Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/319480
Type: Artigo de periódico
Title: Gh53 Endo-beta-1,4-galactanase From A Newly Isolated Bacillus Licheniformis Cbmai 1609 As An Enzymatic Cocktail Supplement For Biomass Saccharification
Abstract: Galactanases (endo-β-1,4-galactanases—EC 3.2.1.89) catalyze the hydrolysis of β-1,4 galactosidic bonds in arabinogalactan and galactan side chains found in type I rhamnogalacturan. The aim of this work was to understand the catalytic function, biophysical properties, and use of a recombinant GH53 endo-beta-1,4-galactanase for commercial cocktail supplementation. The nucleotide sequence of the endo-β-1,4-galactanase from Bacillus licheniformis CBMAI 1609 (Bl1609Gal) was cloned and expressed in Escherichia coli, and the biochemical and biophysical properties of the enzyme were characterized. The optimum pH range and temperature of Bl1609Gal activity were 6.5–8 and 40 °C, respectively. Furthermore, Bl1609Gal showed remarkable pH stability, retaining more than 75 % activity even after 24 h of incubation at pH 4–10. The enzyme was thermostable, retaining nearly 100 % activity after 1-h incubation at pH 7.0 at 25–45 °C. The enzymatic efficiency (Kcat/Km) against potato galactan under optimum conditions was 241.2 s−1 mg−1 mL. Capillary zone electrophoresis demonstrated that the pattern of galactan hydrolysis by Bl1609Gal was consistent with that of endogalactanases. Supplementation of the commercial cocktail ACCELLERASE®1500 with recombinant Bl1609Gal increased hydrolysis of pretreated sugarcane bagasse by 25 %. © 2016 Springer Science+Business Media New York
Editor: Humana Press Inc.
Rights: fechado
Identifier DOI: 10.1007/s12010-016-2003-1
Address: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84958238419&partnerID=40&md5=f1ad9470203528eea625ec64da9e26ae
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

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