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Expression of a Bacillus Phytase C Gene in Pichia pastoris and
Properties of the Recombinant Enzyme

The cloning and expression of a native gene encoding a Bacillus subtilis phytase using Pichia pastoris as the host is described. In addition, the inﬂuence of N-glycosylation on the biochemical properties of the B. subtilis phytase, the inﬂuence of pH on the thermostability of the recombinant and native B. subtilis phytases, and the resistance of both phytases to shrimp digestive enzymes and porcine trypsin are also described. After 48 h of methanol induction in shake ﬂasks, a selected recombinant strain produced and secreted 0.82 U/ml (71mg/liter) recombinant phytase. This phytase was N-glycosylated, had a molecular mass of 39 kDa after N-deglycosylation, exhibited activity within a pH range of 2.5 to 9 and at temperatures of 25 to 70°C, had high residual activity (85% 2%) after 10 min of heat treatment at 80°C and pH 5.5 in the presence of 5 mM CaCl2,
and was resistant to shrimp digestive enzymes and porcine trypsin. Although the recombinant Bacillus phytase had pH and temperature activity proﬁles that were similar to those of the corresponding nonglycosylated native phytase, the thermal stabilities of the recombinant and native phytases were different, although both were calcium concentration and pH dependent

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