Abstract
The secondary structure of commercially purified soybean lipoxygenase (EC 1.13.11.12) was investigated in selected monophasic organic solvents, including chloroform, methanol, acetonitrile, hexane, and octane. The Fourier transform infrared (FT-IR) spectra of the enzyme obtained in chloroform, methanol, and acetonitrile showed an absorption band at 1617 cm(-1) indicative of significant protein aggregation, whereas spectra of lipoxygenase in hexane and octane exhibited substantially less aggregate formation. Variable-temperature infrared studies of lipoxygenase in D(2)O show that the predominately alpha-helical structure of the protein undergoes an irreversible transition to intermolecular beta-sheet at and above 65 degrees C. Chemical imaging technology employing an FT-IR spectrometer equipped with an infrared microscope and a focal-plane array detector was used to examine the changes in the secondary structure of lipoxygenase at the water-hexane interface in the presence and absence of substrate. The secondary structure of lipoxygenase at the hexane-water interface was comparable to that of the structure of lipoxygenase in D(2)O after exposure of lipoxygenase solution to hexane.
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.
