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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.)

A novel cold-adapted and glucose-tolerant GH1 beta-glucosidase from Exiguobacterium antarcticum B7

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Author(s):
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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]
Total Authors: 12
Affiliation:
[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
Total Affiliations: 3
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 82, p. 375-380, JAN 2016.
Web of Science Citations: 14
Abstract

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)

FAPESP's process: 13/13309-0 - Studies of the structural and functional behavior of enzymes evolutionarily specialized in the degradation of plant biomass with potential biotechnological applications
Grantee:Mário Tyago Murakami
Support Opportunities: Regular Research Grants
FAPESP's process: 14/07135-1 - Multi-user equipament approved in grant 2013/13309-0: Beckman Coulter capillary electrophoresis systems with LIF detection system
Grantee:Mário Tyago Murakami
Support Opportunities: Multi-user Equipment Program