ABSTRACT
Endo-cellulases are important to efficiently hydrolyze cellulose, and widely used in biotechnology. In this study, we overexpressed and characterized an endo-cellulase from Aspergillus nidulans. This endo-cellulase was successfully overexpressed in flasks and fermentor, and its concentration in fermentor reached 0.89 mg/mL. The optimal pH and temperature of the were 4.0 and 80 ℃ respectively, and it was very stable between pH 2.0 and 12.0. It was thermally stable below 60 ℃, whereas it was inactivated very quickly above 70 ℃. Its CMCase activity could be enhanced by Co²⁺, Mn²⁺ and Fe²⁺, whereas it was inhibited by Pb²⁺, Ni²⁺ and Cu²⁺. Therefore, this endo-cellulase exhibited good pH stability and thermostability below 60 ℃, and has the potential as commercial enzymes.
ABSTRACT
Eight cell strains of mouse hybridoma named PC 01 to PC 08 have been produced by immu-'nizing the mice with human plasma protein C (HPC) which is purified using physico-chemical method. Each of them has long-term stable ability to secret the monoclonal antibodies. Among them,PC 03 is a conformation-specific monoclonal antibody,and its binding to HPC can be pro-motad distinctly by divalent metal ion. However,the monoclonal antibodies of PC02 and PC03 can noticeably advance the enzymatic activity of HPC,whereas the monoclonal antibody of PC04 has capacity to inhibit the enzymatic activity of HPC.