Abstract
1. 1. Normal carboxylic acids of different hydrophobicities and similar chain lengths were prepared and used for the modification of amino groups of thermolysin (EC 3.4.24.4). They were 4,7,10,13-tetraoxatetradecanoic acid, 4,7,10-trioxatetradecanoic acid, 4,7-dioxatetradecanoic acid and 4-oxatetradecanoic acid. 2. 2. The modified enzymes were isolated by gel filtration. They had 6–7 acyl groups per molecule. Acylation of amino groups with 4-oxatetradecanoic acid and tetradecanoic acid made the enzyme insoluble. 3. 3. The most hydrophilic enzyme derivative had similar enzyme activity and higher heat resistance than the native enzyme. The most hydrophobic derivative showed lower K m (50%) and V (40%) values for proteinase activity and lower heat resistance than the former derivative. The trioxa-derivative had intermediate characteristics. The results are discussed with respect to effects on stability and activity of the enzyme.
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.
