Taguchi design-assisted co-immobilization of lipase A and B from Candida antarctica onto chitosan: Characterization, kinetic resolution application, and docking studies

Moreira, Katerine da Silva; Oliveira, André Luiz Barros de; Júnior, Lourembergue Saraiva de Moura; Sousa, Isamayra Germano de; Cavalcante, Antônio Luthierre Gama; Neto, Francisco Simão; Valério, Roberta Bussons Rodrigues; Chaves, Anderson Valério; Fonseca, Thiago de Sousa; Cruz, Daniel Morais Vieira; Lima, Gledson Vieira; Oliveira, Gabriel P. de; Souza, Monique; Fechine, Pierre Basílio Almeida; Mattos, Marcos Carlos de; Fonseca, Aluísio Marques da; Santos, José Cleiton Sousa dos

doi:10.1016/j.cherd.2021.10.033

Cited by 76 publications

(41 citation statements)

References 200 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzymes have been widely used as natural biocatalysts in the pharmaceutical, chemical, and food industries, in addition to their well-known applications in medicine and in effluent and solid-waste treatment systems [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 ]. This is mainly due to the diversity of reactions enabled by biocatalysts, as well as their high efficiency, specificity, and selectivity [ 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 ]. Furthermore, enzymes are biocompatible and biodegradable structures that can be derived from renewable resources [ 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 ].…”

Section: Introductionmentioning

confidence: 99%

“…Additionally, immobilized enzymes show very little to no allergenicity, high recoveries, and a reuse capacity, rendering processes more economical [ 29 , 53 ]. To increase the stability of the enzymes during storage and make them more resistant to operational conditions, several types of support for enzyme immobilization have been studied, including magnetic nanoparticles, sol-gels, mesoporous silica, and polymers [ 17 , 27 , 43 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 . Immobilization technologies can also prevent subunit dissociation, aggregation, autolysis, and proteolysis, apart from delivering more suitable reaction microenvironments [ 73 , 74 , 75 , 76 ].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

et al. 2022

View full text Add to dashboard Cite

Enzymatic biocatalysis is a sustainable technology. Enzymes are versatile and highly efficient biocatalysts, and have been widely employed due to their biodegradable nature. However, because the three-dimensional structure of these enzymes is predominantly maintained by weaker non-covalent interactions, external conditions, such as temperature and pH variations, as well as the presence of chemical compounds, can modify or even neutralize their biological activity. The enablement of this category of processes is the result of the several advances in the areas of molecular biology and biotechnology achieved over the past two decades. In this scenario, metal–organic frameworks (MOFs) are highlighted as efficient supports for enzyme immobilization. They can be used to ‘house’ a specific enzyme, providing it with protection from environmental influences. This review discusses MOFs as structures; emphasizes their synthesis strategies, properties, and applications; explores the existing methods of using immobilization processes of various enzymes; and lists their possible chemical modifications and combinations with other compounds to formulate the ideal supports for a given application.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

et al. 2022

View full text Add to dashboard Cite

show abstract

“…Lipases have recently emerged as a leading biocatalyst/bioaccelerator (Lima et al., 2017) and served as a potential contributor to this multibillion‐dollar industry, with multifaceted applications in both industries and in situ lipid metabolism (Moreira et al., 2022; Vanleeuw et al., 2019). Lipases have been recently used as a potential biocatalyst in a large number of biotechnological sciences, more specifically, dairy products (cheese recovery, flavor enhancement, and the production of enzyme‐modified cheese), detergents, pharmaceuticals (ibuprofen, naproxen), chemicals, agriculture products (pesticides, insects), and oil chemistry (fat and oil hydrolysis and the synthesis of biodetergents) (Cavalcante, Neto, et al., 2021).…”

Section: Introductionmentioning

confidence: 99%

Rebuilding the lid region from conformational and dynamic features to engineering applications of lipase in foods: Current status and future prospects

Chen

Khan

He³

et al. 2022

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

The applications of lipases in esterification, amidation, and transesterification have broadened their potential in the production of fine compounds with high cumulative values. Mostly, the catalytic triad of lipases is covered by either one or two mobile peptides called the “lid” that control the substrate channel to the catalytic center. The lid holds unique conformational allostery via interfacial activation to regulate the dynamics and catalytic functions of lipases, thereby highlighting its importance in redesigning these enzymes for industrial applications. The structural characteristic of lipase, the dynamics of lids, and the roles of lid in lipase catalysis were summarized, providing opportunities for rebuilding lid region by biotechniques (e.g., metagenomic technology and protein engineering) and enzyme immobilization. The review focused on the advantages and disadvantages of strategies rebuilding the lid region. The main shortcomings of biotechnologies on lid rebuilding were discussed such as negative effects on lipase (e.g., a decrease of activity). Additionally, the main shortcomings (e.g., enzyme desorption at high temperatre) in immobilization on hydrophobic supports via interfacial action were presented. Solutions to the mentioned problems were proposed by combinations of computational design with biotechnologies, and improvements of lipase immobilization (e.g., immobilization protocols and support design). Finally, the review provides future perspectives about designing hyperfunctional lipases as biocatalysts in the food industry based on lid conformation and dynamics.

show abstract

“…However, all these remarkable characteristics of enzymes and their widespread use in various fields of application are often hampered by their unstable structure, short lifetime, separation problems and high costs in enzymatic recycling [ 5 , 6 ]. Although many techniques such as modification or protein engineering have been employed to improve the enzyme catalytic functions and recyclability of the biocatalyst, enzyme immobilization is thought to be one of the strategies to overcome these problems [ 7 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Comparative Studies of Glucose Oxidase Immobilized on Fe3O4 Magnetic Nanoparticles Using Different Coupling Agents

Rusu¹,

Chiriac²,

Niţă³

et al. 2022

Nanomaterials

View full text Add to dashboard Cite

Squaric acid (SA) is a compound with potential to crosslink biomacromolecules. Although SA has become over the last years a well-known crosslinking agent as a result of its good biocompatibility, glutaraldehyde (GA), a compound with proven cytotoxicity is still one of the most used crosslinkers to develop nanomaterials. In this regard, the novelty of the present study consists in determining whether it may be possible to substitute GA with a new bifunctional and biocompatible compound, such as SA, in the process of enzyme immobilization on the surface of magnetic nanoparticles (MNPs). Thus, a direct comparison between SA- and GA-functionalized magnetic nanoparticles was realized in terms of physico-chemical properties and ability to immobilize catalytic enzymes. The optimal conditions of the synthesis of the two types of GOx-immobilized MNPs were described, thus emphasizing the difference between the two reagents. Scanning Electron Microscopy and Dynamic Light Scattering were used for size, shape and colloidal stability characterization of the pristine MNPs and of those coupled with GOx. Binding of GOx to MNPs by using GA or SA was confirmed by FT-IR spectroscopy. The stability of the immobilized and free enzyme was investigated by measuring the enzymatic activity. The study confirmed that the resulting activity of the immobilized enzyme and the optimization of enzyme immobilization depended on the type of reagent used and duration of the process. The catalytic performance of immobilized enzyme was tested, revealing that the long-term colloidal stability of SA-functionalized MNPs was superior to those prepared with GA. In conclusion, the SA-functionalized bioconjugates have a better potential as compared to the GA-modified nanosystems to be regarded as catalytic nanodevices for biomedical purposes such as biosensors.

show abstract

Taguchi design-assisted co-immobilization of lipase A and B from Candida antarctica onto chitosan: Characterization, kinetic resolution application, and docking studies

Cited by 76 publications

References 200 publications

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

Rebuilding the lid region from conformational and dynamic features to engineering applications of lipase in foods: Current status and future prospects

Synthesis and Comparative Studies of Glucose Oxidase Immobilized on Fe3O4 Magnetic Nanoparticles Using Different Coupling Agents

Contact Info

Product

Resources

About