Annals of the New York Academy of Sciences

, volume 1480 , issue 1 , pages 54-72

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Priya Katyal ¹

Stanley Chu ¹

Jin Kim Montclare ^{1, 2, 3, 4}

Hide authors affiliations Show authors affiliations: 4 affiliations

Department of Chemical and Biomolecular Engineering New York University, Tandon School of Engineering Brooklyn New York |

Department of Radiology New York University Langone Health New York New York |

Department of Biomaterials New York University College of Dentistry New York New York |

⁴

Department of Chemistry New York University New York New York |

Publication type: Journal Article

Publication date: 2020-08-19

Wiley

Annals of the New York Academy of Sciences

scimago Q1

wos Q1

SJR: 1.458

CiteScore: 10.3

Impact factor: 4.8

ISSN: 00778923, 17496632

DOI: 10.1111/nyas.14451

Copy DOI

PubMed ID: 32814367

General Biochemistry, Genetics and Molecular Biology

General Neuroscience

History and Philosophy of Science

Abstract

Organophosphorus compounds (OPs), developed as pesticides and chemical warfare agents, are extremely toxic chemicals that pose a public health risk. Of the different detoxification strategies, organophosphate-hydrolyzing enzymes have attracted much attention, providing a potential route for detoxifying those exposed to OPs. Phosphotriesterase (PTE), also known as organophosphate hydrolase (OPH), is one such enzyme that has been extensively studied as a catalytic bioscavenger. In this review, we will discuss the protein engineering of PTE aimed toward improving the activity and stability of the enzyme. In order to make enzyme utilization in OP detoxification more favorable, enzyme immobilization provides an effective means to increase enzyme activity and stability. Here, we present several such strategies that enhance the storage and operational stability of PTE/OPH.

Found

1 citation

Zvereva Maria

DSc in Chemistry, professor

102 publications, 1 295 citations

h-index: 19

Lomonosov Moscow State University

1 citation

Le-Deygen Irina

🥼 🤝

PhD in Chemistry

68 publications, 2 744 citations, 8 reviews

h-index: 19

Lomonosov Moscow State University

Research interests

Antibiotics

Chitosan

Drug delivery systems

Polymers for drug delivery

Proteins

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GOST |

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Katyal P. et al. Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies // Annals of the New York Academy of Sciences. 2020. Vol. 1480. No. 1. pp. 54-72.

GOST all authors (up to 50) Copy

Katyal P., Chu S., Montclare J. K. Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies // Annals of the New York Academy of Sciences. 2020. Vol. 1480. No. 1. pp. 54-72.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1111/nyas.14451

UR - https://doi.org/10.1111/nyas.14451

TI - Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

T2 - Annals of the New York Academy of Sciences

AU - Katyal, Priya

AU - Chu, Stanley

AU - Montclare, Jin Kim

PY - 2020

DA - 2020/08/19

PB - Wiley

SP - 54-72

IS - 1

VL - 1480

PMID - 32814367

SN - 0077-8923

SN - 1749-6632

ER -

BibTex |

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BibTex (up to 50 authors) Copy

@article{2020_Katyal,

author = {Priya Katyal and Stanley Chu and Jin Kim Montclare},

title = {Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies},

journal = {Annals of the New York Academy of Sciences},

year = {2020},

volume = {1480},

publisher = {Wiley},

month = {aug},

url = {https://doi.org/10.1111/nyas.14451},

number = {1},

pages = {54--72},

doi = {10.1111/nyas.14451}

}

MLA

Cite this

MLA Copy

Katyal, Priya, et al. “Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies.” Annals of the New York Academy of Sciences, vol. 1480, no. 1, Aug. 2020, pp. 54-72. https://doi.org/10.1111/nyas.14451.

Publisher

Wiley

Journal

Annals of the New York Academy of Sciences

scimago Q1

wos Q1

SJR

1.458

CiteScore

10.3

Impact factor

4.8

ISSN

00778923 (Print)

17496632 (Electronic)