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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-455 |
| Subject |
Structure and characterization of a novel family VII carbohydrate esterase from Paenibacillus sp. R4. |
| Authors |
Wanki Yoo, Doo Hun Kim1,*
College of Medicine, Sungkyunkwan University, Korea
1Department of Chemistry, Sookmyung Women's University, Korea
|
| Abstract |
Carbohydrate esterases (CEs) catalyze acetylation and de-acetylation of carbohydrates ranging from simple compounds such as a glucose and mannose to complex polysaccharide like cellulose and xylan. The modifications of carbohydrates are necessary for various application field, such as a polishing of fabric, a preparation of biofuels and highly valuable industrial materials. A cold-active enzyme or a cold-adapted enzyme implies an ambiguous group of enzymes which are usually derived from psychrophilic bacteria. The enzymes present its optimal activity at low temperature indicating the superior structural stability of the enzymes. In this study, PbAcE, a novel cold-active family VII carbohydrate esterase derived from Paenibacillus sp. R4 was identified, purified and crystalized. PbAcE was found to have a broad substrate specificity including tertiary alcohol esters, antibiotics related compounds, lipids as well as carbohydrates. Collectively, the crystal structure and biochemical study of PbAcE will provide molecular basis of enzyme reaction for both a carbohydrate esterase and a cold-active enzyme |
| E-mail |
vlqkshqk61@outlook.kr |
|
122nd General Meeting of the KCS