원문정보
초록
영어
Streptomyces sp. strain M3 from marine algae produced poly-guluronate specific lyase. The alginate lyase gene was obtained by using PCR and elucidated to consist of 780bp and 259aa. The region from 1Met to 35Ala was expected to be a signal peptide by using SignalP 3.0 server.
The amino acid sequence of M3 lyase showed 94% , 81%, 28% identity to alginate lyase of Streptomyces sp. ALG-5, Corynebacterium sp. ALY-1 and Sphingomonas sp. A1, respectively. Purified ALG-M3 lyase was activated by 1 mM of CaCl2, MnCl2, CoCl2 and MgCl2, while 1 mM ZnCl2 and HgCl2 inhibited lyase activity completely. ALG-M3 lyase showed temperature stability at 50-60℃, whereas ALG-5 lyase showed temperature stability at 30-40℃. We also carried
out homology modeling and analyzed the energy level of M3 alginate lyase using Prosa 2003 software for improvement of enzyme activity or stability by site directed mutation.
Acknowledgement : This work was financially supported by the 2008 Busan Techno Park program and the Ministry of Knowledge Economy (MKE) and Korea Industrial Technology Foundation (KOTEF) through the Human Resource Training Project for Strategic Technology.