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Mark A. Guelta

Researcher at Edgewood Chemical Biological Center

Publications -  15
Citations -  494

Mark A. Guelta is an academic researcher from Edgewood Chemical Biological Center. The author has contributed to research in topics: Organophosphorus acid anhydrolase & Organophosphorus compound. The author has an hindex of 4, co-authored 15 publications receiving 385 citations.

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Journal ArticleDOI

Encapsulation of a Nerve Agent Detoxifying Enzyme by a Mesoporous Zirconium Metal-Organic Framework Engenders Thermal and Long-Term Stability.

TL;DR: For the first time, a nerve agent detoxifying enzyme, organophosphorus acid anhydrolase (OPAA), has been successfully encapsulated into a water-stable zirconium metal-organic framework (MOF), which features a hierarchical mesoporous channel structure and exhibits a 12 wt % loading capacity.
Journal ArticleDOI

Nanosizing a Metal-Organic Framework Enzyme Carrier for Accelerating Nerve Agent Hydrolysis.

TL;DR: The synthesis and characterization of a water-stable zirconium metal-organic framework (MOF), NU-1003, featuring the largest mesoporous aperture known for a zIRconium MOF, is reported, highlighting a method for rapid and highly efficient hydrolysis of nerve agents using nanosized enzyme carriers.
Book ChapterDOI

Biodegradation of Hydrolyzed Chemical Warfare Agents by Bacterial Consortia

TL;DR: The U.S. Army has custody of chemical weapons (CW) containing nerve and blister (vesicant) agents located in eight sites in the continental United States and at Johnston Island, a small island in the Pacific Ocean as discussed by the authors.

Biodegradation and Oxidation Approaches for the Demilitarization of VX Hydrolysate

TL;DR: In this article, the U.S. Army is required to destroy its stockpile of chemical warfare agents (30,000 tons) by April 2007, and public and political opposition to incineration lead to evaluation of several alternative technologies, including biodegradation 1.
Patent

OPAA FL—a mutant enzyme with increased catalytic efficiency on organophosphorus compound GD

TL;DR: In this article, a non-wild-type organophosphorus acid anhydrolase enzyme with two site mutations, method of production, and method of use to more effectively degrade toxic organophorus compounds and, in particular, toxic chemical GD (3,3-Dimethylbutan-2-ylmethylphosphonofluoridate), was proposed.