Abstract
The gene encoding thermostable T1 lipase secreted by Geobacillus sp. strain T1 has been overexpressed in a prokaryotic system. Preliminary crystallization was conducted with crystal screen and crystal screen II through a sitting drop vapor diffusion method with 0.5 mg/mL purified T1 lipase at 16 °C. Crystallization at 16 °C using formulation 21 of crystal screen II at 2.5 mg/mL yielded bigger and more defined crystals. Good crystals could easily be obtained as the temperature was increased further while retaining other conditions. In fact, crystallization of T1 lipase is still possible at 60 °C. The ability to form crystals at 60 °C is a new discovery in lipase crystallization.
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.
