NDLI: Homologue expression of a β-xylosidase from native Aspergillus niger

Content Provider	Springer Nature Link
Author	Amaro Reyes, A. García Almendárez, B. E. Vázquez Manduja, D. G. Amaya Lla, S. Castaño Tostado, E. Guevara González, R. G. Loera, O. Regalado, C.
Copyright Year	2010
Abstract	Xylan constitutes the second most abundant source of renewable organic carbon on earth and is located in the cell walls of hardwood and softwood plants in the form of hemicellulose. Based on its availability, there is a growing interest in production of xylanolytic enzymes for industrial applications. β-1,4-xylan xylosidase (EC 3.2.1.37) hydrolyses from the nonreducing end of xylooligosaccharides arising from endo-1,4-β-xylanase activity. This work reports the partial characterization of a purified β-xylosidase from the native strain Aspergillus niger GS1 expressed by means of a fungal system. A gene encoding β-xylosidase, xlnD, was successfully cloned from a native A. niger GS1 strain. The recombinant enzyme was expressed in A. niger AB4.1 under control of A. nidulans gpdA promoter and trpC terminator. β-xylosidase was purified by affinity chromatography, with an apparent molecular weight of 90 kDa, and showed a maximum activity of 4,280 U mg protein−1 at 70°C, pH 3.6. Half-life was 74 min at 70°C, activation energy was 58.9 kJ mol−1, and at 50°C optimum stability was shown at pH 4.0–5.0. β-xylosidase kept residual activity >83% in the presence of dithiothreitol (DTT), β-mercaptoethanol, sodium dodecyl sulfate (SDS), ethylenediaminetetraacetate (EDTA), and Zn2+. Production of a hemicellulolytic free xylosidase showed some advantages in applications, such as animal feed, enzymatic synthesis, and the fruit-juice industry where the presence of certain compounds, high temperatures, and acid media is unavoidable in the juice-making process.
Starting Page	1311
Ending Page	1319
Page Count	9
File Format	PDF
ISSN	13675435
Journal	Journal of Industrial Microbiology and Biotechnology
Volume Number	38
Issue Number	9
e-ISSN	14765535
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-11-30
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Aspergillus niger GS1 β-xylosidase activity Thermostability Homologue expression Genetic Engineering Microbiology Biotechnology Inorganic Chemistry Biochemistry Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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