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Functional expression of phospholipase A1 from Serratia sp. MK1 using Escherichia coli system
임혜진,박유진,장연재,( Devi Casi ),( Christy Catherine ),이경호,( Tong Yi ),이종두,박지현,이소정,오준영,송재광,김동명 한국공업화학회 2016 한국공업화학회 연구논문 초록집 Vol.2016 No.0
Phospholipase A1 (EC 3.1.1.32) is an enzyme that hydrolyzes phospholipid into a fatty acid and a lysophosphoslipid and has potential industrial applications in such fields as bioenergy, food, and pharmaceutical industry. Phospholipase has lipolytic activity, however, causes inhibition of cell growth and phospholipase hinders its production in the conventional cell-based expression methods. Because it does not require membrane integrity for protein synthesis, cell-free protein synthesis system using cell lysates can offer an alternative route. In this study, we attempted to express the phospholipase A1 gene cloned from the chromosomal DNA of Serratia sp. MK1 either in E.coli cells or a cell-free synthesis system derived from the lysate of the E.coli cells. From the same amount of cellular protein, cell-free protein synthesis produced over a 1000-fold higher titer of functional phospholipase A1 than standard recombinant techniques using whole E.coli cells.