Abstract

This work proposes an innovative method of fouling mitigation by protein and genetic engineering. It makes use of the strong affinity of proteins in binding and removing the key dissolved metal ion (in the fluid) that triggers scale formation on heat exchanger surfaces. It shows that by raising temperature to its melting temperature, a metal-binding protein with chelated metal ions can change its native (folded) conformational state to its denatured, random-coiled polypeptide (unfolded) state, and that by raising the temperature above the melting temperature, the protein will release the chelated ions. It is further proved that by repeating the heating and cooling cycle, the protein can chelate and release the scale-inducing metal ions, thus establishing the feasibility of developing a new class of effective biodegradable antifoulants that are thermally regenerative and friendly to the environment. Also reported are the measured melting temperatures of metal-chelated proteins by a nano differential scanning calorimeter (Nano-DSC).

Full Text
Paper version not known

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 call

Disclaimer: 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.