Draft genome sequence data of Gordonia hongkongensis strain EUFUS-Z928 isolated from the octocoral Eunicea fusca.

Octocorals are among the most prolific sources of biologically active compounds. A significant part of their specialized metabolites richness is linked to the abundance of their associated microbiota. Consequently, research on the bioprospecting potential of microorganisms associated with these marine invertebrates has gained much interest. Here, we describe the draft genome of Gordonia hongkongensis strain EUFUS-Z928 isolated from the octocoral Eunicea fusca. The genome was assembled de novo from short-read whole-genome sequencing data. Additionally, functional annotation of predicted genes was performed using the RAST tool kit, including genome mining for specialized metabolite biosynthetic gene clusters using the antiSMASH v6.0 tool. The genome sequence data of G. hongkongensis EUFUS-Z928 can provide information for further analysis of the potential biotechnological use of this microorganism and guide the characterization of other related actinobacterial isolates. Likewise, this information increases the analytical capacity for studying the genus Gordonia.

Enzyme Bioprospection of Marine-Derived Actinobacteria from the Chilean Coast and New Insight in the Mechanism of Keratin Degradation in Streptomyces sp. G11C.

Marine actinobacteria are viewed as a promising source of enzymes with potential technological applications. They contribute to the turnover of complex biopolymers, such as pectin, lignocellulose, chitin, and keratin, being able to secrete a wide variety of extracellular enzymes. Among these, keratinases are a valuable alternative for recycling keratin-rich waste, which is generated in large quantities by the poultry industry. In this work, we explored the biocatalytic potential of 75 marine-derived actinobacterial strains, focusing mainly on the search for keratinases. A major part of the strains secreted industrially important enzymes, such as proteases, lipases, cellulases, amylases, and keratinases. Among these, we identified two streptomycete strains that presented great potential for recycling keratin wastes-Streptomyces sp. CHA1 and Streptomyces sp. G11C. Substrate concentration, incubation temperature, and, to a lesser extent, inoculum size were found to be important parameters that influenced the production of keratinolytic enzymes in both strains. In addition, proteomic analysis of culture broths from Streptomyces sp. G11C on turkey feathers showed a high abundance and diversity of peptidases, belonging mainly to the serine and metallo-superfamilies. Two proteases from families S08 and M06 were highly expressed. These results contributed to elucidate the mechanism of keratin degradation mediated by streptomycetes.