earticle

영어

A novel oligoalginate lyase from Stenotrophomonas maltophilia KJ-2 was identified and characterized. The KJ-2 oligoalginate lyase consisted of AlgL- and heparinase II/III-like domains. The KJ-2 oligoalginate lyase, AlgL- and heparinase II/III-like domains were cloned using PCR with the specific primers designed from homologous nucleotide sequences. The recombinant KJ-2 oligoalginate lyase showed substrate preference toward polymannuronate and oligoalginate. During the course of alginate degradation by KJ-2 oligoalginate lyase, alginate oligomers such as dimers, trimers and tetramers were generated together with monosaccharides. The KJ-2 oligoalginate lyase can be used for alginate saccharification.