Can I read Proteolysis of Milk Proteins Lactosylated in Model Systems on EtoBox?

Proteolysis of Milk Proteins Lactosylated in Model Systems by Trine Kastrup Dalsgaard; Jacob Holm Nielsen; Lotte Bach Larsen is a scholarly article available to read on EtoBox.

What is Proteolysis of Milk Proteins Lactosylated in Model Systems about?

## Abstract Five different milk proteins (α‐casein, β‐casein, κ‐casein, β‐lactoglobulin, and lactoferrin) and a peptide substrate were applied as substrates for the investigation of how lactosylation affected proteolysis by different proteases. After a lactosylation period of 4 days in aqueous solution, at 65°C and pH 6.8 in a protein: lactose ratio of 1000 the proteins were enzymatically hydrolyzed by the three milk relevant proteases plasmin, cathepsin D, and chymosin. Lactosylation of all substrates affected hydrolysis by plasmin negatively, with the largest effect on the globular proteins. This could be explained by modification of lysine residues, being the preferred cleavage site for plasmin, but also the residue generally preferred for lactosylation. Lactosylation of the caseins and of β‐lactoglobulin did not affect subsequent cleavage by cathepsin D and chymosin significantly, but for β‐lactoglobulin, both the secondary as well as the tertiary structure were affected by lactosylation. In contrast, decreased hydrolysis by cathepsin D and chymosin was observed for lactoferrin after lactosylation. Decreased hydrolysis may be caused by a more compact tertiary structure induced

Author

Trine Kastrup Dalsgaard; Jacob Holm Nielsen; Lotte Bach Larsen

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley (ISSN 1613-4125)

Published

2007

Language

EN