Publicação: Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis
Carregando...
Arquivos
Data
Orientador
Coorientador
Pós-graduação
Curso de graduação
Título da Revista
ISSN da Revista
Título de Volume
Editor
Springer
Tipo
Artigo
Direito de acesso
Acesso aberto
Resumo
Objectives To biochemically characterize an expansin-like X protein domain from Xanthomonas campestris (XcEXLX1) and to study its synergy with cellulases in cellulose depolymerization. Results The protein was purified using a combination of ion exchange and size exclusion chromatography rendering about 30 mg pure protein/l culture medium. Circular dichroism spectroscopy and small-angle X-ray scattering studies of XcEXLX1 reveal that it is a strongly disordered beta-sheet protein. Its low resolution envelope fits nicely the crystallographic structure of the homologous protein EXLX1 from Bacillus subtillis. Furthermore, we demonstrate that XcEXLX1 shows a synergistic, pH-dependent effect when combined with a commercial enzymatic preparation (Accellerase 1500), enhancing its hydrolytic activity on a cellulosic substrate. The strongest effect was observed in acid pHs with an increase in sugar release of up to 36 %. Conclusion The synergistic effect arising from the action of the expansin-like protein was considerable in the presence of significantly larger amounts of the commercial enzymatic cocktail then previously observed (0.35 FPU of Accellerase 1500/g substrate).
Descrição
Palavras-chave
Accellerase, Biofuel, Cellulase, Cellulose depolymerization, Expansin synergism, Xanthomonas campestris
Idioma
Inglês
Como citar
Biotechnology Letters. Dordrecht: Springer, v. 37, n. 12, p. 2419-2426, 2015.
