PMID- 33316714
OWN - NLM
STAT- MEDLINE
DCOM- 20210311
LR  - 20210311
IS  - 1873-7072 (Electronic)
IS  - 0308-8146 (Linking)
VI  - 345
DP  - 2021 May 30
TI  - Mechanisms of plastein formation influence the IgE-binding activity of egg white 
      protein hydrolysates after simulated static digestion.
PG  - 128783
LID - S0308-8146(20)32645-5 [pii]
LID - 10.1016/j.foodchem.2020.128783 [doi]
AB  - Egg is the second most common food allergen among infants and young children. 
      This work investigated the influence of plastein reaction on immunoglobulin E 
      (IgE)-binding activities of egg white protein hydrolysates after simulated 
      gastrointestinal (GIT) digestion. Compared to hydrolysate precursors, the 
      IgE-binding activity of Pepsin-Plastein significantly decreased from 35 +/- 7% to 
      8 +/- 2% (P < 0.05), and Papain-Plastein from 70 +/- 5% to 59 +/- 4%. Further GIT 
      hydrolysis of Pepsin-Plastein maintained the reduced IgE-binding activity 
      (7 +/- 3%) whereas Papain-Plastein digestion restored the IgE-binding reactivity to 
      66 +/- 7%. This discrepancy is related to the different mechanisms of plastein 
      formation. Covalent modifications (decreased free amino nitrogen and sulfhydryl 
      contents) provided biostability for Pepsin-Plastein, whereas hydrophobic 
      interactions (increased surface hydrophobicity) mainly contributed to 
      Papain-Plastein formation. The latter can be destroyed during GIT digestion 
      leading to re-exposure of hidden IgE-binding epitopes. Taken together, plastein 
      reaction is a promising strategy for inducing structural modifications that 
      reduce the immune reactivity of allergenic proteins.
CI  - Copyright (c) 2020 Elsevier Ltd. All rights reserved.
FAU - Sun, Xiaohong
AU  - Sun X
AD  - School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, 
      Ottawa, Ontario K1H 8M5, Canada; College of Food and Biological Engineering, 
      Qiqihar University, Qiqihar, Heilongjiang 161006, China.
FAU - Acquah, Caleb
AU  - Acquah C
AD  - School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, 
      Ottawa, Ontario K1H 8M5, Canada.
FAU - Gazme, Behzad
AU  - Gazme B
AD  - School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, 
      Ottawa, Ontario K1H 8M5, Canada; Department of Food Science, Engineering, and 
      Technology, University of Tehran, 31587-77871 Karaj, Iran.
FAU - Boachie, Ruth T
AU  - Boachie RT
AD  - School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, 
      Ottawa, Ontario K1H 8M5, Canada.
FAU - Nwachukwu, Ifeanyi D
AU  - Nwachukwu ID
AD  - School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, 
      Ottawa, Ontario K1H 8M5, Canada; School of Public Health, Loma Linda University, 
      Loma Linda, CA, United States.
FAU - Udenigwe, Chibuike C
AU  - Udenigwe CC
AD  - School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, 
      Ottawa, Ontario K1H 8M5, Canada; Department of Chemistry and Biomolecular 
      Sciences, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada. Electronic 
      address: cudenigw@uottawa.ca.
LA  - eng
PT  - Journal Article
DEP - 20201203
PL  - England
TA  - Food Chem
JT  - Food chemistry
JID - 7702639
RN  - 0 (Allergens)
RN  - 0 (Egg Proteins)
RN  - 0 (Protein Hydrolysates)
RN  - 0 (plastein)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 3.4.23.1 (Pepsin A)
SB  - IM
MH  - Allergens/metabolism
MH  - Child
MH  - Child, Preschool
MH  - *Digestion
MH  - Egg Proteins/*metabolism
MH  - Food Hypersensitivity
MH  - Humans
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Immunoglobulin E/*metabolism
MH  - Pepsin A/metabolism
MH  - Protein Binding
MH  - Protein Hydrolysates/*metabolism
OTO - NOTNLM
OT  - Covalent modification
OT  - Egg white protein hydrolysate
OT  - Hydrophobic interaction
OT  - IgE-binding activity
OT  - Plastein reaction
OT  - Simulated static digestion
EDAT- 2020/12/15 06:00
MHDA- 2021/03/12 06:00
CRDT- 2020/12/14 20:14
PHST- 2020/08/16 00:00 [received]
PHST- 2020/09/19 00:00 [revised]
PHST- 2020/11/29 00:00 [accepted]
PHST- 2020/12/15 06:00 [pubmed]
PHST- 2021/03/12 06:00 [medline]
PHST- 2020/12/14 20:14 [entrez]
AID - S0308-8146(20)32645-5 [pii]
AID - 10.1016/j.foodchem.2020.128783 [doi]
PST - ppublish
SO  - Food Chem. 2021 May 30;345:128783. doi: 10.1016/j.foodchem.2020.128783. Epub 2020 
      Dec 3.