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제122회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structure and characterization of a novel family VII carbohydrate esterase from Paenibacillus sp. R4.

2018년 8월 30일 13시 38분 47초
LIFE.P-455 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 19일 (금요일) 11:00~12:30
Life Chemistry
저자 및
Wanki Yoo, Doo Hun Kim1,*
College of Medicine, Sungkyunkwan University, Korea
1Department of Chemistry, Sookmyung Women's University, Korea
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