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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Grand Ballroom |
| Time |
10월 19일 (금요일) 11:00~12:30 |
| Code |
LIFE.P-454 |
| Subject |
Characterization of a novel GDSL family lipase (NmLip) from Neisseria meningitidis 053442 |
| Authors |
Wanki Yoo, Doo Hun Kim1,*
College of Medicine, Sungkyunkwan University, Korea
1Department of Chemistry, Sookmyung Women's University, Korea
|
| Abstract |
Family II lipases, also known as GDSL family lipases, exhibit a broad substrates specificity hydrolyzing carbohydrates, tertiary alcohol esters, and lipids. GDSL family lipases have a typical α/β hydrolase folding and catalytic triads which are generally found in bacterial lipases/esterases. In contrast to esterases, lipases generally have hydrophobic exterior characteristic displaying hydrophobic amino acids on their surface. This property of lipases facilitates the catalysis of lipids at oil-water boundary. Here, NmLip, a novel GDSL family lipase from Neisseria meningitidis 053442 was identified, purified, and characterized by biochemical and biophysical methods. Homology searching found that NmLip shows high sequence similarity to TesA, an E. coli lipase belonging to GDSL family. The results of site-directed mutagenesis and molecular simulation revealed that hydrophobic amino acid, Leu92 near the catalytic pocket play a critical role for NmLip’s hydrolase activity and substrate specificity through hydrophobic interaction and steric hinderance. As last, immobilization by cross-linking and enzyme-inorganic hybrid nanoflower (hNF) were applied to NmLip which have shown a good durability after repeated usages and an improved catalytic efficiency. Collectively, these studies provide a deeper insight to substrate specificity of GDSL family lipase and emphasize potential of NmLip as a biocatalyst in the pharmaceutical and chemical industries. |
| E-mail |
vlqkshqk61@outlook.kr |
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122nd General Meeting of the KCS