earticle

영어

An alginate lyase from Pseudomonas sp. KS408 was cloned and characterized. Recombinant E. coli harvested with alginate gene was expressed by IPTG induction and purified by using Ni-Sepharose affinity chromatography. Alginate oligomers obtained by degrading alginate with KS408 alginate lyase were analized by using FPLC and H-NMR. Peak profile from NMR showed that KS408 alginate lyase was polyM-specific lyase (β1-4 lyase, EC4.2.2.3). KS408 alginate lyase could cleavage between D-b-mannuronate and D-b-mannuronate linkage (MM) not D-b-mannuronate and L-α-guluronate linkage (MG). The molecular weight of oligoalginate products also analyzed with Electron-spray-ionization/Mass spectroscopy (ESI-MS). When polyM block was treated with KS408, four part of dimer and 1 part of trimer could be obtained. Acknowledgement : This work was supported by New &Renewable Energy R&D program(20093020090020) under the Korea Ministry of Knowledge Economy(MKE) and Korea Industrial Technology Foundation (KOTEF) through the Human Resource Training Project for Strategic Technology.