Abstract
Laccases are multicopper oxidases that are able to catalyze reactions involving a range of substrates, including phenols and amines, and this ability is related to the existence of different laccases. Basidiomycetes usually have more than one gene for laccase, but until now, this feature has not been demonstrated in a marine-derived fungus. Peniophora sp. CBMAI 1063 is a basidiomycete fungus isolated from a marine sponge that exhibits the ability to secrete significant amounts of laccase in saline conditions. In the present study, we identified laccase sequences from the transcriptome of Peniophora sp. CBMAI 1063 and used them to perform different molecular in silico analyses. The results revealed the presence of at least eight putative genes, which may encode ten different laccases with peptide lengths ranging from 482 to 588 aa and molecular weights ranging from 53.5 to 64.4 kDa. These laccases seem to perform extracellular activities, with the exception of one that may represent an intracellular laccase. The 10 predicted laccases expressed by Peniophora sp. CBMAI 1063 in laccase-induced media showed different patterns of N-glycosylation and isoelectric points and are divided into two classes based on the residue associated with the regulation of the redox potential of the enzyme. None of the predicted laccases showed more than 61% similarity to other fungal laccases. Based on the differences among the laccases expressed by Peniophora sp. CBMAI 1063, this marine-derived basidiomycete represents a valuable resource with strong potential for biotechnological exploitation.
Highlights
Laccases (EC 1.10.3.2) are oxidoreductases that are widespread in nature and present in plants, insects, bacteria and fungi, though more expressly in the white rot fungal group (Giardina et al 2010; Rivera-Hoyos et al 2013)
The Heterobasidion irregulare and Stereum hirsutum sequences presented the highest similarities to the Peniophora sp
The majority of putative laccases expressed by Peniophora sp
Summary
Laccases (EC 1.10.3.2) are oxidoreductases that are widespread in nature and present in plants, insects, bacteria and fungi, though more expressly in the white rot fungal group (Giardina et al 2010; Rivera-Hoyos et al 2013). These enzymes seem to perform different physiological functions, such as lignin synthesis and degradation, spore pigmentation, cell wall elongation and stress defenses (Riva 2006; Giardina et al 2010). Sequence analyses have demonstrated that fungal laccases differ from other multicopper oxidases by a sequence signature corresponding to four conserved regions, namely, L1, L2, L3, and L4 These regions display the 12 residues that bind the copper ions but
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