Nano-organic supports for enzyme immobilization: Scopes and perspectives

Zahirinejad, Sahar; Hemmati, Roohullah; Homaei, Ahmad; Dinari, Ali; Hosseinkhani, Saman; Mohammadi, Soheila; Vianello, Fábio

doi:10.1016/j.colsurfb.2021.111774

Cited by 140 publications

(48 citation statements)

References 104 publications

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“…Other characteristics that justify the use of nanofibers are the high adhesion capacity of enzymes with a homogeneous dispersion, less probability of denaturation and enzymatic dysfunctions, and less resistance to mass transfer. [27] Adsorption on electrospinning PAN membranes is the easiest and least expansive method of immobilization. However, despite providing high enzymatic retention on the support, it is less efficient than covalent binding, as the adsorbed enzymes are more likely to be gradually released with the reuse of the biocatalyst.…”

Section: R E C O R D R E V I E W T H E C H E M I C a L R E C O R Dmentioning

confidence: 99%

A Perspective Review on the Application of Polyacrylonitrile‐Based Supports for Laccase Immobilization

Vieira

Gurgel

Henriques

et al. 2021

The Chemical Record

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The use of laccases applied in bioremediation processes has been increasingly studied, given the urgent need to overcome the environmental problems caused by emerging contaminants. It is known that immobilized enzymes have better operational stability under reaction conditions, allowing for greater applicability. However, given the lack of commercially available immobilized laccases, the search for immobilization materials and methods continues to gain effort. The use of polyacrylonitrile (PAN) to immobilize enzymes has been investigated since it is a low-cost material and can be modified and functionalized to well interact with the enzyme. This polymer can be used with different morphologies such as fibers, beads, and coreshell, presenting as an easily applicable alternative. This review presents the missing link between polymer and enzyme through an overview of PAN's current use as support for laccase immobilization and polymer functionalization methods, considering the importance of immobilized laccases in several industrial sectors.

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Section: R E C O R D R E V I E W T H E C H E M I C a L R E C O R Dmentioning

confidence: 99%

A Perspective Review on the Application of Polyacrylonitrile‐Based Supports for Laccase Immobilization

Vieira

Gurgel

Henriques

et al. 2021

The Chemical Record

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“…The materials considered as enzyme supports should be physically stable against mechanical deformations, possess many enzyme binding sites, be microbe resistant, biologically compatible, commercially available, and have a good cost-performance relation. 47 In addition, supports should provide a suitable microenvironment for catalysis after enzyme immobilization, which implies a good diffusion rate for both substrate and products, 48 as well as an easy way for the separation from the reaction media. 42 Supports may be classified into organic and inorganic materials; examples of organic supports are synthetic polymers, such as polypropylene and polyvinyl resin.…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

“…39 For example, new hybrid nano-supports are attractive materials for the immobilization of enzymes that allows the formation of multienzyme biocatalytic systems applicable to environmental processes and food additive production. 48,49 Metalorganic frameworks (MOFs) are an example of porous nanomaterials that are good matrices for enzyme immobilization due to their high surface area and the possibility of easy pore size design. 50 In the future, the immobilization of multi-enzymes, along with cofactor regeneration and retention, could be gainfully exploited in the development of biochemical processes that involve complex chemical conversions.…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

Polypropylene as a selective support for the immobilization of lipolytic enzymes: hyper‐activation, purification and biotechnological applications

Sánchez-Otero

Quintana‐Castro

Rojas-Vázquez

et al. 2021

J of Chemical Tech & Biotech

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Lipases are the versatile biological catalysts used in a wide range of commercial synthetic applications. Microbial lipases have been widely used in the pharmaceutical, food, textile, oleochemical, paper, and bioenergy industries, in the composition of detergents, and in the production of polymers and enantiomerically pure chemical intermediates. Lipases have a unique lid opening mechanism that makes them interesting biocatalysts to catalyze reactions in hydrophobic environments. Water insoluble substrates have also been efficiently transformed by lipases in organic solvents. The use of lipases in industrial processes could be limited by the cost of their production, the difficulties in their recovery and disposal, or by the harsh conditions of some processes that could inactivate or denature the protein. The immobilization of enzymes helps overcome these physical and economical drawbacks, making the catalyst more active, stable, and reusable, resulting in the reduction of costs and of contaminating and harmful byproducts. Polypropylene has unique properties that aid in the activation of the lid opening mechanism and improve the catalytic efficiency of immobilized lipases. The aim of this review is to present an overview of the uses of polypropylene as a support for immobilization of lipolytic enzymes, the study of the immobilization procedure conditions, the characteristics of the immobilized enzymes, and the perspectives of their use in the future as a powerful tool in sustainable industry.

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“…Boosting the catalytic activity and operational stability of enzymes and facilitating their recovery and reuse, are considered the primary objectives of enzyme immobilization 1 , 2 . To take advantage of practical utilization of the immobilized enzymes, some contributing factors should be noticed, such as choosing the proper immobilization protocols and the appropriate support materials for minimizing the risks of subunit dissociation, deactivation, aggregation, autolysis, or leaching of the enzymes 3 – 5 .…”

Section: Introductionmentioning

confidence: 99%

Synthesis of two novel bio-based hydrogels using sodium alginate and chitosan and their proficiency in physical immobilization of enzymes

Shakeri

Ariaeenejad

Ghollasi

et al. 2022

Sci Rep

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Herein, four novel and bio-based hydrogel samples using sodium alginate (SA) and chitosan (CH) grafted with acrylamide (AAm) and glycidyl methacrylate (GMA) and their reinforced nanocomposites with graphene oxide (GO) were synthesized and coded as SA-g-(AAm-co-GMA), CH-g-(AAm-co-GMA), GO/SA-g-(AAm-co-GMA), and GO/CH-g-(AAm-co-GMA), respectively. The morphology, net charge, and water absorption capacity of samples were entirely changed by switching the biopolymer from SA to CH and adding a nano-filler. The proficiencies of hydrogels were compared in the immobilization of a model metagenomic-derived xylanase (PersiXyn9). The best performance was observed for GO/SA-g-poly(AAm-co-GMA) sample indicating better stabilizing electrostatic attractions between PersiXyn9 and reinforced SA-based hydrogel. Compared to the free enzyme, the immobilized PersiXyn9 on reinforced SA-based hydrogel showed a 110.1% increase in the released reducing sugar and almost double relative activity after 180 min storage. While immobilized enzyme on SA-based hydrogel displayed 58.7% activity after twelve reuse cycles, the enzyme on CH-based carrier just retained 8.5% activity after similar runs.

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Nano-organic supports for enzyme immobilization: Scopes and perspectives

Cited by 140 publications

References 104 publications

A Perspective Review on the Application of Polyacrylonitrile‐Based Supports for Laccase Immobilization

A Perspective Review on the Application of Polyacrylonitrile‐Based Supports for Laccase Immobilization

Polypropylene as a selective support for the immobilization of lipolytic enzymes: hyper‐activation, purification and biotechnological applications

Synthesis of two novel bio-based hydrogels using sodium alginate and chitosan and their proficiency in physical immobilization of enzymes

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