UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides
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UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides. / Ye, Yuhui; Engholm-Keller, Kasper; Fang, Yajing; Nielsen, Christian Fiil; Jorda, Ariadna; Lund, Marianne N.; Chatterton, Dereck E. W.
In: Food & Function, Vol. 13, No. 1, 2022, p. 344-355.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides
AU - Ye, Yuhui
AU - Engholm-Keller, Kasper
AU - Fang, Yajing
AU - Nielsen, Christian Fiil
AU - Jorda, Ariadna
AU - Lund, Marianne N.
AU - Chatterton, Dereck E. W.
PY - 2022
Y1 - 2022
N2 - Ready-to-feed liquid infant formulas (IF) were subjected to direct (D) or indirect (ID) ultra-high-temperature (UHT) treatment and then stored at 40 degrees C under aseptic conditions for 60-120 days simulating global transportation which accelerates the Maillard reaction. Low pasteurized and unstored IF (LP) was included as a control for the UHT treatments. Simulated infant in vitro digestion was conducted. SDS-PAGE indicated that protein aggregate formation correlated with thermal treatment, being greatest after 60 days of storage. Limited protein digestion was observed after pepsin treatment for 2 h. Beta-lactoglobulin (beta-Lg), alpha-lactalbumin (alpha-La) and protein aggregates remained undigested after 2 h of pepsin digestion in LP and D, but less beta-Lg and alpha-La remained in ID. The digestion of beta-Lg and alpha-La was enhanced in D and ID stored for 60 days, but aggregates remained undigested. After pepsin and pancreatin digestion, large amounts of beta-Lg remained undigested in the LP, but digestion increased after UHT treatment (ID > D) and increased further after storage for 60 and 120 days, indicating that heat treatment and storage facilitate the digestion of unaggregated proteins. No aggregates remained after pancreatin digestion of LP, D, ID and D stored for 60 days, but were present in ID stored for 60 days. Aggregates were mainly disulphide-linked, but dityrosine linkages were detected in D and ID stored for 120 days. LC-MS/MS indicated limited proteolysis arising from endogenous milk proteases prior to in vitro digestion, being highest in D. Peptide numbers increased following pepsin and further during pancreatin digestion (beta-casein > beta-Lg > beta-La), and released beta-Lg peptides, typically 5-8 amino acids in length, contained several bioactivities, e.g., dipeptidyl-peptidase IV (DPP-IV) and angiotensin converting enzyme (ACE) inhibition.
AB - Ready-to-feed liquid infant formulas (IF) were subjected to direct (D) or indirect (ID) ultra-high-temperature (UHT) treatment and then stored at 40 degrees C under aseptic conditions for 60-120 days simulating global transportation which accelerates the Maillard reaction. Low pasteurized and unstored IF (LP) was included as a control for the UHT treatments. Simulated infant in vitro digestion was conducted. SDS-PAGE indicated that protein aggregate formation correlated with thermal treatment, being greatest after 60 days of storage. Limited protein digestion was observed after pepsin treatment for 2 h. Beta-lactoglobulin (beta-Lg), alpha-lactalbumin (alpha-La) and protein aggregates remained undigested after 2 h of pepsin digestion in LP and D, but less beta-Lg and alpha-La remained in ID. The digestion of beta-Lg and alpha-La was enhanced in D and ID stored for 60 days, but aggregates remained undigested. After pepsin and pancreatin digestion, large amounts of beta-Lg remained undigested in the LP, but digestion increased after UHT treatment (ID > D) and increased further after storage for 60 and 120 days, indicating that heat treatment and storage facilitate the digestion of unaggregated proteins. No aggregates remained after pancreatin digestion of LP, D, ID and D stored for 60 days, but were present in ID stored for 60 days. Aggregates were mainly disulphide-linked, but dityrosine linkages were detected in D and ID stored for 120 days. LC-MS/MS indicated limited proteolysis arising from endogenous milk proteases prior to in vitro digestion, being highest in D. Peptide numbers increased following pepsin and further during pancreatin digestion (beta-casein > beta-Lg > beta-La), and released beta-Lg peptides, typically 5-8 amino acids in length, contained several bioactivities, e.g., dipeptidyl-peptidase IV (DPP-IV) and angiotensin converting enzyme (ACE) inhibition.
KW - IN-VITRO
KW - MILK-PROTEINS
KW - PLASMINOGEN ACTIVATORS
KW - COMPUTATIONAL PLATFORM
KW - BETA-LACTOGLOBULIN
KW - DIGESTIBILITY
KW - TEMPERATURE
KW - PARAMETERS
KW - STABILITY
KW - MECHANISM
U2 - 10.1039/d1fo02619d
DO - 10.1039/d1fo02619d
M3 - Journal article
C2 - 34904610
VL - 13
SP - 344
EP - 355
JO - Food & Function
JF - Food & Function
SN - 2042-6496
IS - 1
ER -
ID: 288118496