摘要
T4 lysozyme was engineered with disulfide bonds and expressed in Pichia pastoris. The secreted proteins were purified and made into powder by lyophiliza-tion. Recombinant protein purity was more than 70% measured by HPLC. The lytic activity of variant T4-lysozyme was measured by the lysis of the cel wal of Xan-thomonas oryzae pv. oryzae, X. oryzae pv. oryzicola, Ralstonia solanacearum comb. nov, Clavibacter michiganensis subsp. michiganensis, X. campestris pv. mal-vacearum, Fusarium oxysporium sp. vasinfectum, Verticil ium dahliae kleb. Inhibition zone assay showed that variant T4 lysozyme significantly inhibited X. o. oryzicola and X. c. malvacearum. The antifungal activities of this protein against F. o. vasin-fectum and V. d. kleb were also analyzed.
T4 lysozyme was engineered with disulfide bonds and expressed in Pichia pastoris. The secreted proteins were purified and made into powder by lyophilization. Recombinant protein purity was more than 70% measured by HPLC. The lytic activity of variant T4-lysozyme was measured by the lysis of the cell wall of Xanthomonas oryzae pv. oryzae, X. oryzae pv. oryzicola, Ralstonia solanacearum comb.nov, Clavibacter michiganensis subsp. michiganensis, X. campestris pv. malvacearum, Fusarium oxysporium sp. vasinfectum, Verticillium dahliae kleb. Inhibition zone assay showed that variant T4 lysozyme significantly inhibited X. o. oryzicola and X. c. malvacearum. The antifungal activities of this protein against F. o. vasinfectum and V. d. kleb were also analyzed.
基金
Supported by the National Biotechnology Program for Crop Breeding(2013ZX08005004,2009ZX08009-089B)
