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Biospecific chromatography of chymosin on quinonated Sepharose and its application to enzyme content determination in rennets

Published online by Cambridge University Press:  01 June 2009

Francesco Di Gregorio
Affiliation:
ASSORENI, Laboratories for Biochemical Processes, 00015 Monterotondo, Rome, Italy
Raffaello Sisto
Affiliation:
ASSORENI, Laboratories for Biochemical Processes, 00015 Monterotondo, Rome, Italy
Franco Morisi
Affiliation:
ASSORENI, Laboratories for Biochemical Processes, 00015 Monterotondo, Rome, Italy

Summary

An 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.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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Biospecific chromatography of chymosin on quinonated Sepharose and its application to enzyme content determination in rennets
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