Denaturation Temperature Research Articles

Development of a cabin for fast freezing in a household refrigerator and examination of its effects on the quality characteristics of beef

In this study, a cabin design was made for fast freezing in household refrigerators using different fan types (radial fan velocity of 1100, 1500 and 1900 rpm) and axial (1350 rpm) and the effects on the quality characteristics of beef were examined. Before the freezing process, the beef (Semitendinosus) was sized at 10 × 10 × 2 cm as a single fillet; 2 × 2 × 2 cm as the cubed sample and the minced beef was prepared by the butcher from the same meat and shaped with the dimensions of 10 × 10 × 2 cm. It was seen that when the fan velocity was 1900 rpm during the freezing process, the weight (0.39–11.61 %) and cooking loss (26.69–44.66 %) values of the beef samples decreased. A decrease was observed in the TBARS values (0.34–0.87) of the sample as the radial fan velocity increased in radial fan. When the total color change values (3.96–7.59) of all beef samples were examined, it was seen that the least color change was achieved with the axial fan before and after cooking. When the textural properties of the meat were examined before and after cooking, it was observed that the hardness decreased as the radial fan velocity increased, and the lowest hardness value was obtained from freezing with the axial fan. In addition, porosity values decreased and protein denaturation temperatures increased due to the formation of smaller ice crystals with the axial fan. As a result, it has been observed that fan type and velocity have significant effects on accelerating the freezing process and preserving the quality of beef samples.

An improved linear systems model of hydrothermal isometric tension testing to aid in assessing bone collagen quality: Effects of ribation and type-2 diabetes.

This study sought to further develop and validate a previously proposed physics-based model that maps denaturation kinetics from differential scanning calorimetry (DSC) to the isometric tension generated during hydrothermal isometric tension (HIT) testing of collagenous tissues. The primary objectives of this study were to verify and validate two physics-based model parameters: α, which indicates the amount of instantaneous isometric tension developed per unit of collagen denaturation, and β, which captures the proportionality between temperature and the generated isometric tension post denaturation initiation. These parameters were used as measures of bone collagen quality, employing data from HIT and DSC testing of human bone collagen from two previous studies. Additionally, given the physical basis of the model, the study aimed to further validate Max.Slope, the rate of change in isometric tensile stress with change in temperature, as an independent measure of collagen network connectivity. Max.Slope has previously been positively correlated with measures of cortical bone fracture resistance. Towards this verification and validation, the hypotheses were a) that α would correlate strongly with HIT denaturation temperature, Td, and the enthalpy of melting (ΔH) from DSC, and b) that β would correlate positively and strongly with Max.Slope.The model was employed in the analysis of HIT-DSC data from the testing of demineralized bone collagen isolated from cadaveric human femurs in two prior studies. In one study, data were collected from HIT-DSC testing of cortical bone collagen from 74 donors. Among them, 38 had a history of type 2 diabetes +/− chronic kidney disease, while the remaining 36 had no history of T2D again with or without CKD. Cortical bone specimens were extracted from the lateral mid-shaft. The second study involved 15 donor femora, with four cortical bone specimens extracted from each. Of these four, two specimens underwent a 4-week incubation in 0.1 M ribose at 37 °C to induce non-enzymatic ribation and advanced glycation endproducts, while the other two served as non-ribated controls.The examination involved investigating correlations between the model parameters α and β and various measures, such as Max.Slope, Td, ΔH, age, and duration of type 2 diabetes. The results revealed positive correlations between the model parameter β and Max.Slope (r = 0.55–0.58). The parameter α was found to be associated with Td, but also sensitive to the shape of the HIT curve around Td resulting in difficulties with variability and interpretation. As a result, while both hypotheses are confirmed, Max.Slope and β are better indicators of bone collagen quality because they are measures of the connectivity or, more generally, the integrity of the bone collagen network.

Expanding the Frontiers of nail product evaluation: Novel application of differential scanning calorimetry (DSC) for assessing crosslinking density and predicting nail brittleness and flexibility.

While modern industry advancements have expanded nail beautification options, scientific literature primarily focuses on nail biology and medicine, with limited attention on cosmetic treatments. This study aimed to investigate human nail denaturation properties, including gender impact, blending nails to enlarge the sample pool, nail sensitization through bleaching, and active effectiveness testing. The objective was to understand the DSC and bending fatigue relationship, and define the consumer relevance of the DSC test. Nail clippings were collected from adult female and male volunteers. The wet DSC was employed to validate sample preparation, explore the effects of gender, and assess the potential of using blended nails for claims substantiation testing. Nails were sensitized through bleaching using hydrogen peroxide. The effects were confirmed through DSC and nail flexure tests. Furthermore, the ability of actives to address concerns related to nail softness and brittleness was assessed using these techniques. The results confirmed the viability of equilibrating nails in water for up to 14 h as a standardized testing method. The denaturation temperature results were independent of gender and suitable for claims substantiation testing. Blending nails from different sources did not yield significant variations in denaturation properties. A preliminary study suggested that cadaver nails should be used with caution because they exhibited differences in denaturation temperature, influenced by the sampling location. Bending fatigue tests highlighted the significance of humidity, with higher humidity conditions (80%) enhancing nail flexibility and providing better resolution for claims substantiation. Sensitizing the nails with hydrogen peroxide induced alterations in both DSC and bending fatigue results. Proof-of-principle studies demonstrated an elevation in denaturation temperature and a decrease in the number of cycles to break, indicating a nail-hardening effect when formaldehyde was applied. The use of a nail softener led to an enhancement in nail fatigue resistance due to a notable reduction in nail crosslinking density. The measurement of crosslinking density proved to be a sensitive tool for assessing the effects of cosmetic treatments on nails, particularly in predicting outcomes related to nail brittleness and flexibility.

Preparation, Optimization, and Characterization of Bovine Bone Gelatin/Sodium Carboxymethyl Cellulose Nanoemulsion Containing Thymol.

The aim of this study is to produce a biodegradable food packaging material that reduces environmental pollution and protects food safety. The effects of total solids content, substrate ratio, polyphenol content, and magnetic stirring time on bovine bone gelatin/sodium carboxymethylcellulose nanoemulsion (BBG/SCMC-NE) were investigated using particle size, PDI, turbidity, rheological properties, and zeta potential as evaluation indexes. The micro, structural, antioxidant, encapsulation, and release properties were characterized after deriving its optimal preparation process. The results showed that the nanoemulsion was optimally prepared with a total solids content of 2%, a substrate ratio of 9:1, a polyphenol content of 0.2%, and a magnetic stirring time of 60 min. SEM showed that the nanoemulsion showed a dense and uniform reticulated structure. FTIR and XRD results showed that covalent cross-linking of proteins and polysaccharides altered the structure of gelatin molecular chains to a more compact form but did not change its semi-crystalline structure. DSC showed that the 9:1 BBG/SCMC-NE had a higher thermal denaturation temperature and greater thermal stability, and its DPPH scavenging rate could reach 79.25% and encapsulation rate up to 90.88%, with excellent slow-release performance. The results of the study provide basic guidance for the preparation of stable active food packaging with excellent properties.

The influence of pectinase treatments on the characteristics of pre‐treated and lyophilised sunflower meal‐whey blends

SummaryWhey and sunflower meals are primary by‐products of dairy cheese and vegetable oil production, respectively. Due to their widespread abundance, their valorisation could enable the generation of various value‐added food ingredients or products. In this study, an effort was made to utilise enzymatic pectinolysis along with other pre‐treatments to generate mixtures from whey and sunflower meal (SFM). The increasing presence of SFM increased the critical denaturation temperature of the mixtures and induced less protein structural changes. In addition, the presence of complex carbohydrates in SFM enhanced water and oil holding capacities. In general, pectinase and ultrasonication led to enhanced foaming of the mixtures, although the foams were relatively short‐lived. SFM inclusion limited foaming and emulsification capacities of the blends. In most cases, increasing the ratio of SFM to protein resulted in lower total reducing sugars (TRS), suggesting a more limited enzymatic activity. On the other hand, heating temperature or ultrasonication improved the extent of pectinolysis. Pre‐treatments and pectinolysis improved the functional properties of SFM and whey protein concentrate blends and are promising as an alternative protein source in new product applications.

Comparison of Sucrose and Trehalose for Protein Stabilization Using Differential Scanning Calorimetry.

The disaccharide trehalose is generally acknowledged as a superior stabilizer of proteins and other biomolecules in aqueous environments. Despite many theories aiming to explain this, the stabilization mechanism is still far from being fully understood. This study compares the stabilizing properties of trehalose with those of the structurally similar disaccharide sucrose. The stability has been evaluated for the two proteins, lysozyme and myoglobin, at both low and high temperatures by determining the glass transition temperature, Tg, and the denaturation temperature, Tden. The results show that the sucrose-containing samples exhibit higher Tden than the corresponding trehalose-containing samples, particularly at low water contents. The better stabilizing effect of sucrose at high temperatures may be explained by the fact that sucrose, to a greater extent, binds directly to the protein surface compared to trehalose. Both sugars show Tden elevation with an increasing sugar-to-protein ratio, which allows for a more complete sugar shell around the protein molecules. Finally, no synergistic effects were found by combining trehalose and sucrose. Conclusively, the exact mechanism of protein stabilization may vary with the temperature, as influenced by temperature-dependent interactions between the protein, sugar, and water. This variability can make trehalose to a superior stabilizer under some conditions and sucrose under others.

Preliminarily revealing rheological behaviors of mesoscale collagen fibrils in suspension

Using natural mesoscopic collagen as the structural unit has gradually emerged as a promising processing strategy for the preparation of high-performance collagen materials. These mesoscopic collagen fibrils (CAs) are exfoliated from biological tissues and dispersed in liquid media to prepare subsequent materials. The present work explores the effects of solid content, size, and temperature on the rheological behavior of collagen fibril suspensions under shearing through steady-state and dynamic rheological studies. Suspensions tend to exhibit shear-thinning and gel-like behavior, attributed to mesoscopic collagen forming a rigid network. Suspensions with large-size collagen fibers (aspect ratio > 100) exhibit high resistance to shear deformation at low solid contents (0.5 wt%) due to the intensive physical entanglement. The viscosity of the suspension was temperature-dependent and decreased rapidly near the hydrated thermal denaturation temperature of collagen. This work reveals the interactions between mesoscale collagen's surface interfaces and provides the necessary theoretical basis for collagen processing.

A solution for fillet quality: Slaughter age's effect on protein mechanism and oxidation

Physico-chemical properties of fish flesh are reliable predictors of fillet quality and nutritional value. In our study, the age-related variations of the chemical composition, pH, water activity (aw), water holding capacity (WHC), color and texture analysis, protein thermal stability, myofibrillar fragmentation index (MFI), glycogen content, protein oxidation and protein profiles were investigated in Oncorhynchus mykiss (rainbow trout) fillet. The results revealed that protein denaturation temperatures (Tmax1 and Tmax2) decreased by 2 % and 11.6 % depending on fish age. Tmax1 and Tmax2 values in the same groups were raised 71 % at 11 months' fish and this increase was 58 % at 23 months’ fish. An age-related reduction by 66.6 % and 31.25 % was noticed for protein oxidation markers sulfhydryl groups and disulfide bonds. MFI value increased by 86.6 % connected with age.The characteristics of fish meat quality are complex and are influenced by various factors that affect the degree of freshness of the product and its acceptance in the market. Taking into account the different demands of the consumer, this study has shown that age at slaughter has an impact on final product quality and that the recommended age at slaughter, taking into account market weight, positively affects meat quality.

Exploring the rheological and thermal behavior of cowpea protein concentrate: Impact of pH and concentration

This study confronts challenges from global population growth, focusing on protein supply strains and the environmental impact of traditional animal sources. Delving into unexplored territory, this study investigates the combined effects of pH, concentration, and temperature on the rheological and thermal properties of cowpea protein concentrate (CPC). Steady-state and oscillatory rheological tests, along with differential scanning calorimetric analysis, were conducted to unveil the behavior of CPC solutions. The results revealed sensitivity to protein concentration and shear rate, especially at higher concentrations (>10%), and pH emerged as a critical factor, significantly influencing shear stress and viscosity. The elastic and viscous components of alkaline CPC solutions exhibit weak gel behavior, influenced by both pH and frequency. Temperature-induced changes in viscosity and gelation highlight the interaction between thermal conditions and protein structures. The thermal cycle helps explain changes in molecular interactions induced by temperature, with pH playing a role in influencing gelatinization and denaturation. The denaturation temperature (Td) in the thermograms corresponds to vicilin fractions and emphasizes the prominence of denaturation and gelation at neutral pH, where Td was pH 7 > pH 9 > pH 11. Alkaline pH induced significant structural changes, resulting in a gelation onset temperature below the denaturation onset temperature. This study provides a deeper understanding into the rheological and thermal properties of CPC solutions, emphasizing the roles of concentration, pH, and temperature, useful for various steps of industrial processing, before and after thermal gelation. These findings are important for promoting the use of cowpea proteins in the food industry in response to the evolving needs of a growing global population.

Dynamics and thermal stability of the bypass polymerase, DinB homolog (Dbh).

The DinB homolog polymerase (Dbh) is a member of the Y-family of translesion DNA polymerases that can synthesize using a damaged DNA template. Since Dbh comes from the thermophilic archaeon Sulfolobus acidocaldarius, it is capable of functioning over a wide range of temperatures. Existing X-ray structures were determined at temperatures where the protein is least active. Here we use NMR and circular dichroism to understand how the structure and dynamics of Dbh are affected by temperature (2°C-65°C) and metal ion binding in solution. We measured hydrogen exchange protection factors, temperature coefficients, and chemical shift perturbations with and without magnesium and manganese. We report on regions of the protein that become more dynamic as the temperature is increased toward the functional temperature. Hydrogen exchange protection factors and temperature coefficients reveal that both the thumb and finger domains are very dynamic relative to the palm and little-finger (LF) domains. These trends remain true at high temperature with dynamics increasing as temperatures increase from 35°C to 50°C. Notably, NMR spectra show that the Dbh tertiary structure cold denatures beginning at 25°C and increases in denaturation as the temperature is lowered to 5°C with little change observed by CD. Above 35°C, chemical shift perturbation analysis in the presence and absence of magnesium and manganese reveals three ion binding sites, without DNA bound. In contrast, these bound metals are not apparent in any Dbh crystal structures of the protein without DNA. Two ion binding sites are confirmed to be near the active site, as reported in other Y-family polymerases, and we report a novel ion binding site in the LF domain. Thus, the solution-state structure of the Dbh polymerase is distinct from that of the solid-state structures and shows an unusually high cold denaturation temperature.

Structure, functional and physicochemical properties of lotus seed protein under different pH environments.

The present study investigated the structure, functional and physicochemical properties of lotus seed protein (LSP) under different pH environments. The structures of LSP were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Fourier transform infrared spectroscopy (FTIR), zeta potential, particle size distributions, free sulfhydryl and rheological properties. The functional and physicochemical properties of LSP were characterized by color, foaming property, emulsification property, solubility, oil holding capacity, water holding capacity, differential scanning calorimetry analysis and surface hydrophobicity. LSP was mainly composed of eight subunits (18, 25, 31, 47, 51, 56, 65 and 151 kDa), in which the richest band was 25 kDa. FTIR results showed that LSP had high total contents of α-helix and β-sheet (44.81-46.85%) in acidic environments. Meanwhile, there was more β-structure and random structure in neutral and alkaline environments (pH 7.0 and 9.0). At pH 5.0, LSP had large particle size (1576.98 nm), high emulsion stability index (91.43 min), foaming stability (75.69%) and water holding capacity (2.21 g g-1), but low solubility (35.98%), free sulfhydryl content (1.95 μmol g-1) and surface hydrophobicity (780). DSC analysis showed the denaturation temperatures (82.23 °C) of LSP at pH 5.0 was higher than those (80.10, 80.52 and 71.82 °C) at pH 3.0, 7.0 and 9.0. The analysis of rheological properties showed that LSP gel had high stability and great strength in an alkaline environment. The findings of the present study are anticipated to serve as a valuable reference for the implementation of LSP in the food industry. © 2024 Society of Chemical Industry.

Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures

For irreversible denaturation transitions such as those exhibited by monoclonal antibodies, differential scanning calorimetry provides the denaturation temperature, Tm, the rate of denaturation at Tm, and the activation energy at Tm. These three quantities are essential but not sufficient for an accurate extrapolation of the rate of denaturation to temperatures of 25 °C and below. We have observed that the activation energy is not constant but temperature dependent due to the existence of an activation heat capacity, Cp,a. It is shown in this paper that a model that incorporates Cp,a is able to account for previous observations like, for example, that increasing the Tm does not always improve the stability at low temperatures; that some antibodies exhibit lower stabilities at 5 °C than at 25 °C; or that low temperature stabilities do not follow the rank order derived from Tm values. Most importantly, the activation heat capacity model is able to reproduce time dependent stabilities measured by size exclusion chromatography at low temperatures.

Effects of the extraction conditions on functional and structural characteristics of proteins from fenugreek seeds.

The aim of this study is to optimize the extraction process and characterize the proteins found in fenugreek seeds. The water and oil holding capacities, coagulated protein content, foaming and emulsification properties of the isolated proteins at all extraction conditions were investigated. Also, solubility, molecular weights, structural and thermal properties were determined. In the extraction processes carried out at different pHs (pH 6.0-12.0) and solid:solvent ratios (20-60 g/L), it was determined that the highest extraction yield (94.3±0.3%) was achieved when the pH was 11.47 and the solid-solvent ratio was 34.50 g/L. Three distinct bands (46, 59 and 80 kDa) in the range of 22-175 kDa were determined for the fenugreek seed protein isolate obtained at optimum extraction conditions. Protein secondary structures were achieved using Fourier Transform Infrared (FT-IR) spectra and it was determined that β-sheet structures were highly present. In addition, denaturation temperatures and denaturation enthalpy were calculated as ~119°C and 28 mJ/g, respectively.

Comparison of Structural and Physicochemical Characteristics of Skin Collagen from Chum Salmon (Cold-Water Fish) and Nile Tilapia (Warm-Water Fish).

This study compared collagens from cold-water and warm-water fish for their structural, rheological, and functional properties, and explored their potential applications, aiming to realize the high-value utilization of marine biological resources. To this end, chum salmon skin collagen (CSSC) and Nile tilapia skin collagen (NTSC) were both successfully extracted. Collagens from the two species had different primary and secondary structures, with NTSC having a higher molecular weight, imino acid content, and α-helices and β-turns content. The denaturation temperatures were 12.01 °C for CSSC and 31.31 °C for NTSC. CSSC was dominated by viscous behavior and its structure varied with temperature, while NTSC was dominated by elastic behavior and its structure remained stable with temperature. Both collagens had good oil holding capacity, foaming capacity, and emulsifying activity, but NTSC had better water holding capacity and foaming and emulsifying stability. Their different properties make CSSC more suitable for the preservation of frozen and chilled foods and the production of sparkling beverages, and give NTSC greater potential in biofunctional materials and solid food processing.

Monomeric Far-red and Near-infrared Fluorescent Biliproteins of Ultrahigh Brightness.

Far-red and near-infrared fluorescent proteins have regions of maximum transmission in most tissues and can be widely used as fluorescent biomarkers. We report that fluorescent phycobiliproteins originating from the phycobilisome core subunit ApcF2 can covalently bind biliverdin, named BDFPs. To further improve BDFPs, we conducted a series of studies. Firstly, we mutated K53Q and T144A of BDFPs to increase their effective brightness up to 190 % in vivo. Secondly, by homochromatic tandem fusion of high-brightness BDFPs to achieve monomerization, which increases the effective brightness by up to 180 % in vivo, and can effectively improve the labeling effect. By combining the above two approaches, the brightness of the tandem BDFPs was much improved compared with that of the previously reported fluorescent proteins in a similar spectral range. The tandem BDFPs were expressed stably while maintaining fluorescence in mammalian cells and Caenorhabditis elegans. They were also photostable and resistant to high temperature, low pH, and chemical denaturation. The tandem BDFPs advantages were proved in applications as biomarkers for imaging in super-resolution microscopy.

Effect mechanism of capsaicin and dihydrocapsaicin in chili on the oxidative stability of myoglobin in duck meat.

Myoglobin (Mb) in duck meat is commonly over-oxidized when heated at high temperatures, which may worsen the color of the meat. Enhancing the oxidative stability of Mb is essential for improving the color of duck meat. Capsaicin and dihydrocapsaicin (CA-DI) in chili exhibit antioxidant properties. This study investigated the effects of CA-DI on the structure and oxidative damage of Mb by fluorescence spectroscopy, differential scanning calorimetry analysis and particle size in duck meat during heat treatment. When the ratio of CA-DI to Mb was 10:1 g kg-1 and heat-treated for 36 min, oxymyoglobin significantly increased, and metmyoglobin significantly decreased compared with the control group (P < 0.05). In parallel, the carbonyl content of Mb in the CA-DI group decreased by 43.40 ± 0.10%, the sulfhydryl content increased by 188 ± 0.21%, and the free radical scavenging activity of Mb was significantly enhanced (P < 0.05). Moreover, the addition of CA-DI resulted in a significant decrease in the particle size of the Mb surface (P < 0.05). When the ratio of CA-DI to Mb was 10:1 g kg-1, CA-DI enhanced the thermal stability and significantly increased the thermal denaturation temperature of Mb. The molecular docking results indicated that hydrophobic interactions and hydrogen bonds were involved in the binding of CA-DI to Mb. CA-DI could combine with Mb and improve the oxidation stability of Mb in duck meat. This suggested that CA-DI could be a potential natural antioxidant that improves the color of meat products. © 2024 Society of Chemical Industry.

Vitrification cryopreservation of ligaments based on zwitterionic betaine

Ligament cryopreservation enables a prolonged shelf life of allogeneic ligament grafts, which is fundamentally important to ligament reconstruction. However, conventional cryopreservation techniques fail to eliminate the damage caused by ice crystal growth and the toxicity of cryopreservation agents (CPAs). Here, we report a novel CPA vitrification formulation primarily composed of betaine for ligament cryopreservation. Comprehensive optimization was conducted on the methods for vitrification and rewarming, as well as the loading and unloading conditions, based on the critical cooling rate (CCR), critical warming rate (CWR), and permeation properties of the cryoprotectant. Using biomechanical and histological level tests, we demonstrate the superior performance of our method in ligament cryopreservation. After 30 days of vitrification cryopreservation, parameters such as the Young's modulus, tensile stress, denaturation temperature, and glycosaminoglycans (GAGs) content of the ligament remained essentially unchanged. This work pioneers the application of ice-free cryopreservation for ligament and holds great potential for improving the long-term storage of ligament, providing valuable insights for future technique development.

Activity-stability trade-off observed in variants at position 315 of the GH10 xylanase XynR

XynR is a thermostable alkaline GH10 xylanase, for which we have previously examined the effects of saturation mutagenesis at position 315 on enzyme alkaliphily, and found that at pH 10, the activities of variants could be ordered as follows: T315Q > T315S = T315N > T315H = wild-type XynR (WT) > 15 other variants. In this study, we sought to elucidate the mechanisms underlying the variable activity of these different variants. Crystallographic analysis revealed that the Ca2+ ion near position 315 in WT was absent in the T315Q variant. We accordingly hypothesized that the enhancement of alkaliphily in T315Q, and probably also in the T315H, T315N, and T315S variants, could be ascribed to an activity-stability trade-off associated with a reduction in stability due to the lack of this Ca2+ ion. Consistent with expectations, the alkaline resistance of T315H, T315N, T315Q, and T315S, evaluated through the pH-dependence of stability at 0 mM CaCl2 under alkaline conditions, was found to be lower than that of WT: the residual activity at pH 11 of WT was 78% while those of T315H, T315N, T315Q, and T315S were 0, 9, 0, and 43%, respectively. In addition, the thermostabilities of these four variants, as assessed using the denaturing temperatures (Tm) at 0 mM CaCl2 based on ellipticity at 222 nm in circular dichroism measurements, were lower than that of WT by 2–8 °C. Furthermore, the Tm values of WT and variants at 5 mM CaCl2 were higher than those at 0 mM CaCl2 by 6–11 °C. Collectively, our findings in this study indicate that mutation of the T residue at position 315 of XynR to H, N, Q, and S causes an increase in the alkaliphily of this enzyme, thereby reducing its stability.

Influence of the processing on composition, protein structure and techno-functional properties of mealworm protein concentrates produced by isoelectric precipitation and ultrafiltration/diafiltration

Edible insects represent a great alternative protein source but food neophobia remains the main barrier to consumption. However, the incorporation of insects as protein-rich ingredients, such as protein concentrates, could increase acceptance. In this study, two methods, isoelectric precipitation and ultrafiltration-diafiltration, were applied to produce mealworm protein concentrates, which were compared in terms of composition, protein structure and techno-functional properties. The results showed that the protein content of the isoelectric precipitation concentrate was higher than ultrafiltration-diafiltration (80 versus 72%) but ash (1.91 versus 3.82%) and soluble sugar (1.43 versus 8.22%) contents were lower. Moreover, the protein structure was affected by the processing method, where the ultrafiltration-diafiltration concentrate exhibited a higher surface hydrophobicity (493.5 versus 106.78 a.u) and a lower denaturation temperature (161.32 versus 181.44 °C). Finally, the ultrafiltration-diafiltration concentrate exhibited higher solubility (87 versus 41%) and emulsifying properties at pH 7 compared to the concentrate obtained by isoelectric precipitation.

Effect of pH and biopolymer ratio on phase behavior, rheology, and structural characteristics of pea protein isolate‐locust bean gum coacervates

AbstractBackgroundInteraction between plant‐based proteins and polysaccharides depends on several factors. This work reports the influence of pH and biopolymer ratios on the protein (pea protein isolate, PPI)‐polysaccharide (locust bean gum, LBG) coacervates. Electrostatic interaction and hydrogen bond between the biopolymers strongly influenced the formation of the coacervates.ResultsThe optimum coacervate conditions were observed at pH 4.5 and PPI:LBG ratio of 5:1. The coacervates showed a honeycomb porous architecture having an amorphous nature. Complex coacervates showed a significant elevation of denaturation temperature as compared to biopolymers alone.ConclusionThese results indicates that PPI‐LBG coacervates can be used as an effective biomaterial for encapsulating heat‐sensitive bioactive compounds and other multiple uses in food processing.