Peptidomic Profile of Milk of Holstein Cows at Peak Lactation

被引:46
|
作者
Dallas, David C. [1 ,2 ]
Guerrero, Andres [3 ]
Parker, Evan A. [3 ]
Garay, Luis A. [1 ]
Bhandari, Aashish [1 ]
Lebrilla, Carlito B. [2 ,3 ]
Barile, Daniela [1 ,2 ]
German, J. Bruce [1 ,2 ]
机构
[1] Univ Calif Davis, Dept Food Sci & Technol, Davis, CA 95616 USA
[2] Univ Calif Davis, Foods Hlth Inst, Davis, CA 95616 USA
[3] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
peptidomics; bovine milk; bioactive peptides; protease; PROTEOSE-PEPTONE FRACTION; GLOBULE-MEMBRANE PROTEOME; BOVINE-MILK; BIOACTIVE PEPTIDES; PLASMINOGEN-ACTIVATOR; ENZYMATIC HYDROLYSATE; BETA-CASEIN; PROTEINS; PROTEOLYSIS; MASTITIS;
D O I
10.1021/jf4040964
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Bovine milk is known to contain naturally occurring peptides, but relatively few of their sequences have been determined. Human milk contains hundreds of endogenous peptides, and the ensemble has been documented for antimicrobial actions. Naturally occurring peptides from bovine milk were sequenced and compared with human milk peptides. Bovine milk samples from six cows in second-stage peak lactation at 78-121 days postpartum revealed 159 peptides. Most peptides (73%) were found in all six cows sampled, demonstrating the similarity of the intramammary peptide degradation across these cows. One peptide sequence, ALPIIQKLEPQIA from bovine perilipin 2, was identical to another found in human milk. Most peptides derived from beta-casein, alpha(s1)-casein, and alpha(s2)-casein. No peptides derived from abundant bovine milk proteins such as lactoferrin, beta-lactoglobulin, and secretory immunoglobulin A. The enzymatic cleavage analysis revealed that milk proteins were degraded by plasmin, cathepsins B and D, and elastase in all samples.
引用
收藏
页码:58 / 65
页数:8
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