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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-452 |
| Subject |
Molecular characterization of a novel family V esterase form Lactobacillus acidophilus NCFM |
| Authors |
Ly Thi Huong Luu Le, Doo Hun Kim*
Department of Chemistry, Sookmyung Women's University, Korea
|
| Abstract |
A novel esterase, LaEst, was identified from Lactobacillus acidophilus NCFM. The enzyme consisted of 247 amino acids and the molecular mass of LaEst was estimated to be 27,369 Da. LaEst displayed a significant sequence similarity with LJ0536, a serine cinnamoyl esterase produced by the probiotic bacterium Lactobacillus johnsonii N6.2. Futher sequence analysis of LaEst revealed a conserved pentapeptide of G-X-S-X-G and a putative catalytic triad of Ser106-Asp197-His225. LaEst preferred p-nitrophenyl butyrate as a substrate and showed its maximum activity at pH 8.0. In addition, LaEst efficiently hydrolyzed α-D-glucose pentaacetate and glyceryl tributyrate. Taken together, this work might provide some useful information in sequence, biophysical properties and catalytic activity of family V esterase. |
| E-mail |
ly.12000532@gmail.com |
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122nd General Meeting of the KCS