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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.)

Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis

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Author(s):
de Araujo, Evandro Ares [1] ; Manzine, Livia Regina [1] ; Piiadov, Vassili [1] ; Seiki Kadowaki, Marco Antonio [1] ; Polikarpov, Igor [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Av Trabalhador Sao Carlense 400, BR-13560970 Sao Carlos, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 111, p. 302-310, MAY 2018.
Web of Science Citations: 1
Abstract

Economic sustainability of modern biochemical technologies for plant cell wall transformations in renewable fuels, green chemicals, and sustainable materials is considerably impacted by the elevated cost of enzymes. Therefore, there is a significant drive toward discovery and characterization of novel carbohydrate-active enzymes. Here, the BICel48 cellulase from Bacillus licheniformis, a glycoside hydrolase family 48 member (GH48), was functionally and biochemically characterized. The enzyme is catalytically stable in a broad range of temperatures and pH conditions with its enzymatic activity at pH 5.0 and 60 degrees C. BlCel48 exhibits high hydrolytic activity against phosphoric acid swollen cellulose (PASC) and bacterial cellulose (BC) and significantly lower activity against carboxymethylcellulose (CMC). BlCel48 releases predominantly cellobiose, and also small amounts of cellotriose and cellotetraose as products from PASC hydrolysis. Small-angle X-ray scattering (SAXS) data analysis revealed a globular molecular shape and monomeric state of the enzyme in solution. Its molecular mass estimated based on SAXS data is similar to 77.2 kDa. BlCel48 has an (alpha alpha)(6)-helix barrel-fold, characteristic of GH48 members. Comparative analyses of homologous sequences and structures reveal the existence of two distinct loops in BlCel48 that were not present in other structurally characterized GH48 enzymes which could have importance for the enzyme activity and specificity. (C) 2017 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants
FAPESP's process: 10/52362-5 - Targeted analysis of microbial lignocellulolytic secretomes: a new approach to enzyme discovery
Grantee:Igor Polikarpov
Support type: Regular Research Grants
FAPESP's process: 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis
Grantee:Marco Antonio Seiki Kadowaki
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 14/00769-5 - Structural studies of glycoside hydrolyses in solution using small-angle scattering (SAS) techniques
Grantee:Vasilii Piiadov
Support type: Scholarships in Brazil - Doctorate (Direct)