Abstract
Aspergillus niger has been used for homologous and heterologous expressions of many protein products. In this study, the α-L-rhamnosidase from A. niger (Rha-N1, GenBank XP_001389086.1) was homologously expressed in A. niger 3.350 by Agrobacterium tumefaciens-mediated transformation. The enzyme activity of Rha-N1 was 0.658 U/mL, which was obtained by cultivation of engineered A. niger in a 5-L bioreactor. Rha-N1 was purified by affinity chromatography and characterized. The optimum temperature and optimum pH for Rha-N1 were 60°C and 4.5, respectively. Enzyme activity was promoted by Al3+, Li+, Mg2+, and Ba2+ and was inhibited by Mn2+, Fe3+, Ca2+, Cu2+, and organic solvents. The result indicated that rutin was the most suitable substrate for Rha-N1 bycomparison with the other two flavonoid substrates hesperidin and naringin. Thetransformed products of isoquercitrin, hesperetin-7-O-glucoside, and prunin were identified by LC-MS and 1H-NMR.
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