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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 Member of GH16 Family Derived from Sugarcane Soil Metagenome

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Author(s):
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Alvarez, Thabata Maria [1] ; Liberato, Marcelo Vizona [1] ; Franco Cairo, Joo Paulo L. [1] ; Paixo, Douglas A. A. [1] ; Campos, Bruna M. [2] ; Ferreira, Marcel R. [3] ; Almeida, Rodrigo F. [1] ; Pereira, Isabela O. [1] ; Bernardes, Amanda [4] ; Ematsu, Gabriela C. G. [1] ; Chinaglia, Mariana [1] ; Polikarpov, Igor [4] ; Neto, Mario de Oliveira [3] ; Squina, Fabio Marcio [1]
Total Authors: 14
Affiliation:
[1] Ctr Nacl Pesquisa Energia & Mat CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, BR-13083100 Campinas, SP - Brazil
[2] Ctr Nacl Pesquisa Energia & Mat CNPEM, Lab Nacl Biociencias LNBio, BR-13083100 Campinas, SP - Brazil
[3] Univ Estadual Paulista UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP - Brazil
[4] Univ Sao Paulo, Inst Fis Sao Carlos, Sao Carlos, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Applied Biochemistry and Biotechnology; v. 177, n. 2, p. 304-317, SEP 2015.
Web of Science Citations: 2
Abstract

Glycoside hydrolases (GHs) are enzymes found in all living kingdoms that are involved in multiple physiological functions. Due to their multiple enzymatic activities, GHs are broadly applied in bioethanol, food, and paper industry. In order to increase the productivity of these industrial processes, a constant search for novel and efficient enzymes has been proved to be necessary. In this context, metagenomics is a powerful approach to achieve this demand. In the current study, we describe the discovery and characterization of a novel member of GH16 family derived from the sugarcane soil metagenome. The enzyme, named SCLam, has 286 amino acid residues and displays sequence homology and activity properties that resemble known laminarases. SCLam is active against barley beta-glucan, laminarin, and lichenan (72, 33, and 10 U mg(-1), respectively). The optimal reaction conditions were identified as 40 A degrees C and pH 6.5. The low-resolution structure was determined using the small-angle X-ray scattering technique, revealing that SCLam is a monomer in solution with a radius of gyration equal to 19.6 . To the best of our knowledge, SCLam is the first nonspecific (1,3/1,3:1,4)-beta-d-glucan endohydrolase (EC 3.2.1.6) recovered by metagenomic approach to be characterized. (AU)

FAPESP's process: 10/11469-1 - Library generation for biomass-conversion enzymes from soil metagenome
Grantee:Thabata Maria Alvarez
Support type: Scholarships in Brazil - Doctorate (Direct)
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