2. Academic Validation
  3. A novel cold-adapted and glucose-tolerant GH1 β-glucosidase from Exiguobacterium antarcticum B7

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

  • Int J Biol Macromol. 2016 Jan:82:375-80. doi: 10.1016/j.ijbiomac.2015.09.018.
Elaine Crespim 1,  Letícia M Zanphorlin 1,  Flavio H M de Souza 2,  José A Diogo 1,  Alex C Gazolla 1,  Carla B Machado 1,  Fernanda Figueiredo 1,  Amanda S Sousa 1,  Felipe Nóbrega 3,  Vivian H Pellizari 3,  Mário T Murakami 2,  Roberto Ruller 4
Affiliations

Affiliations

  • 1 Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Caixa Postal 6192, CEP 13083-970, Campinas, São Paulo, Brasil.
  • 2 Laboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Caixa Postal 6192, CEP 13083-970, Campinas, São Paulo, Brasil.
  • 3 Instituto Oceanográfico, Universidade de São Paulo, São Paulo, São Paulo, Brasil.
  • 4 Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Caixa Postal 6192, CEP 13083-970, Campinas, São Paulo, Brasil. Electronic address: roberto.ruller@bioetanol.org.br.
PMID: 26475230 DOI: 10.1016/j.ijbiomac.2015.09.018
Abstract

A novel GH1 β-glucosidase (EaBgl1A) from a bacterium isolated from Antarctica soil samples was recombinantly overexpressed in Escherichia coli 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. EaBgl1A is also a cold-adapted Enzyme, exhibiting activity in the temperature range from 10 to 40°C with optimal activity at 30°C, which allows its application in industrial processes using low temperatures. Kinetic characterization revealed an enzymatic turnover (Kcat) of 6.92s(-1) (cellobiose) and 32.98s(-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 200 mM 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.

Keywords

Cold adaptation; Exiguobacterium antarcticum B7; Glucose tolerance; β-Glucosidase.

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