Purification and characterization of a lysozyme from a marine microorganism.
- Author:
Yan-Li ZOU
1
;
Mi SUN
;
Yue-Jun WANG
Author Information
1. Laboratory of Marine Enzyme and Enzyme Engineering, Yellow Sea Fisheries Research Institute, Qingdao 266071, China.
- Publication Type:Journal Article
- MeSH:
Bacterial Proteins;
isolation & purification;
metabolism;
Enzyme Stability;
Micrococcus;
enzymology;
Muramidase;
isolation & purification;
metabolism;
Seawater;
microbiology
- From:
Chinese Journal of Biotechnology
2005;21(3):420-424
- CountryChina
- Language:Chinese
-
Abstract:
A novel lysozyme was purified from a marine microorganism and its major characteristics were studied. Cell-free supernatant was prepared by centrifugation of culture broth, ultrafiltration using a hollow fiber (molecular weight cut off, 50kD) and concentration using a hollow fiber (molecular weight cut off, 10kD). The crude lysozyme was purified 34.7 fold to electrophoretic homogeneity with a recovery of 24.1% by CM-Sepharose FF cationic-exchange and Sephadex G-100 gel chromatography. The relative molecular weight of this lysozyme was determined as about 39 kD. The optimum pH and temperature towards Micrococcus lysodleikticus were pH 8.0 and 35 degrees C respectively, and the enzyme was stable at temperature below 50 degrees C and pH 5.0 - 10.0. The lysozyme activity was slightly enhanced by Zn2+ and Cu2+ and slightly inhibited by Mn2+ and Ag+. The lysozyme showed good compatibility to many common chemical agents such as EDTA (0.1%) and KH2 PO4 (1.0%). The lysozyme had broad-spectrum against many bacteria, including a number of pathogens, which were resistant to egg-white lysozyme.
