Biochemical characterization of an endoxylanase from Pseudozyma brasiliensis sp. nov. strain GHG001 isolated from the intestinal tract of Chrysomelidae larvae associated to sugarcane roots

Autor: André Damasio, Gustavo H. Goldman, Thuanny A. Borges, Diego Mauricio Riaño-Pachón, Renato Augusto Corrêa dos Santos, Ednildo A. Machado, Fabio M. Squina, Aline Tieppo de Souza, Juliana Velasco de Castro Oliveira
Rok vydání: 2014
Předmět:
Zdroj: Process Biochemistry. 49:77-83
ISSN: 1359-5113
DOI: 10.1016/j.procbio.2013.10.004
Popis: Endo-xylanases play a key role in the hydrolysis of xylan and recently they have attracted much attention due to their potential applications on the biofuel and paper industries. We isolated a Pseudozyma brasiliensis sp. nov. strain from the intestinal tract of Chrysomelidae larvae that parasitize sugarcane roots. This basidiomycetous yeast produces a xylanase designated PbXynA which was purified and characterized. The molecular weight of PbXynA is 24 kDa, it belongs to the GH11 family and its optimum pH and optimum temperature are 4.0 and 55 °C, respectively. PbXynA has as secondary structure predominantly β-sheets and sigmoidal kinetic behavior with elevated speed conversion from substrate-to-products ( V max = 2792.0 μmol product/min/mg protein). It is highly activated by bivalent cations such as Ca 2+ , however in the presence of Cu 2+ xylanase activity was inhibited. It has a high specific activity and produces xylooligosaccharides that have a variety of industrial applications, indicating PbXynA has a great biotechnological potential.
Databáze: OpenAIRE