Abstract
A novel microbial phospholipase C from Bacillus mycoides strain 970 was purified to apparent homogeneity by an improved purification process, in which DEAE-Cellulose adsorption was first used to remove bulk of dark brown impurities and then a combination of DEAE-Cellulose ion-exchange, Phenyl Sepharose hydrophobic interaction and Sephacryl S-100 gel filtration chromatography was used to separate the enzyme from remained contaminants. The enzyme appeared to be a single peptide of 75.1 kDa on SDS-PAGE. The optimum temperature and pH of the enzyme were 60°C and 7.0 - 7.5, respectively. The enzyme was stable at temperatures lower than 50°C and pH 5 - 9.5. This purified phospholipase C was characterized as a metallophospholipase C and Ca2+, Mg2+, Zn2+ , Ba2+ were essential for its PLC activity. The enzyme showed no lecithinase activity on egg yolk agar and also no hemolytic activity on blood agar. Key words: Phospholipase C, purification, metalloenzyme, nonhemolytic activity,Bacillus mycoides.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
