Defluviitalea phaphyphila sp. nov., a Novel Thermophilic Bacterium That Degrades Brown Algae

• Published in: Applied and environmental microbiology Vol. 82; no. 3; pp. 868 - 877
• Main Authors: Ji, Shi-Qi, Wang, Bing, Lu, Ming, Li, Fu-Li
• Format: Journal Article
• Language: English
• Published: United States American Society for Microbiology 01-02-2016
• Subjects: Acetic Acid - metabolism; Algae; Alginates - metabolism; Bacteria; Bacterial Typing Techniques; Base Composition; DNA, Bacterial - genetics; DNA, Ribosomal - genetics; Enzymes; Ethanol - metabolism; Genes; Genome, Bacterial; Genomes; Geologic Sediments - microbiology; Glucans - metabolism; Glucuronic Acid - metabolism; Gram-Positive Bacteria - classification; Gram-Positive Bacteria - genetics; Gram-Positive Bacteria - isolation & purification; Gram-Positive Bacteria - metabolism; Hexuronic Acids - metabolism; Mannitol - metabolism; Multigene Family; Phaeophyceae - metabolism; Phylogeny; Physiology; Pyruvic Acid - metabolism; RNA, Ribosomal, 16S - genetics; Sequence Analysis, DNA
• ISSN: 0099-2240; 1098-5336
• DOI: 10.1128/AEM.03297-15

Brown algae are one of the largest groups of oceanic primary producers for CO2 removal and carbon sinks for coastal regions. However, the mechanism for brown alga assimilation remains largely unknown in thermophilic microorganisms. In this work, a thermophilic alginolytic community was enriched from coastal sediment, from which an obligate anaerobic and thermophilic bacterial strain, designated Alg1, was isolated. Alg1 shared a 16S rRNA gene identity of 94.6% with Defluviitalea saccharophila LIND6LT2(T). Phenotypic, chemotaxonomic, and phylogenetic studies suggested strain Alg1 represented a novel species of the genus Defluviitalea, for which the name Defluviitalea phaphyphila sp. nov. is proposed. Alg1 exhibited an intriguing ability to convert carbohydrates of brown algae, including alginate, laminarin, and mannitol, to ethanol and acetic acid. Three gene clusters participating in this process were predicted to be in the genome, and candidate enzymes were successfully expressed, purified, and characterized. Six alginate lyases were demonstrated to synergistically deconstruct alginate into unsaturated monosaccharide, followed by one uronic acid reductase and two 2-keto-3-deoxy-d-gluconate (KDG) kinases to produce pyruvate. A nonclassical mannitol 1-phosphate dehydrogenase, catalyzing D-mannitol 1-phosphate to fructose 1-phosphate in the presence of NAD(+), and one laminarase also were disclosed. This work revealed that a thermophilic brown alga-decomposing system containing numerous novel thermophilic alginate lyases and a unique mannitol 1-phosphate dehydrogenase was adopted by the natural ethanologenic strain Alg1 during the process of evolution in hostile habitats.