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