Other Publication Details
Mandatory Fields
Other
Huppertz, T,Uniacke, T,Kelly, AL,Fox, PF
2006
June
Inhibition of the proteolytic activity of indigenous plasmin or exogenous chymosin and pepsin in bovine milk by blood serum
Validated
1
()
Optional Fields
blood serum milk plasmin chymosin inhibition ALPHA-2 MACROGLOBULIN PROTEINASE-INHIBITORS PROTEASE INHIBITORS MECHANISM PEPSTATIN SERPIN ALPHA2-MACROGLOBULIN PURIFICATION SUPERFAMILY EVOLUTION
Adding bovine or ovine blood serum (0.5-2.0%, v/v) to bovine milk did not affect the hydrolysis of caseins by plasmin, but equine, and particularly porcine, serum strongly inhibited casein hydrolysis.- in milk containing 1.0-2.0% porcine serum, caseins were not hydrolysed by plasmin on incubation at 37 degrees C for 7 d. Porcine, and particularly equine, serum also impaired the coagulation of milk by chymosin or pepsin; equine serum (2.0%) increased the chymosin-induced coagulation time of milk similar to 4-fold and a firm chymosin-induced milk gel did not form. Adding heated (70 degrees C for 5 min) serum from any of the species to milk did not influence plasmin-induced hydrolysis of caseins or chymosin- or pepsin-induced coagulation of milk, suggesting that the inhibitor(s) is heat labile. Plasmin- or chymosin-induced hydrolysis of small synthetic Substrates was not influenced by blood serum. It is suggested that alpha(2)-macroglobulin may be the inhibitory substance, although further study is required to verify this. (c) 2006 Elsevier Ltd. All rights reserved.
691
696
DOI 10.1016/j.idairyj.2005.10.022
Grant Details