@article{article_647525, title={PARTIAL PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPEPTIDASE PRODUCED BY Bacillus amyloliquefaciens FE-K1}, journal={Trakya University Journal of Natural Sciences}, volume={21}, pages={47–61}, year={2020}, DOI={10.23902/trkjnat.647525}, author={Erem, Fundagül and İnan, Mehmet and Karakaş Budak, Barçın and Certel, Muharrem}, keywords={Bacillus amyloliquefaciens,metallopeptidase,ropy bread,purification}, abstract={<p class="MsoNormal" style="margin-bottom:.0001pt;text-align:justify;line-height:150%;">The aim of this study was to purify and characterize the peptidase of Bacillus amyloliquefaciens (Fukumoto) (strain FE-K1) isolated from ropey bread. Peptidases were purified from crude enzyme solution by affinity chromatography with an efficiency of 25 % and a purification coefficient of 1.53. The optimum pH of partially purified peptidase (PPPase) solution was determined as 7.5 and the peptidases retained approximately 90 % of their initial activity in the pH range 7.0-8.5 following incubation at 37°C for 2 h. The optimum temperature for the PPPase was 60°C. The approximate molecular weight of the PPPase was determined as 36 kDa. Inactivation of the PPPase in the presence of O-FEN and EDTA showed them to be metallopeptidases and 5 mM of K+1 and 5 mM of Mn+2 ions increased the enzyme activity by 4 % and 6.15 %, respectively. The presence of Hg+2, Fe+3 and SDS (0.1-1.0 % w/v) caused inactivation whereas the enzyme retained most of its activity in the presence of 0.1-1.0 % (v/v) Triton X-100, Tween 20 and Tween 80 and 1-20 % (v/v) xylene, ethanol, acetone and acetonitrile. Characterization of the PPPase revealed the enzyme as a neutral serine metallopeptidase compatible with some organic solvents and surfactants. <br /> </p> <p> </p>}, number={1}, publisher={Trakya University}, organization={Scientific Research Projects Coordination Unit of Akdeniz University}