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 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.
Tang
Xue-Ming
XM
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
Lakay
F M
FM
Shen
Wei
W
Shao
Wei-Lan
WL
Fang
Hui-Ying
HY
Prior
B A
BA
Wang
Zheng-Xiang
ZX
Zhuge
Jian
J
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
D012697:Serine Endopeptidases; C032923:microbial serine proteinases