Passa al contenuto
Merck

Selective Proteolysis of α-Lactalbumin by Endogenous Enzymes of Human Milk at Acidic pH.

Molecular nutrition & food research (2019-07-05)
Junai Gan, Jingyuan Zheng, Nithya Krishnakumar, Elisha Goonatilleke, Carlito B Lebrilla, Daniela Barile, J Bruce German
ABSTRACT

The use of human milk products is increasing for high-risk infants. Human milk contains endogenous enzymes that comprise a dynamic proteolytic system, yet biological properties of these enzymes and their activities in response to variations including pH within infants are unclear. Human milk has a neutral pH around 7, while infant gastric pH varies from 2 to 6 depending on individual conditions. This study is designed to determine the specificity of enzyme-substrate interactions in human milk as a function of pH. Endogenous proteolysis is characterized by incubating freshly expressed human milk at physiologically relevant pH ranging from 2 to 7 without the addition of exogenous enzymes. Results show that the effects of pH on endogenous proteolysis in human milk are protein-specific. Further, specific interactions between cathepsin D and α-lactalbumin are confirmed. The endogenous enzyme cathepsin D in human milk cleaves α-lactalbumin as the milk pH shifts from 7 to 3. This study documents that selective proteolysis activated by pH shift is a mechanism for dynamic interactions between human milk and the infant. Controlled proteolysis can guide the use of human milk products based on individual circumstance.

MATERIALI
N° Catalogo
Marchio
Descrizione del prodotto

Sigma-Aldrich
α-Lactalbumin from human milk, ≥95% (SDS-PAGE), lyophilized powder
Sigma-Aldrich
Cathepsin D from human liver, lyophilized powder, ≥250 units/mg protein (E1%/280)