F149. Rheological studies of chromatins from repressed nuclei of terminally differentiated cells

Abstract

The sequence of proteolytic cleavages characterizing the action of chymosin on the αauthor-casein-(24-199)-fragment (αauthor-I) and on β-casein in vitro under conditions as present in Gouda cheese, and the possible intervention by the lactococcal cell-envelope proteinase (CEP) in the subsequent chain of reactions in cheese, have been established. Primary cleavage sites with approximately the same susceptibility to chymosin are Leu 149 - Phe 150, Leu 156 - Asp 157 and Trp 164 - Tyr 165 in αauthor-I and Leu 192 - Tyr193 in β-casein. Two of the three main primary products of αauthor-I degradation, viz. fragments f24–149 and f150–164, are rapidly converted by chymosin to several, mostly small fragments. These fragments, together with the primary product f165–199, are considered to be substrates for starter peptidase action in cheese. As long as cell lysis is not significant in cheese, CEP seems to be mainly responsible for further degradation of these peptides. The phosphoserine-containing αauthor-casein fragment f24–74 and the bitter-tasting β-casein fragment f193–209 appear to be most resistant to both chymosin and CEP action.