Journal
MARINE BIOTECHNOLOGY
Volume 14, Issue 2, Pages 189-202Publisher
SPRINGER
DOI: 10.1007/s10126-011-9402-7
Keywords
Oligoalginate lyase; Sphingomonas sp MJ-3; Alginate; Heparinase-like protein; Alginate monosaccharides
Funding
- (Development of Marine-Bioenergy) program
- Ministry of Land, Transport and Maritime Affairs of Korean Government
- Ministry of Knowledge Economy (MKE)
- Korea Institute for Advancement in Technology (KIAT)
- National Research Foundation of Korea [핵C6A1301] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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A bacterium possessing alginate-degrading activity was isolated from marine brown seaweed soup liquefied by salted and fermented anchovy. The isolated strain was designated as Sphingomonas sp. MJ-3 based on the analyses of 16S ribosomal DNA sequences, 16S-23S internal transcribed spacer region sequences, biochemical characteristics, and cellular fatty acid composition. A novel alginate lyase gene was cloned from genomic DNA library and then expressed in Escherichia coli. When the deduced amino acid sequence was compared with the sequences on the databases, interestingly, the cloned gene product was predicted to consist of AlgL (alginate lyase L)-like and heparinase-like protein domain. The MJ-3 alginate lyase gene shared below 27.0% sequence identity with exolytic alginate lyase of Sphingomonas sp. A1. The optimal pH and temperature for the recombinant MJ-3 alginate lyase were 6.5 and 50 degrees C, respectively. The final degradation products of alginate oligosaccharides were analyzed by electrospray ionization mass spectrometry and proved to be alginate monosaccharides. Based on the results, the recombinant alginate lyase from Sphingomonas sp. MJ-3 is regarded as an oligoalginate lyase that can degrade oligoalginate and alginate into alginate monosaccharides.
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