Otero Igor Vinicius Ramos, Ferro Milene, Bacci Maurício, Ferreira Henrique, Sette Lara Durães
Departamento de Bioquímica e Microbiologia, Instituto de Biociências-IB, Universidade Estadual Paulista Júlio de Mesquita Filho-UNESP, 24A, 1515, Rio Claro, SP, 13506-900, Brazil.
Centro de Estudos de Insetos Sociais, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho, Rio Claro, Brazil.
AMB Express. 2017 Dec 20;7(1):222. doi: 10.1186/s13568-017-0526-7.
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.
漆酶是多铜氧化酶，能够催化涉及多种底物的反应，包括酚类和胺类，这种能力与不同漆酶的存在有关。担子菌通常有多个漆酶基因，但到目前为止，这一特征尚未在海洋来源的真菌中得到证实。Peniophora sp. CBMAI 1063是一种从海洋海绵中分离出的担子菌真菌，它能够在含盐条件下分泌大量漆酶。在本研究中，我们从Peniophora sp. CBMAI 1063的转录组中鉴定出漆酶序列，并利用它们进行了不同的计算机模拟分子分析。结果显示至少存在八个推定基因，这些基因可能编码十种不同的漆酶，其肽长度在482至588个氨基酸之间，分子量在53.5至64.4 kDa之间。这些漆酶似乎具有细胞外活性，只有一种可能代表细胞内漆酶除外。Peniophora sp. CBMAI 1063在漆酶诱导培养基中表达的10种预测漆酶显示出不同的N-糖基化模式和等电点，并根据与酶氧化还原电位调节相关的残基分为两类。预测的漆酶与其他真菌漆酶的相似性均不超过61%。基于Peniophora sp. CBMAI 1063表达的漆酶之间的差异，这种海洋来源的担子菌是一种具有强大生物技术开发潜力的宝贵资源。
