dc.contributor.author |
Makam, Pandeeswar |
|
dc.contributor.author |
Yamijala, Sharma S. R. K. C. |
|
dc.contributor.author |
Bhadram, Venkata S. |
|
dc.contributor.author |
Shimon, Linda J. W. |
|
dc.contributor.author |
Wong, Bryan M. |
|
dc.contributor.author |
Gazit, Ehud |
|
dc.date.accessioned |
2023-04-17T12:03:21Z |
|
dc.date.available |
2023-04-17T12:03:21Z |
|
dc.date.issued |
2022-12 |
|
dc.identifier.issn |
20411723 |
|
dc.identifier.uri |
http://localhost:8080/xmlui/handle/123456789/2055 |
|
dc.description |
This paper is submitted by the author of IIT (BHU), Varanasi |
en_US |
dc.description.abstract |
Enzymes are extremely complex catalytic structures with immense biological and technological importance. Nevertheless, their widespread environmental implementation faces several challenges, including high production costs, low operational stability, and intricate recovery and reusability. Therefore, the de novo design of minimalistic biomolecular nanomaterials that can efficiently mimic the biocatalytic function (bionanozymes) and overcome the limitations of natural enzymes is a critical goal in biomolecular engineering. Here, we report an exceptionally simple yet highly active and robust single amino acid bionanozyme that can catalyze the rapid oxidation of environmentally toxic phenolic contaminates and serves as an ultrasensitive tool to detect biologically important neurotransmitters similar to the laccase enzyme. While inspired by the laccase catalytic site, the substantially simpler copper-coordinated bionanozyme is ∼5400 times more cost-effective, four orders more efficient, and 36 times more sensitive compared to the natural protein. Furthermore, the designed mimic is stable under extreme conditions (pH, ionic strength, temperature, storage time), markedly reusable for several cycles, and displays broad substrate specificity. These findings hold great promise in developing efficient bionanozymes for analytical chemistry, environmental protection, and biotechnology. |
en_US |
dc.description.sponsorship |
Airforce research laboratories |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Nature Research |
en_US |
dc.relation.ispartofseries |
Nature Communications; Article number 1505 |
|
dc.subject |
Amino Acids; Catalysis; Environmental Restoration and Remediation; Laccase; Phenols; 2,4 dichlorophenol; amino acid; copper; cysteine; DOPA decarboxylase inhibitor; dopamine 1 receptor; epinephrine; glucose oxidase; glycine; histidine; hydrogen peroxide; laccase; metal organic framework; metal oxide; monophenol monooxygenase; neurotransmitter; noradrenalin; phenylalanine; river water; sodium hydroxide; amino acid; laccase; phenol derivative; amino acid; bioengineering; bioremediation; catalysis; enzyme activity; phenolic compound; ABTS radical scavenging assay; anaphylaxis; Article; atomic absorption spectrometry; atomic force microscopy; bioremediation; biotechnology; catalysis; catalyst; chemical reaction kinetics; colorimetry; computer analysis; cost effectiveness analysis; crystal structure; crystallization; density functional theory; DPPH radical scavenging assay; ecosystem restoration; electrochemical analysis; electron spin resonance; energy dispersive X ray spectroscopy; environmental aspects and related phenomena; environmental protection; enzyme activity; enzyme specificity; fluorescence microscopy; Fourier transform infrared spectroscopy; high resolution scanning electron microscopy; hydrogen bond; in vitro study; ionic strength; limit of detection; mass spectrometry; microscopy; oxidation kinetics; pH; polymerization; range of motion; static electricity; storage temperature; storage time; temperature; thermogravimetry; thermostability; X ray crystallography; X ray diffraction; catalysis; ecosystem restoration; metabolism |
en_US |
dc.title |
Single amino acid bionanozyme for environmental remediation |
en_US |
dc.type |
Article |
en_US |