Abstract
Circular dichroism (CD) spectral analysis of a purified protease of Pseudomonas fluorescens T16 was carried out at different temperatures to determine the relationship between its secondary structure and its heat-stability. The protease protein was found to be 33% β-structure and 67% random coil. The protein lacked α-helical structure. Unfolding of the enzyme molecule was increased from 25°C, with maximum unfolding at 45°C. The enzyme exhibited maximum inactivation (low temperature inactivation [LTI] phenomenon) at temperatures between 45 and 55°C. At higher temperatures (60–95°C) the protease appears to undergo an additional conformational change to a more ordered stable structure. Metal ions such as Ca 2+ appeared to be involved in structural stabilization and are required for protection against heat inactivation. The comparisons of amino acid composition, sequence homology, hydrophobicity index and polarities of heat-stable proteases were made to predict their heat-stabilities.
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.
