High expression of recombinant Streptomyces sp. S38 xylanase in Pichia pastoris by codon optimization and analysis of its biochemical properties |
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Authors: | Xiao-Yan Fu Wei Zhao Ai-Sheng Xiong Yong-Sheng Tian Ri-He Peng |
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Affiliation: | (1) Agro-Biotechnology Research Institute, Shanghai Academy of Agricultural Sciences, 2901 Beidi Rd, Shanghai, 201106, China; |
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Abstract: | In recent years, the biotechnological use of xylanases has grown remarkably. To efficiently produce xylanase for food processing and other industry, a codon-optimized recombinant xylanase gene from Streptomyces sp. S38 was synthesized and extracellularly expressed in Pichia pastoris under the control of AOX1 promoter. SDS-PAGE and activity assay demonstrated that the molecular mass of the recombinant xylanase was estimated to be 25 kDa, the optimum pH and optimum temperature were 5.5 and 50°C, respectively. In shake flask culture, the specific activity of the xylanase activity was 5098.28 U/mg. The K m and V max values of recombinant xylanase were 11.0 mg/ml and 10000 μmol min−1 mg−1, respectively. In the presence of metal ions such as Ca2+, Cu2+, Cr3+ and K+, the activity of the enzyme increased. However, strong inhibition of the enzyme activity was observed in the presence of Hg2+. This is the first report on the expression properties of a recombinant xylanase gene from the Streptomyces sp. S38 using Pichia pastoris. The attractive biochemical properties of the recombinant xylanase suggest that it may be a useful candidate for variety of commercial applications. |
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