Enhancing the stability and catalytic efficiency of alkyl halide dehalogenase through poloxamer temperature-sensitive gel
Jianjun Zhu, Jun Zhang, Feng Gong, Qiong Yu, Xuan Guo, Yu Wang

TL;DR
Researchers improved the stability and efficiency of an enzyme that breaks down mustard gas by encapsulating it in a temperature-sensitive gel.
Contribution
A novel method using poloxamer thermosensitive gels to enhance the stability and catalytic performance of Dha A is introduced.
Findings
Encapsulation in poloxamer gel increased Dha A's solubility and catalytic efficiency for bis(2-chloroethyl) ether.
The gel improved storage and thermal stability of Dha A at 32°C through a tightly packed structure.
Hydrogen bonding between Dha A and poloxamer molecules was observed at an optimal gelation temperature of 25°C.
Abstract
Dha A, a biocatalyst with pronounced efficacy in the degradation of mustard gas, is constrained by its inherent instability, which impedes its broader application. In this study, we encapsulated Dha A within a poloxamer-based thermosensitive hydrogel, a widely utilized protein carrier, to assess its physicochemical characteristics, catalytic performance, and stability enhancement. The Dha A-loaded thermosensitive gel (Dha A@TSG) exhibited interactions between Dha A and poloxamer molecules via hydrogen bonding, with an optimal gelation temperature of 25°C. This encapsulation strategy significantly enhanced the solubility and catalytic efficiency of the mustard gas mimic, bis(2-chloroethyl) ether, surpassing the performance of the free Dha A solution. At 32°C, the poloxamer molecules within Dha A@TSG formed a tightly packed stereostucture, which substantially improved the storage and…
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Taxonomy
TopicsEnzyme Catalysis and Immobilization · Hemoglobin structure and function · Biomedical Research and Pathophysiology
