AI Article Synopsis
- The novel esterase gene lipP1, found in the extremely halophilic archaeon Haloarcula japonica, encodes the enzyme HjEstP1, classified as a family IV esterase with specific conserved motifs.
- HjEstP1 was expressed in its original strain, purified, and characterized, revealing optimal activity at a pH of 6.0 and temperatures above 60 °C.
- The enzyme demonstrated increased activity with higher NaCl concentrations, peaking at over 4.5 M, and preferentially hydrolyzed pNP and glycerol esters with short-chain fatty acids, marking it as the first esterase identified from an extremely halophilic archaeon through homologous expression.
Article Abstract
The novel esterase gene lipP1, which encodes HjEstP1, was discovered in the genome of the extremely halophilic archaeon Haloarcula japonica. A homology search and sequence alignment revealed that HjEstP1 is a member of family IV esterases with conserved GXSXG and HGGG motifs. lipP1 was expressed in its parental strain, and recombinant HjEstP1 was purified and characterized. Optimal pH and temperature of HjEstP1 were 6.0 and > 60 °C, respectively. HjEstP1 showed higher activity with increasing NaCl concentration, and optimal NaCl concentration was > 4.5 M. Furthermore, HjEstP1 preferentially hydrolyzed pNP and glycerol esters with short chain fatty acids. To our knowledge, this is the first report of an esterase from an extremely halophilic archaeon obtained via homologous expression.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11614938 | PMC |
| http://dx.doi.org/10.1007/s00792-024-01370-2 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!