Abstract
The expression of Thermoactinomyces sp. E79 protease gene cloned into E. coli was highly host-dependent and the levels of protease expression was most stable in E. coli RR1 and E. coli HB101. Heating the intracellular extract at 70°C for 15 min converted the inactive recombinant E79 protease to its active mature form and also resulted in purification of the enzyme in a single step. Addition of 10 mM CaCl2 to the E79 protease decreased its autolysis and increased its thermal stability. © Rapid Science Ltd. 1998
Sign-in/Register to access full text options 
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.
