期刊
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 95, 期 6, 页码 1643-1653出版社
SPRINGER
DOI: 10.1007/s00253-012-4266-y
关键词
Alginate; Alginate lyase; PolyMG-specific alginate lyase; Saccharification; Stenotrophomas maltophilia KJ-2
资金
- (Development of Marine-Bioenergy) program
- Ministry of Land, Transport and Maritime Affairs of the Korean Government
- Ministry of Knowledge Economy (MKE)
- Korea Institute for Advancement in Technology (KIAT)
- National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology [2012R1A1A2008647]
- National Research Foundation of Korea [2012R1A1A2008647] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
A gene for a polyMG-specific alginate lyase possessing a novel structure was identified and cloned from Stenotrophomas maltophilia KJ-2 by using PCR with homologous nucleotide sequences-based primers. The recombinant alginate lyase consisting of 475 amino acids was purified on Ni-Sepharose column and exhibited the highest activity at pH 8 and 40 A degrees C. Interestingly, the recombinant alginate lyase was expected to have a similar catalytic active site of chondroitin B lyase but did not show chondroitin lyase activity. In the test of substrate specificity, the recombinant alginate lyase preferentially degraded the glycosidic bond of polyMG-block than polyM-block and polyG-block. The chemical structures of the degraded alginate oligosaccharides were elucidated to have mannuronate (M) at the reducing end on the basis of NMR analysis, supporting that KJ-2 polyMG-specific alginate lyase preferably degraded the glycosidic bond in M-G linkage than that in G-M linkage. The KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate.
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