Biotechnology Letters, Vol.26, No.18, 1421-1424, 2004
Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis
An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60degreesC (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.