Cloning and Sequencing Analysis of Alginate Lyase Genes from the Marine Bacterium Vibrio sp. O2 |
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Authors: | Hitoshi Kawamoto Akio Horibe Yasunari Miki Takayuki Kimura Katsunori Tanaka Tsuyoshi Nakagawa Makoto Kawamukai Hideyuki Matsuda |
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Institution: | (1) Marine Products Kimuraya Co., Ltd., 3307 Watari, Sakaiminato, Tottori 684-0072, Japan;(2) Department of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Japan;(3) Center for Integrated Research in Science, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Japan |
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Abstract: | We isolated a new marine bacteria, which displayed alginate-depolymerizing activity in plate assays, from seawater in Mihonoseki
Harbor, Japan. Analysis of the 16S ribosomal RNA gene sequence of one of the isolates proved that this alginate-depolymerizing
bacterium belonged to the genus Vibrio and it was named Vibrio sp. O2. The alginate lyase genes of Vibrio sp. O2 were cloned and expressed in Escherichia
coli. Two alginate lyase-producing clones, pVOA-A4 and pVOA-B5, were obtained. The alginate lyase gene alyVOA from pVOA-A4 was composed of an 858-bp open reading frame (ORF) encoding 285 amino acid residues, while alyVOB from pVOA-B5 was composed of an 828-bp ORF encoding 275 amino acid residues. The degree of identity between the deduced amino
acid sequences of AlyVOA or AlyVOB and Photobacterium sp. ATCC43367 alginate poly(ManA)lyase AlxM was 92.3% or 32.6%, respectively. Alginate lyase consensus regions corresponding
to the sequences YFKAGXYXQ and RXELR were observed in all three of these sequences. AlyVOA and AlyVOB both degraded polymannuronate
in plate assays and were therefore confirmed to be poly(β-D-mannuronate)lyases. |
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Keywords: | Alginate lyase poly(β D-mannuronate)lyase" target="_blank">-D-mannuronate)lyase Vibrio sp O2 |
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