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  • Title: Engineering the thermostability of a xylanase from Aspergillus oryzae by an enhancement of the interactions between the N-terminus extension and the β-sheet A2 of the enzyme.
    Author: Chen Z, Zhang H, Wang J, Tang C, Wu J, Wu M.
    Journal: Biotechnol Lett; 2013 Dec; 35(12):2073-9. PubMed ID: 23907668.
    Abstract:
    A mesophilic Aspergillus oryzae xylanase (AoXyn11A) belongs to glycoside hydrolase family 11. Hydrogen bonds and a disulfide bridge were introduced between the N-terminus extension and the β-sheet A2 of AoXyn11A, which were located in the corresponding region of a hyperthermostable xylanase. The mutants were designated as AoXyn11A(C5) and AoXyn11A(C5-C32), respectively. The thermostabilities of AoXyn11A and the mutants were assessed by the molecular dynamics simulations. After being incubated at 55 °C for 30 min, AoXyn11A(C5-C32) retained 49 % of its original activity, AoXyn11A(C5) retained 12 % and AoXyn11A retained 3 %. The interactions between the N-terminus extension and the β-sheet A2 were analyzed in depth: there was enhancement of the interactions between the N-terminus extension and the β-sheet A2 of AoXyn11A that improved its thermostability.
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