Christophe Schmitt

Nestlé (Switzerland)

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Lionel Bovetto

Nestlé (Switzerland)

Taco Nicolaï

Institut des Molécules et Matériaux du Mans

Jochen Weiß

University of Hohenheim

Pascal Moll

University of Hohenheim

Hanna Salminen

University of Hohenheim

Juliana V.C. Silva

Nestlé (Switzerland)

Martin E. Leser

University of Fribourg

Claudine Bovay

Nestlé (Switzerland)

Luca Amagliani

Nestlé (Switzerland)

Christophe Chassenieux

Institut des Molécules et Matériaux du Mans

Cooperative Institutions

Nestlé (Switzerland)

Centre National de la Recherche Scientifique

University of Hohenheim

Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement

Le Mans Université

University of Fribourg

Institut National de la Recherche Agronomique

Université de Montpellier

Nestlé (Brazil)

ETH Zurich

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Comparison of the functional properties of RuBisCO protein isolate extracted from sugar beet leaves with commercial whey protein and soy protein isolates

Journal of the Science of Food and Agriculture (2018)

Anneke H. Martin Oscar Castellani Govardus A. H. de Jong Lionel Bovetto Christophe Schmitt

RuBisCO was extracted from sugar beet leaves using soft and food-compatible technologies. Proximate composition, solubility, emulsifying, foaming and gelling properties of the protein isolate were determined. All these properties were systematically benchmarked against commercial whey and soy protein isolates used in food applications.RuBisCO protein isolate (RPI) contained 930 g kg-1 of crude protein. Protein solubility was higher than 80% at pH values lower than 4.0 or higher than 5.5. Foaming capacity of RPI was better at pH 4.0 than at pH 7.0. Interestingly, 10 g kg-1 protein foams were more stable (pH 7.0 and 4.0) than foams obtained with whey or soy protein. Moreover, 10 g kg-1 RPI emulsions at pH 4.0 or 7.0 exhibited good stability, being similar to whey protein isolate. Remarkable gelling properties were observed at pH 7.0, where 50 g kg-1 protein solutions of RPI formed self-supporting gels while more concentrated solutions were needed for whey or soy protein.RuBisCO showed comparable or superior functional properties to those of currently used whey and soy protein isolates. These results highlight the high potential of sugar beet leaf protein isolate as a nutritious and functional food ingredient to face global food security and protein supply. © 2018 Society of Chemical Industry.

Pea protein

Protein isolate

Ingredient

Whey protein isolate

10.1002/jsfa.9335

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Citations (71)

Effect of the pH and NaCl on the microstructure and rheology of mixtures of whey protein isolate and casein micelles upon heating

Food Hydrocolloids (2017)

Bach T. Nguyen Christophe Chassenieux Taco Nicolaï Christophe Schmitt

Syneresis

Whey protein isolate

10.1016/j.foodhyd.2017.03.013

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Citations (45)

Characterization of soluble and insoluble fractions obtained from a commercial pea protein isolate

Journal of Dispersion Science and Technology (2022)

Pascal Moll Hanna Salminen Oskar Seitz Christophe Schmitt Jochen Weiß

In this study, the characteristics of pea protein isolates after aqueous fractionization into water-soluble and water-insoluble fractions by centrifugation, decantation, and lyophilization were studied. Chemical composition and physicochemical properties upon pH changes were determined. The overall protein compositions of both soluble and insoluble pea protein fractions were similar containing albumins, globulins, and lipoxygenases, but amino acid compositions slightly varied. Distinct differences were observed in their charge properties, particle sizes, and voluminosities. The soluble pea protein fraction was free of measurable particles at pH 7, whereas the insoluble proteins contained particles with sizes of > 80 µm. Close to their respective isoelectric points, the soluble (pI = 3.9) and insoluble pea proteins (pI = 4.9) had very similar sizes of 40–50 µm. At pH 3, the particle sizes of soluble proteins did not change, however, the insoluble pea proteins had again sizes of > 80 µm. Voluminosity of the insoluble fraction was pH-dependent and had its highest voluminosity at pH 3 and 7, indicating changes in water binding as a function of pH. In contrast, the voluminosity of the soluble pea protein fraction did not change with pH. Taken together, this study showed that water-soluble and insoluble pea protein fractions of a commercial isolate may differ substantially with respect to their physicochemical properties. Observed inconsistencies in technofunctionality of various commercial preparations could thus be promoted by varying ratios between the two fractions.

Pea protein

Fraction (chemistry)

Water soluble

Decantation

10.1080/01932691.2022.2093214

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Citations (31)

Formation of conjugates between β-lactoglobulin and allyl isothiocyanate: Effect on protein heat aggregation, foaming and emulsifying properties

Food Hydrocolloids (2010)

Koraljka Rade-Kukic Christophe Schmitt Harshadrai M. Rawel

Allyl isothiocyanate

Conjugate

Beta-lactoglobulin

Sinigrin

10.1016/j.foodhyd.2010.08.018

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Citations (52)

Whey Protein Soluble Aggregates from Heating with NaCl: Physicochemical, Interfacial, and Foaming Properties

Langmuir (2007)

Christophe Schmitt Claudine Bovay Martine Rouvet Sabrina Shojaei-Rami E. Kolodziejczyk

Whey protein isolate was heat-treated at 85 °C for 15 min at pH ranging from 6.0 to 7.0 in the presence of NaCl in order to generate the highest possible amount of soluble aggregates before insolubility occurred. These whey protein soluble aggregates were characterized for composition, hydrodynamic diameter, apparent molecular weight, ζ-potential, surface hydrophobicity index, activated thiol group content, and microstructure. The adsorption kinetics and rheological properties (E', ηd) of these soluble aggregates were probed at the air/water interface. In addition, the gas permeability of a single bubble stabilized by the whey protein soluble aggregates was determined. Finally, the foaming and foam-stabilizing properties of these aggregates were measured. The amount of whey protein soluble aggregates after heat treatment was increased from 75% to 95% from pH 6.0 to pH 7.0 by addition of 5 mM to 120 mM NaCl, respectively. These soluble aggregates involved major whey protein fractions and exhibited a maximum of activated thiol group content at pH > 6.6. The hydrodynamic radius and the surface hydrophobicity index of the soluble aggregates increased from pH 6.0 to 7.0, but the molecular weight and ζ-potential decreased. This loss of apparent density was clearly confirmed by microscopy as the soluble aggregates shifted from a spherical/compact structure at pH 6.0 to a more fibrillar/elongated structure at pH 7.0. Surface adsorption was faster for soluble aggregates formed at pH 6.8 and 7.0 in the presence of 100 and 120 mM NaCl, respectively. However, interfacial elasticity and viscosity measured at 0.01 Hz were similar from pH 6.0 to 7.0. Single bubble gas permeability significantly decreased for aggregates generated at pH > 6.6. Furthermore, these aggregates exhibited the highest foamability and foam liquid stability. Air bubble size within the foam was the lowest at pH 7.0. The coarsening exponent, α, fell within predicted values of 1/3 and 1/2, except for very dry foams where it was 1/5.

Whey protein isolate

10.1021/la0632575

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Citations (235)

Heat induced formation of beta-lactoglobulin microgels driven by addition of calcium ions

Food Hydrocolloids (2012)

Tuan Phan-Xuan Dominique Durand Taco Nicolaï Laurence Donato Christophe Schmitt

Molar ratio

Hydrodynamic radius

10.1016/j.foodhyd.2012.09.008

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Citations (73)

Sulfamic acid cleaning solution for 4,4'methylene-bis-ortho-chloroaniline (MOCA)

Christophe Schmitt G. W. CAGLE

extensive 24-hr covalent binding was detected for liver DNA with 49.11 pmol/mg DNA (t1/2 = 11.1 days). After dermal administration of MOCA the major portion of the dose, 86.2%, remained at the application site throughout the study. For these rats the 24-hr covalent binding determined for liver DNA was 0.38 pmol/mg DNA (t1/2 = 15.6 days). Although lower levels were detected after dermal application, similar stability of MOCA-DNA adducts indicates that quantification of such MOCA adducts may be useful for the long-term industrial biomonitoring of MOCA exposure and for the evaluation of human DNA-MOCA adduct formation, a lesion thought to be associated with the production of cancer.

10.2172/4300980

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Solidification of concentrated pea protein–pectin mixtures as potential binder

Journal of the Science of Food and Agriculture (2023)

Pascal Moll Hanna Salminen Lucie Stadtmüller Christophe Schmitt Jochen Weiß

Binders in plant-based meat analogues allow different components, such as extrudate and fat particles, to stick together. Typically, binders then are solidified to transform the mass into a non-sticky, solid product. As an option for a clean-label binder possessing such properties, the solidification behavior of pea protein-pectin mixtures (250 g kg-1 , r = 2:1, pH 6) was investigated upon heating, and upon addition of calcium, transglutaminase, and laccase, or by combinations thereof.Mixtures of (homogenized) pea protein and apple pectin had higher elastic moduli and consistency coefficients and lower frequency dependencies upon calcium addition. This indicated that calcium physically cross-linked pectin chains that formed the continuous phase in the biopolymer matrix. The highest degree of solidification was obtained with a mixture of pea protein and sugar beet pectin upon addition of laccase that covalently cross-linked both biopolymers involved. All solidified mixtures lost their stickiness. A mixture of soluble pea protein and apple pectin solidified only slightly through calcium and transglutaminase, probably due to differences in the microstructural arrangement of the biopolymers.The chemical makeup of the biopolymers and their spatial distribution determines solidification behavior in concentrated biopolymer mixtures. In general, pea protein-pectin mixtures can solidify and therefore have the potential to act as binders in meat analogues. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

Pectin

Pea protein

10.1002/jsfa.12448

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Citations (5)

Effect of Time on the Interfacial and Foaming Properties of β-Lactoglobulin/Acacia Gum Electrostatic Complexes and Coacervates at pH 4.2

Langmuir (2005)

Christophe Schmitt Tânia Palma da Silva Claudine Bovay Sabrina Rami-Shojaei Philippe Frossard

The electrostatic complexation between β-lactoglobulin and acacia gum was investigated at pH 4.2 and 25 °C. The binding isotherm revealed a spontaneous exothermic reaction, leading to a ΔHobs = −2108 kJ mol-1 and a saturation protein to polysaccharide weight mixing ratio of 2:1. Soluble electrostatic complexes formed in these conditions were characterized by a hydrodynamic diameter of 119 ± 0.6 nm and a polydispersity index of 0.097. The effect of time on the interfacial and foaming properties of these soluble complexes was investigated at a concentration of 0.1 wt % at two different times after mixing (4 min, referred as t ∼ 0 h and t = 24 h). At t ∼ 0 h, the mixture is mainly made of aggregating soluble electrostatic complexes, whereas after 24 h these complexes have already insolubilize to form liquid coacervates. The surface elasticity, viscosity and phase angle obtained at low frequency (0.01 Hz) using oscillating bubble tensiometry revealed higher fluidity and less rigidity in the film formed at t ∼ 0 h. This observation was confirmed by diminishing bubble experiments coupled with microscopy of the thin film. It was thicker, more homogeneous and contained more water at t ∼ 0 h as compared to t = 24 h (thinner film, less water). This led to very different gas permeability's of Kt ∼ 0 h = 0.021 cm s-1 and Kt=24h = 0.449 cm s-1, respectively. Aqueous foams produced with the β-lactoglobulin/acacia gum electrostatic complexes or coacervates exhibited very different stability. The former (t ∼ 0 h) had a stable volume, combining low drainage rate and mainly air bubble disproportionation as the destabilization mechanism. By contrast, using coacervates aged for 24 h, the foam was significantly less stable, combining fast liquid drainage and air bubble destabilization though fast gas diffusion followed by film rupture and bubble coalescence. The strong effect of time on the air/water interfacial properties of the β-lactoglobulin/acacia gum electrostatic complexes can be understood by their reorganization at the interface to form a coacervate phase that is more fluid/viscous at t ∼ 0 h vs rigid/elastic at t = 24 h.

Coacervate

Tragacanth

Beta-lactoglobulin

Gum arabic

Dispersity

10.1021/la0510984

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Citations (90)

Preface

Elsevier eBooks (2024)

Janitha P.D. Wanasundara Christophe Schmitt Buddhi Lamsal

10.1016/b978-0-323-91721-6.00020-7

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