Abstract
An alkaline thermotolerant bacterial lipase of Bacillus coagulans MTCC-6375 was purified and immobilized on a methacrylic acid and dodecyl methacrylate (MAc-DMA) hydrogel. The lipase was optimally bound to the matrix after 20 min of incubation at 55°C and pH 9 under shaking conditions. The matrix-bound lipase retained approximately 50% of its initial activity at 70–80°C after 3 h of incubation. The immobilized lipase was highly active on medium chain length p-nitrophenyl acyl ester (C: 8, p-nitrophenyl caprylate) than other p-nitrophenyl acyl esters. The presence of Fe3+, NH4+, K+, and Zn2+ ions at 1 mM concentration in the reaction mixture resulted in a profound increase in the activity of immobilized lipase. Most of the detergents partially reduced the activity of the immobilized lipase. The immobilized lipase performed ∼62% conversion in 12 h at temperature 55°C. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 100: 1420–1426, 2006
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.
