immobilized enzymes
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2022 ◽  
pp. 33-46
Author(s):  
Angitha Balan ◽  
Vaisiri V. Murthy ◽  
Ravi Kumar Kadeppagari
Keyword(s):  

3 Biotech ◽  
2022 ◽  
Vol 12 (1) ◽  
Author(s):  
Sâmilla Gabriella Coelho de Almeida ◽  
Giuliano Formaggio de Mello ◽  
Miquéias Gomes do Santos ◽  
Débora D. Virginio da Silva ◽  
Ellen Cristine Giese ◽  
...  

Author(s):  
Jacob H. Forstater ◽  
Shane T. Grosser

The authors describe an automated, data-rich screening and process development method for rapid discovery, development, and optimization of immobilized enzymes, critical to many biocatalytic processes.


2022 ◽  
Vol 153 ◽  
pp. 111765
Author(s):  
Luciana da Silva Dutra ◽  
Martina Costa Cerqueira Pinto ◽  
Eliane Pereira Cipolatti ◽  
Erika Cristina G. Aguieiras ◽  
Evelin Andrade Manoel ◽  
...  

2022 ◽  
Vol 82 ◽  
Author(s):  
S.-S. Ding ◽  
J.-P. Zhu ◽  
Y. Wang ◽  
Y. Yu ◽  
Z. Zhao

Abstract Enzymes immobilized onto substrates with excellent selectivity and activity show a high stability and can withstand extreme experimental conditions, and their performance has been shown to be retained after repeated uses. Applications of immobilized enzymes in various fields benefit from their unique characteristics. Common methods, including adsorption, encapsulation, covalent attachment and crosslinking, and other emerging approaches (e.g., MOFs) of enzyme immobilization have been developed mostly in recent years. In accordance with these immobilization methods, the present review elaborates the application of magnetic separable nanoparticles and functionalized SBA-15 and MCM-41 mesoporous materials used in the immobilization of enzymes.


2021 ◽  
Vol 23 (1) ◽  
pp. 272
Author(s):  
Jakub Zdarta ◽  
Oliwia Degórska ◽  
Katarzyna Jankowska ◽  
Agnieszka Rybarczyk ◽  
Adam Piasecki ◽  
...  

Enzymatic conversion of pharmaceutically active ingredients (API), using immobilized enzymes should be considered as a promising industrial tool due to improved reusability and stability of the biocatalysts at harsh process conditions. Therefore, in this study horseradish peroxidase was immobilized into sodium alginate capsules and then trapped into poly(vinyl chloride) electrospun fibers to provide additional enzyme stabilization and protection against the negative effect of harsh process conditions. Due to encapsulation immobilization, 100% of immobilization yield was achieved leading to loading of 25 μg of enzyme in 1 mg of the support. Immobilized in such a way, enzyme showed over 80% activity retention. Further, only slight changes in kinetic parameters of free (Km = 1.54 mM) and immobilized horseradish peroxidase (Km = 1.83 mM) were noticed, indicating retention of high catalytic properties and high substrate affinity by encapsulated biocatalyst. Encapsulated horseradish peroxidase was tested in biodegradation of two frequently occurring in wastewater API, sulfamethoxazole (antibiotic) and carbamazepine (anticonvulsant). Over 80% of both pharmaceutics was removed by immobilized enzyme after 24 h of the process from the solution at a concentration of 1 mg/L, under optimal conditions, which were found to be pH 7, temperature 25 °C and 2 mM of H2O2. However, even from 10 mg/L solutions, it was possible to remove over 40% of both pharmaceuticals. Finally, the reusability and storage stability study of immobilized horseradish peroxidase showed retention of over 60% of initial activity after 20 days of storage at 4 °C and after 10 repeated catalytic cycles, indicating great practical application potential. By contrast, the free enzyme showed less than 20% of its initial activity after 20 days of storage and exhibited no recycling potential.


Author(s):  
Jéssica Luzardo ◽  
Douglas Aguiar ◽  
Alexander Silva ◽  
Sanair Oliveira ◽  
Braulio Archanjo ◽  
...  

The use of enzymes as catalysts requires recovery and reuse to make the process viable. Enzymatic immobilization changes enzyme stability, activity, and specificity. It is very important to explore new substrates for immobilization with appropriate composition and structure to improve the efficiency of the immobilized enzymes. This work explores the use of two different graphene oxide papers, one produced by oxidation route (GO) and the other by electrochemical synthesis (EG), aiming for β-galactosidase immobilization. The chemical and structural properties of these two papers were characterized by Raman spectroscopy, X-ray photoelectron spectroscopy and X-ray diffraction. Atomic force microscopy images showed that EG paper ensured more efficient immobilization of the enzymes on the surface of the paper. Cyclic voltammetry was used to monitor the reaction of conversion of lactose to glucose in the free enzyme solution and graphene paper immobilized enzyme solutions. The cyclic voltammetry analysis showed that immobilized enzymes on GO paper showed an improvement in the activity of β-galactose when compared to free enzyme solution, as well as enzyme immobilized on a glassy carbon electrode.


2021 ◽  
Vol 45 (1) ◽  
Author(s):  
Mohammad Rafiq Khan

Abstract Background This article is a comprehensive review of the events recorded in the history of enzymology from twentieth century to the recent work of author’s groups on different biochemical aspects of the immobilized enzymes. The review differs from those presented before on the basis that it is not limited to one or few aspects. It extends its spectrum to a large number of aspects from the definition to biomedical applications of immobilized enzymes. Main body The author and his associates have proposed modification of classification of immobilized enzymes by Enzyme Engineering Conference 1971. His groups have worked on cell bound proteases of medicinal seeds and have given them the name of “naturally immobilized enzymes”. Thus, the author proposes that the enzymes may be basically classified into “naturally immobilized enzymes” and “artificially immobilized enzymes”. The artificially immobilized enzymes may be further sub-classified as done in 1971. Conclusion The classification suggested above sounds logical and thus acceptable to the author and his associates. The author and his associates also suggest some applications on the basis of their results on naturally immobilized enzymes.


2021 ◽  
Author(s):  
Areej Shahbaz ◽  
Nazim Hussain ◽  
Azeem Intisar ◽  
Muhammad Bilal ◽  
Hafiz M. N. Iqbal
Keyword(s):  

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