Effect of synergism of sucrose ester and xanthan gum on the stability of walnut milk.

BACKGROUND: Single emulsifiers have an effect on the stability of plant protein drinks, giving some improvement. Emulsifiers are more effective in maintaining emulsion stability when combined with polysaccharides such as xanthan gum. In this paper, we studied the food-grade emulsifier sucrose ester and measured the average particle size, polydispersity value, zeta potential, microrheological properties, microstructure and creaming index related to walnut protein emulsion by constructing a walnut protein emulsion simulation system. SDS-PAGE and low-field NMR were used to analyze the relative molecular masses of emulsions and the water distribution of emulsions, respectively, to further investigate the synergistic effects of sucrose esters and xanthan gum on the ease of emulsification and intrinsic mechanisms of different molecular weight proteins of walnut protein emulsions. RESULTS: The results indicate that the synergistic effect of sucrose esters and xanthan gum was to stabilize emulsions better than single emulsifiers. Xanthan gum and protein may form protein-polysaccharide complexes, as well as the hydrophobic interaction between sucrose ester and xanthan gum. The properties of xanthan gum can improve the stability of the emulsion by affecting the mechanical properties of walnut protein emulsion, and the combination of sucrose ester and xanthan gum can better stabilize large protein molecules. CONCLUSION: The results not only provide a theoretical basis for the stability of plant protein emulsion systems, but also provide technical support for the production and processing of large-molecule plant proteins into emulsions in this field for improving their stability, and also provide more possibilities for other types of emulsions. © 2023 Society of Chemical Industry.

In vitro digestibility of proteins from historical and modern wheat cultivars.

BACKGROUND: Previous research has suggested that proteins and other quality parameters of wheats may have changed over a century of wheat breeding. These changes may affect protein digestibility. The in vitro protein digestibility of breads made with 21 cultivars of wheat introduced or released in the USA between 1870 and 2013 was therefore evaluated. RESULTS: Protein digestibility increased with release year, but was not normally distributed; three older cultivars had significantly lower digestibility than the other cultivars: 42.0 ± 0.3 mol% (primary amino N/total N) versus 34.7 ± 0.7 mol%; P < 0.001. High molecular weight (MW) protein fractions increased and low MW protein fractions decreased with release year, but these changes were not related to protein digestibility. Thus, other differences in protein composition or other flour components may contribute to diminished digestibility of the three older cultivars. CONCLUSIONS: This study identified differences in protein digestibility among wheat cultivars that may have important implications for human nutrition. Further investigation is required to determine the specific characteristics that differentiate high- and low-digestibility wheat cultivars. © 2020 Society of Chemical Industry.

Effect of different amphiphilic emulsifiers complexed with xanthan gum on the stability of walnut milk and structural characterization of their complexes.

The kind of compounding emulsifier used and the amount of compounding have a significant impact on the emulsion's stability. In this study, the average particle size, Zeta potential, emulsification index, laser confocal microstructure, and rheological properties shows that the ratio of monoglyceride-xanthan gum and sucrose ester-xanthan gum could maintain the good stability of the emulsion in a certain range, and the monoglyceride and sucrose ester compounding could effectively improve the stability of the emulsion in a specific ratio (7:3). The results of fluorescence spectroscopy, Fourier transform infrared spectroscopy and sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that the simultaneous complexation of three substances was more likely to produce hydrophobic interactions with walnut proteins than the simultaneous complexation of two substances. Also confirmed were the hydrogen bonding connections between the proteins and the monoglyceride, sucrose ester, and xanthan gum. Monoglyceride and xanthan gum complexes were also found to stabilize more proteins.

Optimal and sustainable production of tailored fish protein hydrolysates from tuna canning wastes and discarded blue whiting: Effect of protein molecular weight on chemical and bioactive properties.

Thousands tons of discards of blue whiting (BW) and tuna heads (YT) by-products are generated each year in Europe. BW is the species most discarded by European fishing fleet and, in some canning factories, YT are processed for the retrieval of oil rich in omega-3, but producing a huge amount of solid remains and effluents disposal as wastes. The development of optimal and sustainable processes for both substrates is mandatory in order to reach clean solutions under the circular economy precepts. This work focused on the mathematical optimization of the production of tailored fish protein hydrolysates (FPH), from blue whiting and tuna residues, in terms of controlling average molecular weights (Mw) of proteins. For the modeling of the protein depolymerization time-course, a pseudo-mechanistic model was used, which combined a reaction mechanistic equation affected, in the kinetic parameters, by two non-lineal equations (a first-order kinetic and like-Weibull formulae). In all situations, experimental data were accurately simulated by that model achieving R2 values higher than 0.96. The validity of the experimental conditions obtained from modeling were confirmed performing productions of FPH at scale of 5 L-reactor, without pH-control in most of cases, at the different ranges of Mw selected (1-2 kDa, 2-5 kDa and 5-10 kDa). The results showed that FPH from BW with lower Mw led to a remarkable yield of production (12 % w/w of substrate), largest protein contents (77 % w/w of BW hydrolysate), greatest in vitro digestibility (>95 %), highest essential amino acid presence (43 %) and the best antioxidant (DPPH = 62 %) and antihypertensive (IC50-ACE = 80 mg/L) properties. Our results prove that the proposed procedure to produce sustainable FPH, with specific Mw characterisitics, could be extended to other fish waste substrates. Tailored FPH may have the potential to serve as valuable ingredients for functional foods and high-quality aquaculture feed.

Effects of glutenin and gliadin on the surface tackiness of frozen cooked noodles.

The mechanism of glutenin and gliadin on the surface tackiness of recooked frozen cooked noodles (FCNs) is unclear. In this study, the effects of glutenin and gliadin addition on the surface tackiness of FCNs were investigated. The addition of glutenin and gliadin reduced the surface tackiness (3.60 and 3.50 N) of recooked FCNs stored for 0 min. The addition of glutenin increased the rigidity of the gluten network and the compactness of FCNs and made the FCNs have a moisture-distribution with multilayers. The addition of gliadin increased the tensile distance of FCNs, restricted water migration during frozen storage, and increased the membranous structure of the gluten network to wrap starch particles. Glutenin had a stronger effect on reducing the surface tackiness of FCNs than gliadin. In the future, the synergistic effects of different proportions of glutenin and gliadin on the gluten network of FCNs could be further studied.

Pea cell wall integrity controls the starch and protein digestion properties in the INFOGEST in vitro simulation.

The cell wall microstructure has been recognized to modulate the digestibility and bioaccessibility of nutrients in whole pulse foods, while the role of cell wall integrity is unclarified in the hydrolysis of intracellular nutrients during human gastrointestinal transit. Intact pea cells were isolated to prepare a series of cell wall integrity subjected to cooking and followed by the in vitro hydrolysis of starch and protein properties using the INFOGEST 2.0 in vitro simulation. Thermal properties showed that cell samples either in raw or cooked form with different wall integrity exhibited similar and higher starch gelatinization temperatures compared to the isolated starch counterpart. It was found that intact pea cells showed the limited hydrolysis extent of the maltose (16.2%) and NH2 (6.7%) compared to the damaged cells. In addition, intact cells also withheld the cell wall integrity throughout gastrointestinal digestion with minor rupture, and presented the higher protein molecular weight (70 kDa) in the SDS-PAGE profiles. Results suggested that the in vitro starch and protein digestion properties are modulated by the cell wall integrity, which may lead to lower glycemic response and open up the possibilities of designing health food products.

The Protein Level and Molecular Weight Analysis in Different Children's Toothpaste, which Probably Induced Hypersensitivity.

CONTEXT: A new case of an allergic reaction due to the use of toothpaste was found in California, United States, causing the death of an 11-year-old girl. Ingredients contained in toothpaste suspected as a cause of allergies are milk protein compounds. AIMS: The aim is to compare the protein level and molecular weight in children's toothpaste. SETTINGS AND DESIGN: Stratified random sampling. SUBJECTS AND METHODS: Samples used were children's toothpaste products in society, namely, Pepsodent®, Cussons®, Enzyme®, Kodomo®, Formula®, Colgate®, the toothpaste contain recaldent of GC Tooth Moose® and pure cow's milk. Those samples were divided into eight groups, randomly selected according to the purpose (stratified random sampling), and then coded to maintain product confidentiality. Meanwhile, samples used as comparison groups were recaldent paste and pure cow's milk. RESULTS: Each sample was analyzed for protein content using a biuret test and protein molecular weight using the sodium dodecyl sulfate-polyacrylamide gel electrophoresis test. The protein content in toothpaste is compared with the similarity of the molecular protein weight in toothpaste that contains recaldent. Protein was found in samples 2, 3, 5, 6, 7, and 8 through a biuret test, with a concentration of 1.82; 1.53; 2.76; 1.92; 1.85; and 3.2 µg/mL. However, the protein bands were only found in sample 5 with a molecular weight of 20.7 kDa, sample 6 with a molecular weight of 19.1 kDa, sample 7 with a molecular weight of 17.7 kDa, and sample 8 with 2 bands, namely, 28.7 and 39.7 kDa. CONCLUSIONS: We found the presence of protein in children's toothpaste. The protein molecular weight of recaldent paste is 17.7 kDa. Toothpaste containing protein with its molecular weight similar to recaldent's are found in samples 5 and 6.

Determination of Protein Molecular Weights on SDS-PAGE.

An apparent molecular weight (MW) of a protein can be determined from the migration distance of a protein complexed with a strong cationic detergent sodium dodecyl sulfate (SDS) separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This method was established around 1969 and has been utilized substantially even today because of its simplicity. During the following half a century, although it has been reported that many proteins show some deviation in MW when determined on SDS-PAGE especially when their peptide chains are posttranslationally modified, this versatile method is still being used very often in current biochemical works. In this protocol, a simple method to estimate MW by running SDS-PAGE of standard proteins is explained by an example in which proteins extracted from mouse retina were analyzed by two-dimensional isoelectric focusing (2-D IEF) SDS-PAGE followed by protein identification by peptide mass fingerprinting.

Tailored protein release from biodegradable poly(ε-caprolactone-PEG)-b-poly(ε-caprolactone) multiblock-copolymer implants.

In this study, the in vitro release of proteins from novel, biodegradable phase-separated poly(ε-caprolactone-PEG)-block-poly(ε-caprolactone), [PCL-PEG]-b-[PCL]) multiblock copolymers with different block ratios and with a low melting temperature (49-55°C) was studied. The effect of block ratio and PEG content of the polymers (i.e. 22.5, 37.5 and 52.5 wt%) as well as the effect of protein molecular weight (1.2, 5.8, 14, 29 and 66 kDa being goserelin, insulin, lysozyme, carbonic anhydrase and albumin, respectively) on protein release was investigated. Proteins were spray-dried with inulin as stabilizer to obtain a powder of uniform particle size. Spray-dried inulin-stabilized proteins were incorporated into polymeric implants by hot melt extrusion. All incorporated proteins fully preserved their structural integrity as determined after extraction of these proteins from the polymeric implants. In general, it was found that the release rate of the protein increased with decreasing molecular weight of the protein and with increasing the PEG content of the polymer. Swelling and degradation rate of the copolymer increased with increasing PEG content. Hence, release of proteins of various molecular weights from [PCL-PEG]-b-[PCL] multi-block copolymers can be tailored by varying the PEG content of the polymer.