期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 62, 期 29, 页码 7225-7232出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf405601e
关键词
hydrolysate; human milk digestion; milk; nutrition; proteolytic enzymes; bioactive peptide
资金
- Irish Research Council for Science, Engineering and Technology - Marie Curie Actions under FP7
- Enterprise Ireland
- SFI [08/IN.1/B1864]
- University of California Discovery Program [05GEB01NHB]
- National Institutes of Health [HD059127, HD061923]
- California Dairy Research Foundation
- U.S. Department of Agriculture, National Institute for Food and Agriculture postdoctoral fellowship
- National Science Foundation Graduate Research Fellowship Program
- National Institutes of Health Training Program in Biomolecular Technology [2-T3-GM08799]
Human milk is known to contain several proteases, but little is known about whether these enzymes are active, which proteins they cleave, and their relative contribution to milk protein digestion in vivo. This study analyzed the mass spectrometry-identified protein fragments found in pooled human milk by comparing their cleavage sites with the enzyme specificity patterns of an array of enzymes. The results indicate that several enzymes are actively taking part in the digestion of human milk proteins within the mammary gland, including plasmin and/or trypsin, elastase, cathepsin D, pepsin, chymotrypsin, a glutamyl endopeptidase-like enzyme, and proline endopeptidase. Two proteins were most affected by enzyme hydrolysis: beta-casein and polymeric immunoglobulin receptor. In contrast, other highly abundant milk proteins such as alpha-lactalbumin and lactoferrin appear to have undergone no proteolytic cleavage. A peptide sequence containing a known antimicrobial peptide is released in breast milk by elastase and cathepsin D.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据