Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

Çelebioğlu, Hilal Yilmaz; Guðjónsdóttir, María; Meier, Sebastián; Duus, Jens Øllgaard; Lee, Sang M.; Chronakis, Ioannis S.

doi:10.1016/j.foodhyd.2015.04.026

Cited by 23 publications

(24 citation statements)

References 47 publications

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“…This is readily understandable for the case of pH 7.4, where both BLG and BSM were negatively charged, and thus BSM molecules may be repelled in approaching to the interface. However, at pH 3.0, BLG and BSM molecules are oppositely charged and even hydrogen bonding were observed to be activated [8]. Similar trends of the interfacial properties were also observed for the viscous modulus G i '' mix of the mixture when correlated with G i '' BLG and G i '' BSM (the viscous modulus of BLG and BSM) and the term ∆G i '' (Fig.…”

Section: Time Dependence Of the Interfacial Modulussupporting

confidence: 72%

“…For instance, the slopes of G i ' of MIX 2 were -1. formation and lower modulus than MIX 1 due to the higher content of BSM ( Table 3). The higher hydrophilic interaction between the proteins at pH 3.0, as well as the increased electrostatic attraction between positively charged BLG and negatively charged BSM, as suggested at our previous study [8], most probably caused the BSM to be imbedded into the assembled BLG layer and destabilize the interfacial network.…”

Section: 3strain Dependence Of the Interfacial Modulussupporting

confidence: 51%

“…The interaction between a model food protein, BLG, and saliva protein, bovine submaxillary mucin (BSM), has been investigated by different techniques, including nuclear magnetic resonance, dynamic light scattering, circular dichroism, in our recent study [8]. The main findings are: (i) An attractive interaction between the two proteins was suggested.…”

Section: Introductionmentioning

confidence: 99%

“…The positively charged groups of BLG, especially at acidic pHs, neutralized negatively charged groups of BSM and caused the BSM to coil or contract into a smaller hydrodynamic volume [8,9].…”

Section: Introductionmentioning

confidence: 99%

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Interfacial shear rheology of β-lactoglobulin—Bovine submaxillary mucin layers adsorbed at air/water interface

Çelebioğlu

Kmiecik-Palczewska

Lee

et al. 2017

International Journal of Biological Macromolecules

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The interfacial rheological properties of solutions of β-lactoglobulin (BLG), as a model food compound, mixed with bovine submaxillary mucin (BSM), a major salivary protein, have been investigated. Time, frequency, stress sweep and flow measurements have been performed at different pHs (7.4, 5.0 and 3.0), to investigate the air/water interfacial properties. All protein layers (BLG, BSM, and BLG-BSM mixtures) formed an elastic network at the air/water interface with low frequency dependence of the interfacial modulus. The results indicated that BLG moves faster as smaller molecule than mucin, and dominate the surface adsorption and the network formation for the BLG-BSM mixtures. Moreover, BLG-BSM protein mixtures exhibited interfacial properties with lower elastic and viscous moduli than BLG, as a result of competitive displacement of BLG proteins with BSMs from the interface. It is suggested that hydrophobic patches of BSM can be imbedded into the BLG monolayer as driven by a strong hydrophobic interaction with air and disrupt the cohesive assembly of BLG, whereas the hydrophilic (negatively charged) parts of the BSM chain are protruding from the interface towards the bulk water.

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Section: Time Dependence Of the Interfacial Modulussupporting

confidence: 72%

Section: 3strain Dependence Of the Interfacial Modulussupporting

confidence: 51%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Interfacial shear rheology of β-lactoglobulin—Bovine submaxillary mucin layers adsorbed at air/water interface

Çelebioğlu

Kmiecik-Palczewska

Lee

et al. 2017

International Journal of Biological Macromolecules

Self Cite

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“…Salivary mucin, a kind of salivary protein, accompanies with the whole digestive process from the oral to gastrointestinal organs and plays a significant role in the protection of oral cavity [6,7]. Submaxillary mucin is the most associated mucin types in oral processing [5].…”

Section: Introductionmentioning

confidence: 99%

Probing into the Interaction of Nicotine and Bovine Submaxillary Mucin: NMR, Fluorescence, and FTIR Approaches

Liao

Yuan

Yang

et al. 2016

Journal of Spectroscopy

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Nicotine, the important component of cigarette products, may have an impact on the oral environment after inhalation. The research of interaction between nicotine and bovine submaxillary mucin (BSM) contributes to understand the binding mechanism of nicotine and BSM, and the effects of nicotine on the structure and function of the mucin. NMR data demonstrated that the interaction between nicotine and BSM did exist, and it was pyrrolidyl ring of nicotine playing the major role in the binding. The quenching mechanisms of nicotine and BSM in different pH were different: for acidic environment, the quenching was dynamic; while it became static in the alkaline circumstance. Synchronous fluorescence spectra indicated that nicotine had effect on the microenvironment of the Trp rather than Tyr residue. Meanwhile, the impact of nicotine on the conformation of BSM was also confirmed by 3D fluorescence and FTIR spectra.

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NMR Relaxometry and Imaging of Dairy Products

Mariette¹

2017

Modern Magnetic Resonance

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Spectroscopic studies of the interactions between β-lactoglobulin and bovine submaxillary mucin

Cited by 23 publications

References 47 publications

Interfacial shear rheology of β-lactoglobulin—Bovine submaxillary mucin layers adsorbed at air/water interface

Interfacial shear rheology of β-lactoglobulin—Bovine submaxillary mucin layers adsorbed at air/water interface

Probing into the Interaction of Nicotine and Bovine Submaxillary Mucin: NMR, Fluorescence, and FTIR Approaches

NMR Relaxometry and Imaging of Dairy Products

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