Heat-Induced Gelation of Chickpea and Faba Bean Flour Ingredients.

This study aimed to investigate the gelling behavior of faba bean (FB) and chickpea (CP) flour between 10 and 20% (w/w) concentration at pH 3.0, 5.0, and 7.0. Both sources formed at pH 3.0 and 5.0 self-standing gels with 12% (w/w) of flour, while 16% (w/w) of flour was required to obtain a gel at pH 7.0. During gelling between 40 and 70 °C, a sharp increase of the elastic modulus G' was observed in both flours, mainly due to water absorption and swelling of the starch, one of the major constituents in the ingredients. Increasing the temperature at 95 °C, G' increased due to the denaturation of globulins and therefore the exposure of their internal part, which allowed more hydrophobic interactions and the formation of the gel. After cooling, both FB and CP gels displayed a solid-like behavior (tan δ ranging between 0.11 and 0.18) with G' values at pH 3.0 and 5.0 significantly (p < 0.05) higher than those at pH 7.0, due to the lower electrostatic repulsions at pHs far from the isoelectric point. The rheological properties were supported by the water binding capacity values, confirming the better gels' strength described by rheological analysis. These results will enhance our understanding of the role of legume flours in formulating innovative and sustainable food products as alternatives to animal ones.

Enhancing the Techno-Functional Properties of Lentil Protein Isolate Dispersions Using In-Line High-Shear Rotor-Stator Mixing.

In response to global challenges such as climate change and food insecurity, plant proteins have gained interest. Among these, lentils have emerged as a promising source of proteins due to their good nutritional profile and sustainability considerations. However, their widespread use in food products has been impeded by limited solubility. This study aimed to investigate the potential of high-shear mixing, a resource-efficient technique, to enhance lentil protein solubility and its functional properties. Red lentil protein isolate powders were rehydrated and subjected to a semi-continuous in-line high-shear treatment at 10,200 rpm for a timespan ranging from 0 to 15 min. The results highlighted a significant (p < 0.05) increase in solubility from 46.87 to 68.42% after 15 min of shearing and a reduction in particle size as a result of the intense shearing and disruption provided by the rotor and forced passage through the perforations of the stator. The volume-weighted mean diameter decreased from 5.13 to 1.72 µm after 15 min of shearing, also highlighted by the confocal micrographs which confirmed the breakdown of larger particles into smaller and more uniform particles. Rheological analysis indicated consistent Newtonian behaviour across all dispersions, with apparent viscosities ranging from 1.69 to 1.78 mPa.s. Surface hydrophobicity increased significantly (p < 0.05), from 830 to 1245, indicating exposure of otherwise buried hydrophobic groups. Furthermore, colloidal stability of the dispersion was improved, with separation rates decreasing from 71.23 to 24.16%·h-1. The significant enhancements in solubility, particle size reduction, and colloidal stability, highlight the potential of in-line high-shear mixing in improving the functional properties of lentil protein isolates for formulating sustainable food products with enhanced techno-functional properties.

Physicochemical properties of micellar casein retentates generated at different microfiltration temperatures.

Processing temperature has a significant influence on the composition and functionality of the resulting streams following microfiltration (MF) of skim milk. In this study, MF and diafiltration (DF) were performed at 4 or 50°C to produce ß-casein (ß-CN)-depleted and nondepleted (i.e., native casein profile) micellar casein isolate retentates, respectively. Microfiltration combined with extensive DF resulted in a 40% depletion of ß-CN at 4°C, whereas no ß-CN depletion occurred at 50°C. Microfiltration at 4°C led to higher transmission of calcium into permeates, with retentate generated at 4°C containing less total calcium compared with retentate generated at 50°C, based on the volume of retentate remaining. Higher heat stability at 120°C was measured for retentates generated at 4°C compared with those at 50°C, across all pH values measured. Retentates generated at 4°C also had significantly lower ionic calcium values at each pH compared with those generated at 50°C. Higher apparent viscosities at 4°C were measured for retentates generated at 4°C compared with retentates generated at 50°C, likely due to increased voluminosity of ß-CN-depleted casein micelles. The results of this study provide new information on how changing the composition of MF retentate, by appropriate control of processing temperature and DF, can alter physicochemical properties of casein micelles, with potential implications for ingredient functionality.

Impact of Combined Thermal Pressure Treatments on Physical Properties and Stability of Whey Protein Gel Emulsions.

Emulsion gels are gaining interest as fat replacers due to their benefits associated with calorie reduction and their versatility in a wide range of products. Their production process needs to be tailored to obtain the desired stability and physicochemical properties. This study investigated the effect of heat (70, 80, and 90 °C) and pressure (5, 10, and 15 MPa) to produce whey protein emulsion gels using a pilot-scale tubular heat exchanger equipped with a homogenization valve. Both temperature and pressure determined a significant effect (p < 0.05) on the rheological moduli, with the treated samples displaying a predominant elastic behavior. The treatments also showed an improved pseudoplasticity due to the significant reduction in the flow behavior index (p < 0.05). All the samples showed a bimodal particle size distribution; by increasing the temperature up to 80 °C, a reduction in Dv50 (50th percentile) values compared to the control samples was observed. At 90 °C, the Dv50 value increased because of coalescence and flocculation phenomena occurring during or immediately after processing. The greater aggregation and structural development obtained with stronger process conditions improved the stability of the emulsions. The results show the capability to produce gel emulsions with good physical properties that could be proposed as food ingredients to substitute fats in food products.

Formulation and Physical Stability of High Total Solids Lentil Protein-Stabilised Emulsions for Use in Plant Protein-Based Young Child Formulae.

The demand for high-quality plant protein products is increasing and the aim of this work was to evaluate the impact of increasing the total solids content on the formation and stability of lentil protein stabilised oil-in-water emulsions. A series of emulsions were formulated using different proportions of total solids: 23, 26, 29, 32, and 35% (w/v). The emulsions were formulated using three ingredients-lentil protein, sunflower oil, and maltodextrin-which made up 15.85, 27.43, and 56.72% (w/w) of the total solids, respectively. The changes in apparent viscosity, particle size distribution, and colour during thermal processing were evaluated, with the physical stability investigated using an analytical centrifuge. The apparent viscosity of the solutions increased with total solids content (25.6 to 130 mPa.s-1), as did redness colour intensity (a* value increased from 5.82 ± 0.12 to 7.70 ± 0.09). Thermal processing resulted in greater destabilisation for higher total solids samples, as evidenced by greater changes in particle size, along with decreased redness colour. These results bring a better understanding of high total solids plant protein emulsions and factors affecting their stability, which could be used for the development of cost-effective and sustainable processing solutions in the production of plant protein young child formulae.

The Protein Composition and In Vitro Digestive Characteristics of Animal- versus Plant-Based Infant Nutritional Products.

The protein composition and digestive characteristics of four commercially available infant formulae (IF) manufactured using bovine (B-IF), caprine (C-IF), soy (S-IF), and rice (R-IF) as a protein source were examined in this study. Plant-based formulae had significantly higher crude protein and non-protein nitrogen (NPN) concentrations. Static in vitro gastrointestinal digestion of these formulae, and subsequent analysis of their digestates, revealed significantly higher proteolysis of B-IF at the end of gastrointestinal digestion compared to the other formulae, as indicated by the significantly higher concentration of free amine groups. Furthermore, differences in structure formation during the gastric phase of digestion were observed, with formation of a more continuous, firmer coagulum by C-IF, while R-IF demonstrated no curd formation likely due to the extensive hydrolysis of these proteins during manufacture. Differences in digestive characteristics between formulae manufactured from these different protein sources may influence the bio-accessibility and bioavailability of nutrients, warranting additional study.

Plant-Based Alternatives to Cheese Formulated Using Blends of Zein and Chickpea Protein Ingredients.

In this study, zein protein isolate (ZPI) and chickpea protein concentrate (CPC) ingredients were used to formulate five plant-based cheese alternatives. Ingredient ratios based on protein contributions of 0:100, 25:75, 50:50, 75:25 and 100:0 from ZPI and CPC, respectively, were used. Formulations were developed at pH ~4.5, with a moisture target of 59%. Shea butter was used to target 15% fat, while tapioca starch was added to target the same carbohydrate content for all samples. Microstructural analysis showed differences among samples, with samples containing ZPI displaying a protein-rich layer surrounding the fat globules. Schreiber meltability and dynamic low amplitude oscillatory shear rheological analyses showed that increasing the proportion of ZPI was associated with increasing meltability and greater ability to flow at high temperatures. In addition, the sample containing only CPC showed the highest adhesiveness, springiness and cohesiveness values from the texture profile analysis, while the sample containing only ZPI exhibited the highest hardness. Furthermore, stretchability increased with increasing ZPI proportions. This work will help understanding of the role and potential of promising plant-protein-ingredient blends in formulating plant-based alternatives to cheese with desirable functional properties.

Influence of Transglutaminase Crosslinking on Casein Protein Fractionation during Low Temperature Microfiltration.

Low temperature microfiltration (MF) is applied in dairy processing to achieve higher protein and microbiological quality ingredients and to support ingredient innovation; however, low temperature reduces hydrophobic interactions between casein proteins and increases the solubility of colloidal calcium phosphate, promoting reversible dissociation of micellar ß-casein into the serum phase, and thus into permeate, during MF. Crosslinking of casein proteins using transglutaminase was studied as an approach to reduce the permeation of casein monomers, which typically results in reduced yield of protein in the retentate fraction. Two treatments (a) 5 °C/24 h (TA) and (b) 40 °C/90 min (TB), were applied to the feed before filtration at 5 °C, with a 0.1 µm membrane. Flux was high for TA treatment possibly due to the stabilising effect of transglutaminase on casein micelles. It is likely that formation of isopeptide bonds within and on the surface of micelles results in the micelles being less readily available for protein-protein and protein-membrane interactions, resulting in less resistance to membrane pores and flow passage, thereby conferring higher permeate flux. The results also showed that permeation of casein monomers into the permeate was significantly reduced after both enzymatic treatments as compared to control feed due to the reduced molecular mobility of soluble casein, mainly ß-casein, caused by transglutaminase crosslinking.

Influence of Glycomacropeptide on Rehydration Characteristics of Micellar Casein Concentrate Powder.

Glycomacropeptide (GMP) shows potential for enhancing the rehydration properties of high-protein dairy powders due to its hydrophilic nature. This study involved formulating micellar casein concentrate (MCC) solutions (8.6% final protein content) with 0, 10, and 20% GMP as a percentage of total protein, and investigated the physicochemical and rehydration properties of the resultant freeze-dried powders (P-MCC-0G, P-MCC-10G, and P-MCC-20G, respectively). The surface charges of caseins in the control MCC and 10 or 20% GMP blended solutions were -25.8, -29.6, and -31.5 mV, respectively. Tablets prepared from P-MCC-10G or P-MCC-20G powders displayed enhanced wettability with contact angle values of 80.6° and 79.5°, respectively, compared with 85.5° for P-MCC-0G. Moreover, blending of GMP with MCC resulted in faster disintegration of powder particles during rehydration (i.e., dispersibility) compared to P-MCC-0G. Faster and more extensive release of caseins from powder particles into solution was evident with the increasing proportion of GMP, with the majority of GMP released within the first 15 min of rehydration. The results of this study will contribute to further development of formulation science for achieving enhanced solubility characteristics of high-protein dairy powder ingredients, such as MCC.

The effect of pulsed electric fields on carotenoids bioaccessibility: The role of tomato matrix.

Tomato fractions were subjected to pulsed electric fields treatment combined or not with heating. Results showed that pulsed electric fields and heating applied in combination or individually induced permeabilization of cell membranes in the tomato fractions. However, no changes in ß-carotene and lycopene bioaccessibility were found upon combined and individual pulsed electric fields and heating, except in the following cases: (i) in tissue, a significant decrease in lycopene bioaccessibility upon combined pulsed electric fields and heating and heating only was observed; (ii) in chromoplasts, both ß-carotene and lycopene bioaccessibility significantly decreased upon combined pulsed electric fields and heating and pulsed electric fields only. The reduction in carotenoids bioaccessibility was attributed to modification in chromoplasts membrane and carotenoids-protein complexes. Differences in the effects of pulsed electric fields on bioaccessibility among different tomato fractions were related to tomato structure complexity.

Use of time-resolved spectroscopy as a method to monitor carotenoids present in tomato extract obtained using ultrasound treatment.

INTRODUCTION: Compounds exhibiting antioxidant activity have received much interest in the food industry because of their potential health benefits. Carotenoids such as lycopene, which in the human diet mainly derives from tomatoes (Solanum lycopersicum), have attracted much attention in this aspect and the study of their extraction, processing and storage procedures is of importance. Optical techniques potentially offer advantageous non-invasive and specific methods to monitor them. OBJECTIVES: To obtain both fluorescence and Raman information to ascertain if ultrasound assisted extraction from tomato pulp has a detrimental effect on lycopene. METHOD: Use of time-resolved fluorescence spectroscopy to monitor carotenoids in a hexane extract obtained from tomato pulp with application of ultrasound treatment (583 kHz). The resultant spectra were a combination of scattering and fluorescence. Because of their different timescales, decay associated spectra could be used to separate fluorescence and Raman information. This simultaneous acquisition of two complementary techniques was coupled with a very high time-resolution fluorescence lifetime measurement of the lycopene. RESULTS: Spectroscopic data showed the presence of phytofluene and chlorophyll in addition to lycopene in the tomato extract. The time-resolved spectral measurement containing both fluorescence and Raman data, coupled with high resolution time-resolved measurements, where a lifetime of ~5 ps was attributed to lycopene, indicated lycopene appeared unaltered by ultrasound treatment. Detrimental changes were, however, observed in both chlorophyll and phytofluene contributions. CONCLUSION: Extracted lycopene appeared unaffected by ultrasound treatment, while other constituents (chlorophyll and phytofluene) were degraded.

Use of Time-Resolved Fluorescence to Monitor Bioactive Compounds in Plant Based Foodstuffs.

The study of compounds that exhibit antioxidant activity has recently received much interest in the food industry because of their potential health benefits. Most of these compounds are plant based, such as polyphenolics and carotenoids, and there is a need to monitor them from the field through processing and into the body. Ideally, a monitoring technique should be non-invasive with the potential for remote capabilities. The application of the phenomenon of fluorescence has proved to be well suited, as many plant associated compounds exhibit fluorescence. The photophysical behaviour of fluorescent molecules is also highly dependent on their microenvironment, making them suitable probes to monitor changes in pH, viscosity and polarity, for example. Time-resolved fluorescence techniques have recently come to the fore, as they offer the ability to obtain more information, coupled with the fact that the fluorescence lifetime is an absolute measure, while steady state just provides relative and average information. In this work, we will present illustrative time-resolved measurements, rather than a comprehensive review, to show the potential of time-resolved fluorescence applied to the study of bioactive substances. The aim is to help assess if any changes occur in their form, going from extraction via storage and cooking to the interaction with serum albumin, a principal blood transport protein.

Effect of ultrasound treatment, oil addition and storage time on lycopene stability and in vitro bioaccessibility of tomato pulp.

This study was performed to investigate the influence of ultrasound processing on tomato pulp containing no sunflower oil, or increasing amounts (i.e. 2.5%, 5% and 10%), on lycopene concentration and in vitro bioaccessibility at time zero and during storage at 5 °C. Results confirmed previous findings in that ultrasonication was responsible for cell breakage and subsequent lycopene release in a highly viscous matrix. Neither the ultrasound process nor oil addition affected lycopene concentration. A decrease of approximately 35% lycopene content occurred at storage times longer than 15 days, due to isomerisation and oxidation reactions. No differences in lycopene in vitro bioaccessibility were found between the untreated and ultrasonically treated samples; this parameter decreased as a consequence of oil addition. Losses of lycopene in vitro bioaccessibility ranging between 50% and 80% occurred in the untreated and ultrasonically treated tomato pulps with and without oil during storage, mainly due to carotenoid degradation.