THE TOPOGRAPHY OF BOVINE BETA-CASEIN AT AN OIL-WATER INTERFACE AS DETERMINED FROM THE KINETICS OF TRYPSIN-CATALYZED HYDROLYSIS

被引:57
作者
LEAVER, J [1 ]
DALGLEISH, DG [1 ]
机构
[1] HANNAH RES INST,AYR KA6 5HL,SCOTLAND
关键词
PROTEIN TOPOGRAPHY; ENZYME KINETICS; CASEIN; PROTEOLYSIS; PROTEIN ADSORPTION;
D O I
10.1016/0167-4838(90)90275-K
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The topography of bovine beta-casein at a soya oil/water interface was studied by following the kinetics of the trypsin-catalysed hydrolysis. Tryptic peptides were identified from their amino acid compositions and the kinetics were compared with those obtained from beta-casein in solution. Whereas soluble beta-casein was initially hydrolysed at a number of trypsin-sensitive bonds, the hydrolysis of the protein at the interface was a more ordered event. The crucial initiating step was the cleavage of the N-terminal peptides 1-25 and 1-28 from the molecule. Hydrolysis at other trypsin-sensitive sites could then occur. This suggests that with the exception of the large hydrophilic moiety in the N-terminal region, most of the beta-casein molecule is inaccessible to the proteinase, and lies fairly flat on the oil/water interface. After removal of the N-terminal peptide, the remaining macropeptide can reorientate and other hydrophilic regions become accessible to the proteinase.
引用
收藏
页码:217 / 222
页数:6
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