Dallas David C, German J Bruce
Nestle Nutr Inst Workshop Ser. 2017;88:129-136. doi: 10.1159/000455250. Epub 2017 Mar 27.
Milk proteins are a complex and diverse source of biological activities. Beyond their function, intact milk proteins also act as carriers of encrypted functional sequences that, when released as peptides, exert biological functions, including antimicrobial and immunomodulatory activity, which could contribute to the infant's competitive success. Research has now revealed that the release of these functional peptides begins within the mammary gland itself. A complex array of proteases produced in mother's milk has been shown to be active in the milk, releasing these peptides. Moreover, our recent research demonstrates that these milk proteases continue to digest milk proteins within the infant's stomach, possibly even to a larger extent than the infant's own proteases. As the neonate has relatively low digestive capacity, the activity of milk proteases in the infant may provide important assistance to digesting milk proteins. The coordinated release of these encrypted sequences is accomplished by selective proteolytic action provided by an array of native milk proteases and infant-produced enzymes. The task for scientists is now to discover the selective advantages of this protein-protease-based peptide release system.
乳蛋白是生物活性的复杂多样来源。除了其功能外,完整的乳蛋白还充当加密功能序列的载体,这些序列在作为肽释放时发挥生物功能,包括抗菌和免疫调节活性,这可能有助于婴儿的生存竞争优势。现在的研究表明,这些功能性肽的释放始于乳腺本身。母乳中产生的一系列复杂蛋白酶已被证明在乳汁中具有活性,从而释放这些肽。此外,我们最近的研究表明,这些乳蛋白酶在婴儿胃内会持续消化乳蛋白,甚至可能比婴儿自身的蛋白酶消化程度更大。由于新生儿消化能力相对较低,婴儿体内乳蛋白酶的活性可能为消化乳蛋白提供重要帮助。这些加密序列的协同释放是通过一系列天然乳蛋白酶和婴儿产生的酶提供的选择性蛋白水解作用来实现的。科学家们现在的任务是发现这种基于蛋白质-蛋白酶的肽释放系统的选择性优势。