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Updated: Apr 30, 2026
High Throughput Screening of Fungal Endoglucanase Activity in Escherichia coli
Published on: August 13, 2011
Cloning, expression, sequence analysis, and partial characterization of two alkaline β-1, 4-endoglucanases of
Xi-Hua Zhao1, Dong-Zhi Wei, Wei Wang
1State key Lab of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200237, China.
Abstract:
Here we cloned and expressed two alkaline β-1, 4-endoglucanases of Phaeosphaeria sp. LH21 from deep-sea mud. The two enzymes shared 71 and 63 % of identities with their known β-1, 4-endoglucanases, respectively. According to the primary and spatial structures, the potential active sites of one of the two enzymes could be Asp122 and Asp11, while the other enzyme could be Asp16. The enzymatic properties of their recombinant enzymes from Pichia pastoris GS115 showed that they were optimally active at pH 8 and 60-65 °C, exhibited >90 % residual relative activities at pH 3-10, and obtained relative activities >75 % at pH 5-10.
