Interactions of salivary mucins and saliva with food proteins: a review

Hilal Yilmaz Çelebioğlu, Seunghwan Lee, Ioannis S. Chronakis*

*Corresponding author for this work

Research output: Contribution to journalReviewResearchpeer-review

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Abstract

Mucins are long glycoprotein molecules responsible for the gel nature of the mucous layer that covers epithelial surfaces throughout the body. Mucins, as the major salivary proteins, are also important proteins for the food oral processing and digestion. The interactions of salivary mucins and saliva with several food proteins and food protein emulsions, as well as their functional properties related to the food oral processing were reviewed in this paper. The target food proteins of focus were whey proteins (lactoferrin and beta-lactoglobulin) and non-whey proteins (casein, gelatin, galectin/lectin, and proline-rich proteins). Most of the studies suggest that electrostatic attraction (between positively charged food proteins with negatively charged moieties of mucin mainly on glycosylated region of mucin) is the major mode of interaction between them. On the other hand, casein attracts the salivary proteins only via non-covalent interactions due to its naturally self-assembled micellar structure. Moreover, recent studies related to β-lactoglobulin (BLG)-mucin interactions have clarified the importance of hydrophobic as well as hydrophilic interactions, such as hydrogen bonding. Furthermore, in vitro studies between protein emulsions and saliva observed a strong aggregating effect of saliva on caseinate and whey proteins as well as on surfactant-stabilized emulsions. Besides, the sign and the density of the charge on the surface of the protein emulsion droplets contribute significantly to the behavior of the emulsion when mixed with saliva. Other studies also suggested that the interactions between saliva and whey proteins depends on the pH in addition to the flow rate of the saliva. Overall, the role of interactions of food proteins and food protein emulsions with mucin/saliva-proteins in the oral perception, as well as the physicochemical and structural changes of proteins were discussed.
Original languageEnglish
JournalCritical Reviews in Food Science and Nutrition
Volume60
Issue number1
Pages (from-to)64-83
Number of pages20
ISSN1040-8398
DOIs
Publication statusPublished - 2020

Keywords

  • Casein
  • Emulsion
  • Gelatin
  • Lactoferrin
  • Lectins
  • Whey
  • β-lactoglobulin

Cite this

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title = "Interactions of salivary mucins and saliva with food proteins: a review",
abstract = "Mucins are long glycoprotein molecules responsible for the gel nature of the mucous layer that covers epithelial surfaces throughout the body. Mucins, as the major salivary proteins, are also important proteins for the food oral processing and digestion. The interactions of salivary mucins and saliva with several food proteins and food protein emulsions, as well as their functional properties related to the food oral processing were reviewed in this paper. The target food proteins of focus were whey proteins (lactoferrin and beta-lactoglobulin) and non-whey proteins (casein, gelatin, galectin/lectin, and proline-rich proteins). Most of the studies suggest that electrostatic attraction (between positively charged food proteins with negatively charged moieties of mucin mainly on glycosylated region of mucin) is the major mode of interaction between them. On the other hand, casein attracts the salivary proteins only via non-covalent interactions due to its naturally self-assembled micellar structure. Moreover, recent studies related to β-lactoglobulin (BLG)-mucin interactions have clarified the importance of hydrophobic as well as hydrophilic interactions, such as hydrogen bonding. Furthermore, in vitro studies between protein emulsions and saliva observed a strong aggregating effect of saliva on caseinate and whey proteins as well as on surfactant-stabilized emulsions. Besides, the sign and the density of the charge on the surface of the protein emulsion droplets contribute significantly to the behavior of the emulsion when mixed with saliva. Other studies also suggested that the interactions between saliva and whey proteins depends on the pH in addition to the flow rate of the saliva. Overall, the role of interactions of food proteins and food protein emulsions with mucin/saliva-proteins in the oral perception, as well as the physicochemical and structural changes of proteins were discussed.",
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year = "2020",
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pages = "64--83",
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Interactions of salivary mucins and saliva with food proteins: a review. / Çelebioğlu, Hilal Yilmaz; Lee, Seunghwan; Chronakis, Ioannis S.

In: Critical Reviews in Food Science and Nutrition, Vol. 60, No. 1, 2020, p. 64-83.

Research output: Contribution to journalReviewResearchpeer-review

TY - JOUR

T1 - Interactions of salivary mucins and saliva with food proteins: a review

AU - Çelebioğlu, Hilal Yilmaz

AU - Lee, Seunghwan

AU - Chronakis, Ioannis S.

PY - 2020

Y1 - 2020

N2 - Mucins are long glycoprotein molecules responsible for the gel nature of the mucous layer that covers epithelial surfaces throughout the body. Mucins, as the major salivary proteins, are also important proteins for the food oral processing and digestion. The interactions of salivary mucins and saliva with several food proteins and food protein emulsions, as well as their functional properties related to the food oral processing were reviewed in this paper. The target food proteins of focus were whey proteins (lactoferrin and beta-lactoglobulin) and non-whey proteins (casein, gelatin, galectin/lectin, and proline-rich proteins). Most of the studies suggest that electrostatic attraction (between positively charged food proteins with negatively charged moieties of mucin mainly on glycosylated region of mucin) is the major mode of interaction between them. On the other hand, casein attracts the salivary proteins only via non-covalent interactions due to its naturally self-assembled micellar structure. Moreover, recent studies related to β-lactoglobulin (BLG)-mucin interactions have clarified the importance of hydrophobic as well as hydrophilic interactions, such as hydrogen bonding. Furthermore, in vitro studies between protein emulsions and saliva observed a strong aggregating effect of saliva on caseinate and whey proteins as well as on surfactant-stabilized emulsions. Besides, the sign and the density of the charge on the surface of the protein emulsion droplets contribute significantly to the behavior of the emulsion when mixed with saliva. Other studies also suggested that the interactions between saliva and whey proteins depends on the pH in addition to the flow rate of the saliva. Overall, the role of interactions of food proteins and food protein emulsions with mucin/saliva-proteins in the oral perception, as well as the physicochemical and structural changes of proteins were discussed.

AB - Mucins are long glycoprotein molecules responsible for the gel nature of the mucous layer that covers epithelial surfaces throughout the body. Mucins, as the major salivary proteins, are also important proteins for the food oral processing and digestion. The interactions of salivary mucins and saliva with several food proteins and food protein emulsions, as well as their functional properties related to the food oral processing were reviewed in this paper. The target food proteins of focus were whey proteins (lactoferrin and beta-lactoglobulin) and non-whey proteins (casein, gelatin, galectin/lectin, and proline-rich proteins). Most of the studies suggest that electrostatic attraction (between positively charged food proteins with negatively charged moieties of mucin mainly on glycosylated region of mucin) is the major mode of interaction between them. On the other hand, casein attracts the salivary proteins only via non-covalent interactions due to its naturally self-assembled micellar structure. Moreover, recent studies related to β-lactoglobulin (BLG)-mucin interactions have clarified the importance of hydrophobic as well as hydrophilic interactions, such as hydrogen bonding. Furthermore, in vitro studies between protein emulsions and saliva observed a strong aggregating effect of saliva on caseinate and whey proteins as well as on surfactant-stabilized emulsions. Besides, the sign and the density of the charge on the surface of the protein emulsion droplets contribute significantly to the behavior of the emulsion when mixed with saliva. Other studies also suggested that the interactions between saliva and whey proteins depends on the pH in addition to the flow rate of the saliva. Overall, the role of interactions of food proteins and food protein emulsions with mucin/saliva-proteins in the oral perception, as well as the physicochemical and structural changes of proteins were discussed.

KW - Casein

KW - Emulsion

KW - Gelatin

KW - Lactoferrin

KW - Lectins

KW - Whey

KW - β-lactoglobulin

U2 - 10.1080/10408398.2018.1512950

DO - 10.1080/10408398.2018.1512950

M3 - Review

C2 - 30632771

VL - 60

SP - 64

EP - 83

JO - Critical Reviews in Food Science and Nutrition

JF - Critical Reviews in Food Science and Nutrition

SN - 1040-8398

IS - 1

ER -