Expression and biochemical characterization of recombinant α-l-rhamnosidase r-Rha1 from Aspergillus niger JMU-TS528

International Journal of Biological Macromolecules
Lijun LiFeng Chen

Abstract

A putative cDNA of α-l-rhamnosidase was PCR-cloned from Aspergillus niger JMU-TS528 and further extracellular over-expressed in Pichia pastoris GS115. The activity of the recombinant α-l-rhamnosidase r-Rha1 was 711.9U/mL, eightfold higher than the native α-l-rhamnosidase from A. niger JMU-TS528. r-Rha1 is a N-glycosylated protein of 90kDa and possesses broad substrate specificities by hydrolyzing α-1,2, α-1,3 α-1,4, and α-1,6 linkages to β-d-glucosides. This is the first report presenting that α-l-rhamnosidase showed activity on four kinds of glucosidic linkages. Compared with other previously characterized α-l-rhamnosidases, r-Rha1 showed a good thermostability and wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C. r-Rha1 activity was not greatly affected by representative metal ions and other detected effectors and showed excellent tolerance abilities against glucose and ethanol. These beneficial characteristics of r-Rha1 suggest that r-Rha1 should be considered a potential new biocatalyst for food and drug industrial applications.

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Citations

Jul 25, 2018·International Journal of Molecular Sciences·Kristýna SlámováKateřina Valentová
Nov 6, 2018·Acta Crystallographica. Section D, Structural Biology·Petr PachlPavlína Řezáčová
Jun 5, 2019·Applied Biochemistry and Biotechnology·Deqing WangPengcheng Chen
Nov 15, 2019·Archives of Biochemistry and Biophysics·Brendan TerryMatthew H Sazinsky

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