Influence of chitosan coating on protein-based nanohydrogels properties and in vitro gastric digestibility

Bourbon, Ana I.; Pinheiro, Ana Cristina; Cerqueira, Miguel A.

doi:10.1016/j.foodhyd.2016.03.002

Cited by 50 publications

(28 citation statements)

References 41 publications

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“…Samples of β-Lg were characterized in terms of particle size, polydispersity index (PDI) and ζ-potential by Dynamic Light Scattering (DLS) apparatus (Zetasizer Nano ZS, Malvern Instruments, UK) equipped with He-Ne laser at a wavelength of 633 nm, at 25°C (Bourbon, Pinheiro, Cerqueira, & Vicente, 2016). Particle size was determined by the method of cumulants fit and was translated into average particle diameters (Z-value) using the Stokes-Einstein relationship .…”

Section: Particle Size Polydispersity Index and ζ-Potentialmentioning

confidence: 99%

“…CD spectra were obtained resorting to a Jasco J-1500 spectropolarimeter (Jasco International Co, Japan). For far-UV experiments, samples in appropriate dilution and spectra were recorded at 25°C, under constant nitrogen flush, using a quartz cuvette with an optical path length of 1.0 mm (Hellma Analytics, Germany), from 190 nm to 260 nm wavelength range with data pitch of 1.0 nm and accumulation of 3 scan, following the procedure used by Bourbon et al (2016). The CD baseline scan was recorded using a standard solution of 25 mmol L −1 sodium phosphate buffer and then subtracted to scans from β-Lg solutions.…”

Section: Circular Dichroismmentioning

confidence: 99%

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Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables

et al. 2020

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A B S T R A C Tβ-lactoglobulin (β-Lg) is the major protein fraction of bovine whey serum and its principal gelling agent. Its gelation capacity enables conformational changes associated with protein-protein interactions that allow the design of structures with different properties and morphologies. Thus, the aim of this work was to successfully use β-Lg, purified from a commercial whey protein isolate, to develop food-grade micro-(with diameters between 200 and 300 nm) and nano-(with diameters ≤ 100 nm) structures. For this purpose, the phenomena involved in β-Lg gelation were studied under combined effects of concentrations (from 5 to 15 mg mL −1 ), heating temperature (from 60 to 80°C) and heating time (from 5 to 25 min) for pH values of 3, 4, 6 and 7. The effects of such conditions on β-Lg structures were evaluated and the protein was fully characterized in terms of size, polydispersity index (PDI) and surface charge (by dynamic light scattering -DLS), morphology (by transmission electron microscopy -TEM) and conformational structure (circular dichroism, intrinsic and extrinsic fluorescence). Results have shown that β-Lg nanostructures were formed at pH 3 (with diameters between 12.1 and 22.3 nm) and at 7 (with diameters between 8.9 and 35.3 nm). At pH 4 structures were obtained at macroscale (i.e., ≥ 6 μm) for all β-Lg concentrations when heated at 70 and 80°C, independent of the time of heating. For pH 6, it was possible to obtain β-Lg structures either at micro-(245.0 -266.4 nm) or nanoscale (≤ 100 nm) with the lowest polydispersity (PDI) values (≤ 0.25), in accordance with TEM analyses, for heating at 80°C for 15 min. Intrinsic and extrinsic fluorescence data and far-UV circular dichroism spectra measurements revealed conformational changes on β-Lg structure that support these evidences. A strict control of the physical and environmental conditions is crucial for developing β-Lg structures with the desired characteristics, thus calling for the understanding of the mechanisms of protein aggregation and intermolecular interaction when designing β-Lg structures with novel functionalities.

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Section: Particle Size Polydispersity Index and ζ-Potentialmentioning

confidence: 99%

Section: Circular Dichroismmentioning

confidence: 99%

Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables

et al. 2020

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“…The increment in absolute zeta potential of PWP could be observed when the level of SL increased from 0 to 1%. Besides the electrostatic attraction and hydrophobic interactions between WP and SL that could induce the exposure of negative residues, heat treatment could also change the structure and expose inner groups of proteins (Bourbon et al, 2016). Zeta potential of PWP exhibited a minimum of −69.44 ± 2.61 mV with 1% SL; the value increased with the increase in SL level.…”

Section: Zeta Potential Of Wp or Pwp In The Presence Of Slmentioning

confidence: 99%

“…Interactions between surfactants and proteins can induce changes in protein conformation (Kelley and Mcclements, 2003). As a technique for evaluating the secondary structure of proteins, CD spectroscopy can be used to investigate the interactions between proteins and other molecules (Bourbon et al, 2016). The effect of the addition of SL on the secondary structure of WP and PWP by heating for 20 min was investigated by CD spectroscopy (Figure 7).…”

Section: Secondary Structure Of Wp or Pwp In The Presence Of Slmentioning

confidence: 99%

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

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Soybean lecithin is often used as a surfactant in food formulation. The aim of this study was to investigate the interactions between soybean lecithin (SL, 0-3%, wt/vol) and whey protein (WP, 10%, wt/vol) or polymerized whey protein (PWP, 10%, wt/vol) induced by heating WP solutions at 85°C for 0 to 20 min at pH 7.0. The samples were evaluated for zeta potential, particle size, morphology, rheological properties, thermal properties, secondary structure, and surface hydrophobicity. Zeta potential of WP increased linearly as SL level increased from 0 to 3%, whereas that of PWP changed with plateau at SL level of 1%, which may be due to the aggregation of SL. The addition of SL increased the particle size and apparent viscosity of both WP and PWP. All the samples exhibited different morphology depending on SL level and heating time according to transmission electron microscopy images. Whey protein showed obviously decreased gelation time and increased storage modulus in the presence of SL. Differential scanning calorimetry curves confirmed the effects of SL on the thermal properties of both WP and PWP. Circular dichroism spectra indicated that SL had effects on the secondary structure of both WP and PWP. The changes in surface hydrophobicity indicated the hydrophobic interactions between WP/PWP and SL. Data indicate that the physicochemical and functional properties of WP and PWP can be altered by adding soybean lecithin.

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“…These large particles sizes were due to precipitates formed during in vitro digestion. These precipitates production could be due to aggregation or flocculation provoked by digestive enzymes action or to changes in pH and ionic strength (Bourbon, Pinheiro, Cerqueira, & Vicente, 2016;Pinheiro et al, 2013).…”

Section: Evaluation Of β-Lg Micro-and Nanostructures Responsiveness Amentioning

confidence: 99%

β-lactoglobulin micro- and nanostructures as bioactive compounds vehicle: In vitro studies

Simões

Martins

Pinheiro

et al. 2020

Food Research International

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Lactoglobulin (β-Lg) is known to be capable to bind hydrophilic and hydrophobic bioactive compounds. This research aimed to assess the in vitro performance of β-Lg micro-(diameter ranging from 200 to 300 nm) and nano (diameter < 100 nm) structures associated to hydrophilic and hydrophobic model compounds on Caco-2 cells and under simulated gastrointestinal (GI) conditions. Riboflavin and quercetin were studied as hydrophilic and hydrophobic model compounds, respectively. Cytotoxicity experiment was conducted using in vitro cellular model based on human colon carcinoma Caco-2 cells. Moreover, the digestion process was simulated using the harmonized INFOGEST in vitro digestion model, where samples were taken at each phase of digestion processoral, gastric and intestinal-and characterized in terms of particle size, polydispersity index (PDI), surface charge by dynamic light scattering (DLS); protein hydrolysis degree by 2,4,6-trinitrobenzene sulfonic acid (TNBSA) assay and native polyacrylamide gel electrophoresis; and bioactive compound concentration. Caco-2 cell viability was not affected up to 21 × 10 −3 mg mL −1 of riboflavin and 16 × 10 −3 mg mL −1 quercetin on β-Lg micro-and nanostructures. In the oral phase, β-Lg structures' particle size, PDI and surface charge values were not changed comparing to the initial β-Lg structures (i.e., before being subjected to in vitro GI digestion). During gastric digestion, β-Lg structures were resistant to proteolytic enzymes and to acid environment of the stomachconfirmed by TNBSA and native gel electrophoresis. In vitro digestion results indicated that β-Lg micro-and nanostructures protected both hydrophilic and hydrophobic compounds from gastric conditions and deliver them to target site (i.e., intestinal phase). In addition, β-Lg structures were capable to enhance riboflavin and quercetin bioaccessibility and bioavailability potential compared to bioactive compounds in their free form. This study indicated that β-Lg micro-and nanostructures were capable to enhance hydrophilic and hydrophobic compounds bioavailability potential and they can be used as oral delivery systems.

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Influence of chitosan coating on protein-based nanohydrogels properties and in vitro gastric digestibility

Cited by 50 publications

References 41 publications

Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables

Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

β-lactoglobulin micro- and nanostructures as bioactive compounds vehicle: In vitro studies

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