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Abstract
A 1.2 kb DNA fragment coding for the pro-peptide and mature keratinase from Bacillus licheniformis PWD-1 (kerA) was cloned into vectors pPICZαA and pGAPZαA for extracellular expression in the methylotrophic yeast, Pichia pastoris. Recombinant keratinase was secreted by the pPICZαA-kerA transformants 24 h after methanol induction of shake-flask cultures, and reached a final yield of 124 mg l−1 (285 U ml−1) 144 h after the induction. The recombinant keratinase was glycosylated (∼ 39 kDa), and was optimal between pH 8.5–9.5 and between 55 °C –60 °C using azokeratin as substrate. The enzyme degraded bovine serum albumin, collagen, and soy protein concentrate. In conclusion, P. pastoris can be used as an efficient host to express keratinase for nutritional and environmental applications.
Published Version
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