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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Comparative analysis of three hyperthermophilic GH1 and GH3 family members with industrial potential

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Autor(es):
Cota, Junio [1] ; Correa, Thamy L. R. [1] ; Damasio, Andre R. L. [1] ; Diogo, Jose A. [1] ; Hoffmam, Zaira B. [1] ; Garcia, Wanius [2] ; Oliveira, Leandro C. [1, 3] ; Prade, Rolf A. [4] ; Squina, Fabio M. [1]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Campinas, SP - Brazil
[2] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre, SP - Brazil
[3] UNESP Univ Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas IBILCE, Dept Fis, Sao Jose Do Rio Preto, SP - Brazil
[4] Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 - USA
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: NEW BIOTECHNOLOGY; v. 32, n. 1, p. 13-20, JAN 25 2015.
Citações Web of Science: 24
Resumo

Beta-glucosidases (BGLs) are enzymes of great potential for several industrial processes, since they catalyze the cleavage of glucosidic bonds in cellobiose and other short cellooligosaccharides. However, features such as good stability to temperature, pH, ions and chemicals are required characteristics for industrial applications. This work aimed to provide a comparative biochemical analysis of three thermostable BGLs from Pyrococcus furiosus and Thermotoga petrophila. The genes PrBgl1 (Gill from P. furiosus), TpBgl1 (GH1 from T. petrophila) and TpBgl3 (GH3 from T. petrophila) were cloned and proteins were expressed in Escherichia coli. The purified enzymes are hyperthermophilic, showing highest activity at temperatures above 80 C at acidic (TpBgl3 and PfBgl1) and neutral (TpBgl1) pHs. The BGLs showed greatest stability to temperature mainly at pH 6.0. Activities using a set of different substrates suggested that TpBg13 (GH3) is more specific than GH1 family members. In addition, the influence of six monosaccharides on BGL catalysis was assayed. While PfBgl1 and TpBgl3 seemed to be weakly inhibited by monosaccharides, TpBgl1 was activated, with xylose showing the strongest activation. Under the conditions tested, TpBgl1 showed the highest inhibition constant (K-i = 1100.00 mM) when compared with several BGLs previously characterized. The BGLs studied have potential for industrial use, specifically the enzymes belonging to the GH1 family, due to its broad substrate specificity and weak inhibition by glucose and other saccharides. (AU)

Processo FAPESP: 11/13242-7 - Estudos de modelos de mecanismos enzimáticos para o aprimoramento da produção de biocombustíveis
Beneficiário:Leandro Cristante de Oliveira
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 12/21054-9 - Estudos biofísicos e da ação sinérgica de enzimas termofílicas envolvidas na hidrólise de mananas
Beneficiário:Wanius José Garcia da Silva
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 08/58037-9 - Geração de biblioteca para conversão enzimática de biomassa a partir de metagenoma do solo
Beneficiário:Fábio Márcio Squina
Linha de fomento: Auxílio à Pesquisa - Programa BIOEN - Apoio a Jovens Pesquisadores
Processo FAPESP: 10/18198-3 - Biologia de sistemas das interações microbianas na decomposição do bagaço de cana
Beneficiário:Fábio Márcio Squina
Linha de fomento: Auxílio à Pesquisa - Pesquisador Visitante - Internacional