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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
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]
Total Authors: 9
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: NEW BIOTECHNOLOGY; v. 32, n. 1, p. 13-20, JAN 25 2015.
Web of Science Citations: 22
Abstract

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)

FAPESP's process: 11/13242-7 - Studies of enzymatic mechanisms for the improvement of bio-fuel production
Grantee:Leandro Cristante de Oliveira
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 08/58037-9 - Library generation for biomass-conversion enzymes from soil metagenome
Grantee:Fábio Márcio Squina
Support type: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants
FAPESP's process: 12/21054-9 - Biophysical studies and of the synergistic action of thermophilics enzymes involved in the hydrolysis of mannans
Grantee:Wanius José Garcia da Silva
Support type: Regular Research Grants
FAPESP's process: 10/18198-3 - Systems biology of sugarcane bagasse microbial decomposition interactions
Grantee:Fábio Márcio Squina
Support type: Research Grants - Visiting Researcher Grant - International