A Gram-staining-negative, aerobic, yellow-orange-pigmented, rod-shaped bacterium designated D-24 T was isolated from seawater from sandy shoreline in Johor, Malaysia. The genus Vitellibacter is a member of the family Flavobacteriaceae in the phylum Bacteroidetes. The genus was first proposed by Nedashkovskaya et al. . Members of this genus are typically Gram-staining-negative, rodshaped, aerobic bacteria that have been isolated from marine environments, except for strain V. soesokkakensis RSSK-12 T which was isolated from the junction between the ocean and a freshwater spring. Menaquinone-6 (MK-6) was found to be the only respiratory quinone in all species of the genus Vitellibacter (Kim et al., 2010). Generally, the members of this genus possess iso-C 15 : 0 and iso-C 17 : 0 3-OH as major fatty acids and have a DNA G+C content in the range of 38.9-48.7 mol% . The current study aimed to determine the taxonomic position of strain D-24 T , based on phenotypic, genotypic and chemotaxonomic analyses.

A halophilic bacterium, sp. strain CD6, was isolated from salted fish and its extracellular protease was characterized. Protease production was found to be highest when yeast extract was used as nitrogen source for growth. The protease exhibited stability at wide range of salt concentration (0-12.5%, w/v), temperatures (20-60 °C), and pH (4-10) with maximum activity at 10.0% (w/v) NaCl, 60 °C, pH 7 and 10, indicating its polyextremophilicity. The protease activity was enhanced in the presence of Mg, Mn, Cd, and Al (107-122% relative activity), and with retention of activity > 80% for all of other metal ions examined (K, Ca, Cu, Co, Ni, Zn, and Fe). Both PMSF and EDTA inhibited protease activity, denoting serine protease and metalloprotease properties, respectively. High stability (> 70%) was demonstrated in the presence of organic solvents and detergent constituents, and the extracellular protease from strain CD6 was also found to be compatible in commercial detergents. Proteinaceous stain removal efficacy revealed that crude protease of strain CD6 could significantly enhance the performance of commercial detergent. The protease from sp. strain CD6 could serve as a promising alternative for various applications, especially in detergent industry.

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The genus Meridianimaribacter is one of the least-studied genera within Cytophaga-Flavobacteria. To date, no genomic analysis of Meridianimaribacter has been reported. In this study, Meridianimar ibacter sp. strain CL38, a lignocellulose degrading halophile was isolated from mangrove soil. The genome of strain CL38 was sequenced and analyzed. The assembled genome contains 17 contigs with 3.33 Mbp, a GC content of 33.13% and a total of 2982 genes predicted. Lignocellulose degrading enzymes such as cellulases (GH3, 5, 9, 16, 74 and 144), xylanases (GH43 and CE4) and mannanases (GH5, 26, 27 and 130) are encoded in the genome. Furthermore, strain CL38 demonstrated its ability to decompose empty fruit bunch, a lignocellulosic waste residue arising from palm oil industry. The genome information coupled with experimental studies confirmed the ability of strain CL38 to degrade lignocellulosic biomass. Therefore, Meridianimar ibacter sp. strain CL38, with its halotolerance, could be useful for seawater based lignocellulosic biorefining.

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