UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

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 journalJournal articleResearchpeer-review

Harvard

Ye, Y, Engholm-Keller, K, Fang, Y, Nielsen, CF, Jorda, A, Lund, MN & Chatterton, DEW 2022, 'UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides', Food & Function, vol. 13, no. 1, pp. 344-355. https://doi.org/10.1039/d1fo02619d

APA

Ye, Y., Engholm-Keller, K., Fang, Y., Nielsen, C. F., Jorda, A., Lund, M. N., & Chatterton, D. E. W. (2022). UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides. Food & Function, 13(1), 344-355. https://doi.org/10.1039/d1fo02619d

Vancouver

Ye Y, Engholm-Keller K, Fang Y, Nielsen CF, Jorda A, Lund MN et al. UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides. Food & Function. 2022;13(1):344-355. https://doi.org/10.1039/d1fo02619d

Author

Ye, Yuhui ; Engholm-Keller, Kasper ; Fang, Yajing ; Nielsen, Christian Fiil ; Jorda, Ariadna ; Lund, Marianne N. ; Chatterton, Dereck E. W. / UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides. In: Food & Function. 2022 ; Vol. 13, No. 1. pp. 344-355.

Bibtex

@article{63c562156f15412eb5070967797c8cae,
title = "UHT treatment and storage of liquid infant formula affects protein digestion and release of bioactive peptides",
abstract = "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.",
keywords = "IN-VITRO, MILK-PROTEINS, PLASMINOGEN ACTIVATORS, COMPUTATIONAL PLATFORM, BETA-LACTOGLOBULIN, DIGESTIBILITY, TEMPERATURE, PARAMETERS, STABILITY, MECHANISM",
author = "Yuhui Ye and Kasper Engholm-Keller and Yajing Fang and Nielsen, {Christian Fiil} and Ariadna Jorda and Lund, {Marianne N.} and Chatterton, {Dereck E. W.}",
year = "2022",
doi = "10.1039/d1fo02619d",
language = "English",
volume = "13",
pages = "344--355",
journal = "Food & Function",
issn = "2042-6496",
publisher = "Royal Society of Chemistry",
number = "1",

}

RIS

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