title: Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis.
abstract: 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 60 degrees C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.
authors.affiliation: The Key Laboratory of Industrial Biotechnology, Ministry of Education, Research Center of Industrial Microbiology, Southern Yangtze University, Wuxi 214036, PR China. txm@sun.ac.za
authors.forename: Xue-Ming
authors.initials: XM
authors.lastname: Tang
authors.forename: F M
authors.initials: FM
authors.lastname: Lakay
authors.forename: Wei
authors.initials: W
authors.lastname: Shen
authors.forename: Wei-Lan
authors.initials: WL
authors.lastname: Shao
authors.forename: Hui-Ying
authors.initials: HY
authors.lastname: Fang
authors.forename: B A
authors.initials: BA
authors.lastname: Prior
authors.forename: Zheng-Xiang
authors.initials: ZX
authors.lastname: Wang
authors.forename: Jian
authors.initials: J
authors.lastname: Zhuge
mesh_terms: D001407:Bacillus / Q000145:classification / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007221:Industry; D008970:Molecular Weight; D012697:Serine Endopeptidases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification*; D013045:Species Specificity; D013696:Temperature
chemical_list: D012697:Serine Endopeptidases; C032923:microbial serine proteinases