Dual functional roles of a novel bifunctional β-lactamase/esterase from Lactococcus garvieae

Int J Biol Macromol. 2022 May 1:206:203-212. doi: 10.1016/j.ijbiomac.2022.02.081. Epub 2022 Feb 17.


A novel bifunctional β-lactamase/esterase (LgLacI), which is capable of hydrolyzing β-lactam-containing antibiotics including ampicillin, oxacillin, and cefotaxime as well as synthesizing biodiesels, was cloned from Lactococcus garvieae. Unlike most bacterial esterases/lipases that have G-x-S-x-G motif, LgLacI, which contains S-x-x-K catalytic motif, has sequence similarities to bacterial family VIII esterase as well as β-lactamases. The catalytic properties of LgLacI were explored using a wide range of biochemical methods including spectroscopy, assays, structural modeling, mutagenesis, and chromatography. We confirmed the bifunctional property of LgLacI hydrolyzing both esters and β-lactam antibiotics. This study provides novel perspectives into a bifunctional enzyme from L. garvieae, which can degrade β-lactam antibiotics with high esterase activity.

Keywords: Antibiotics; Bifunctional enzyme; Biodiesels; LgLacI; β-Lactamase/esterase.

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Cefotaxime
  • Esterases* / chemistry
  • Lactococcus
  • beta-Lactamases* / chemistry


  • Anti-Bacterial Agents
  • Esterases
  • beta-Lactamases
  • Cefotaxime

Supplementary concepts

  • Lactococcus garvieae