Whole cell evaluation and the enzymatic kinetic study of urease from ureolytic bacteria affected by potentially toxic elements

Weila Li, Ayelet Fishman, Varenyam Achal*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Microbially induced carbonate precipitation (MICP) is a biomineralization process that has various applications in environmental pollution remediation and restoration of a range of building materials. In this study, a ureolytic bacterium, Lysinibacillus sp. GY3, isolated from an E-waste site, was found as a promising catalyst for remediation of heavy metals via the MICP process. This bacterial isolate produced significant amounts of urease and showed a great persistence in immobilization of potentially toxic elements. A reference ureolytic strain, Bacillus megaterium VS1, was selected in order to compare the efficiency of Lysinibacillus sp. GY3. Study on urease localization indicated 80% more urease activity secreted extracellularly as for Lysinibacillus sp. GY3 compared to B. megaterium VS1. From the investigation on effects of metals on both intra- and extra-cellular urease, it was clear that Lysinibacillus sp. GY3 produced the most stable urease under conditions of metal pressure, especially retaining more than 70% activity in the presence of 1 g/L Pb2+ and Zn2+. These results suggest that this isolated microorganism could be promisingly introduced in the MICP process to stabilize complex heavy metal pollutions, with reference to the regulating ability under harsh conditions to stabilize urease activity. This species is so important both for its biological features and environmental impacts. In addition, the present study will bring new insight in the field of metal remediation coupled with enzyme engineered biotechnology.
Original languageEnglish
JournalMicrobiological Research
DOIs
StateE-pub ahead of print - 21 Sep 2022

Keywords

  • Ureolytic bacteria
  • Urease
  • Toxic elements
  • Whole cell biocatalysis
  • Protein structure

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