The gene of P-mannanase from T. reesei was successfully cloned and expressed in P. pastoris. The enzyme was used to investigate its enzyme properties. The optimal pH and temperature of the purified recombinant P-mannanase were 6.0 and 80 °C, respectively. The enzyme had a high alkali resistance and a relatively poor acid resistance. It showed higher thermostability at 60 °C than 70 °C. K~+, Zn~(2+), Fe~(3+), Ca~(2+) and Mg~(2+) promoted the activity of the recombinant P-mannanase in different degree, while Fe~(2+), Cu~(2+), Li~(2+) and EDTA have strong inhibitory effects on the activity of the recombinant P-mannanase. The K_m and V_(max) of the recombinant P-mannanase were 0.5 mg/mL and 253.8 IU/mg, respectively.
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