Abstract
SummaryAn insoluble benzoquinone derivative, obtained by reacting benzoquinone with Sepharose 4B and subsequent deactivation with ethanolamine, selectively absorbed chymosin from a mixture of milk-clotting enzymes and other proteins such as in rennets. This selective absorption has been used for developing a purification method and for quantitatively estimating the chymosin content of commercial rennets. Thus, from a powdered calf rennet, it was possible to obtain in one step an 8-fold purified chymosin free of bovine pepsins. The proposed analytical test involves 2 milk-clotting activity measurements and a chromatographic elution of the sample on a quinonated Sepharose column. It can be applied directly to commercial rennets, because it does not require pre-dialysis of the sample against the elution buffer. Furthermore, a combination of quinonated Sepharose and DEAE-cellulose chromatography gave a method for isolation of bovine pepsin I from rennets.
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.
