| Texto completo | |
| Autor(es): Mostrar menos - |
Crespim, Elaine
[1]
;
Zanphorlin, Leticia M.
[1]
;
de Souza, Flavio H. M.
[2]
;
Diogo, Jose A.
[1]
;
Gazolla, Alex C.
[1]
;
Machado, Carla B.
[1]
;
Figueiredo, Fernanda
[1]
;
Sousa, Amanda S.
[1]
;
Nobrega, Felipe
[3]
;
Pellizari, Vivian H.
[3]
;
Murakami, Mario T.
[2]
;
Ruller, Roberto
[1]
Número total de Autores: 12
|
| Afiliação do(s) autor(es): | [1] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, BR-13083970 Campinas, SP - Brazil
[2] CNPEM, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, SP - Brazil
[3] Univ Sao Paulo, Inst Oceanog, Sao Paulo, SP - Brazil
Número total de Afiliações: 3
|
| Tipo de documento: | Artigo Científico |
| Fonte: | International Journal of Biological Macromolecules; v. 82, p. 375-380, JAN 2016. |
| Citações Web of Science: | 14 |
| Resumo | |
A novel GH1 beta-glucosidase (EaBgl1 A) from a bacterium isolated from Antarctica soil samples was recombinantly overexpressed in Escherichia coil cells and characterized. The enzyme showed unusual pH dependence with maximum activity at neutral pH and retention of high catalytic activity in the pH range 6 to 9, indicating a catalytic machinery compatible with alkaline conditions. EaBgl1 A is also a coldadapted enzyme, exhibiting activity in the temperature range from 10 to 40 degrees C with optimal activity at 30 degrees C, which allows its application in industrial processes using low temperatures. Kinetic characterization revealed an enzymatic turnover (K-cat) of 6.92s(-1) (cellobiose) and 32.98 s(-1) (pNPG) and a high tolerance for product inhibition, which is an extremely desirable feature for biotechnological purposes. Interestingly, the enzyme was stimulated by up to 200mM glucose, whereas the commercial cocktails tested were found fully inhibited at this concentration. These properties indicate EaBgl1A as a promising biocatalyst for biotechnological applications where low temperatures are required. (c) 2015 Elsevier B.V. All rights reserved. (AU) | |
| Processo FAPESP: | 13/13309-0 - Estudos do comportamento funcional e estrutural de enzimas evolutivamente especializadas na degradação de biomassa vegetal com potenciais aplicações biotecnológicas |
| Beneficiário: | Mário Tyago Murakami |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 14/07135-1 - EMU concedido no processo 2013/13309-0 - aquisição do sistema de eletroforese capilar com detector de fluorescência - Beckman Coulter |
| Beneficiário: | Mário Tyago Murakami |
| Modalidade de apoio: | Auxílio à Pesquisa - Programa Equipamentos Multiusuários |