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Article

Enhanced thermostability and catalytic activity for arginine deiminase from Enterobacter faecalis SK32.001 via combinatorial mutagenesis.

International journal of biological macromolecules - 1 Jan 2025

Li Mengli, Zhang Yijing, Zhang Tao, Miao Ming

Abstract excerpt

Arginine deiminase (ADI) exhibits potential for clinical and industrial applications, yet its low thermostability and catalytic efficiency under physiological conditions limit its utility. In this work, the ADI of Enterococcus faecalis SK32.001 was rationally designed. A total of 120 combinatorial mutants, ranging from two-point to six-point mutations, were constructed by sequentially stacking single-point...

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Identifiers

PMID: 39586434
DOI: 10.1016/j.ijbiomac.2024.138004

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