Thermal and Rheological Properties of Various Compounds Literature Review

Background[edit | edit source]

A main goal of this literature review is to determine differential scanning calorimetry (DSC) operating parameters (heating rate and range, purge gas flow rate, amount of sample) to analyze the thermal properties of various plant protein sources. The sample materials of interest are pea protein, rice protein, soy protein, yeast, and spirulina. Properties for each sample like denaturation temperature, denaturation enthalpy, and various thermal trends were also noted from the literature for future comparison. Another objective of this literature review is to investigate the viscosity and rheological properties of the various sample materials to eventually compare with experimental data. Plant proteins are increasing in popularity as a more sustainable alternative to animal protein. Thermal and rheological properties of the sample materials can influence food production feasibility and methods.

Search Terms[edit | edit source]

Sample materials: Pea protein, soy protein, rice protein, spirulina, yeast, water

• *Sample material* DSC
• *Sample material* thermal stability
• Differential scanning calorimetry *sample material*
• *Sample material* denaturation temperature
• *Sample material* viscosity
• *Sample material* rheometry
• *Sample material* shear-thinning

Literature[edit | edit source]

Pea, Chickpea and Lentil Protein Isolates: Physiochemical Characterization and Emulsifying Properties[edit | edit source]

Yakoub Ladjal-Ettoumi, Hafid Boudries, Mohamed Chibane and Alberto Romero, "Pea, Chickpea and Lentil Protein Isolates: Physiochemical Characterization and Emulsifying Properties", Food Biophysics, 11(1), 43-51, 2016

Abstract:

The physiochemical and emulsifying properties of pea protein (PP), chickpea protein (CP) and lentil protein (LP) were evaluated. Thermal stability was determined through differential scanning calorimetry. Emulsifying properties were analyzed as a function of pH. All three proteins were observed to have good thermal stability and solubility, despite high levels of denaturation. Emulsion stability was found to improve as the difference between the pH value and the isoelectric point increased. This study concluded that the proteins are strong contenders as food emulsifiers.

Summary:

• Compounds analyzed included fresh matter of 85.7%±0.6% PP, 85.9%±0.2% CP, and 84.8%±0.1% LP.
• The samples used in the DSC were 2 mg of the different proteins mixed with 5 μl deionized water.
• The DSC was conducted using sealed pans heated from 20-120ºC in intervals of 5ºC/min, with a sealed pan acting as a reference.
• A higher denaturation temperature (T_d) was associated with a more compact tertiary structure for the proteins.
• All thermograms derived from the DSC produced an endothermic peak, which represents T_d.
  • CP exhibited a T_d of 87.2ºC, PP 104.6ºC, and LP 106.5ºC
• PP and LP may have higher levels of stability due to stronger presence of legumin than CP.
• PP also exhibited a weaker peak of 83.3ºC, which may be attributed to the presence of vicilin, an amino acid present in peas.
• The solubilities for each protein reached maximums at pH levels of 2 and 8, and a minimum at 4.5
• The determined solubility relationship is that under acidic conditions, the increased net positive charge creates a soluble environment; under alkaline conditions, the increased net negative protein charge dissociates the aggregates, and the solubility increases.

Stability of 3D printing using a mixture of pea protein and alginate: Precision and application of additive layer manufacturing simulation approach for stress distribution[edit | edit source]

Timilehin Martins Oyinloye, Won Byong Yoon, "Stability of 3D printing using a mixture of pea protein and alginate: Precision and application of additive layer manufacturing simulation approach for stress distribution", Journal of Food Engineering, Volume 288, 2021, 110127, ISSN 0260-8774, 2020

Abstract:

Five blends of pea protein and alginate solutions were analyzed in terms of their rheology, textural, and thermal properties to determine an optimum 3D printing material mixture ratio. Obtain values include a storage modulus of 633.32 to 1303.89 Pa at 2ºC/min heating rate, an enthalpy range of 636.20 to 2202.53 J/g, and a hardness range of 73.06 to 159.85 N. The different values increased with a higher pea protein concentration. The optimum ratio was found to be 80:20 alginate to pea protein. This material was used in additive-layer manufacturing (ALM) to further analyze stress values and printing conditions.

Summary:

• Pea protein paste was made from a 20:80 mix of pea powder and distilled water; alginate gel was made form a combination of sodium phosphate, calcium chloride, sodium alginate and distilled water.
• 100% Pea protein paste, 100% alginate gel solution, and mixtures of alginate and pea protein at ratios of 90:10, 80:20, and 70:30 were tested.
• DSC was conducted using 10-15 mg samples of the different pastes weighed and sealed into DSC pans, and an empty sealed pan was used as reference.
• The DSC temperature range was 20-150ºC at a heating rate of 10ºC/min, and was flushed with nitrogen for all runs at a rate of 50 mL/min.
• The endothermic peaks in the DSC thermograms were used to determine the denaturation temperature (T_d) and enthalpy of denaturation (DH) for each sample.
• The 100% pea protein sample had 2 endothermic peaks at 42.44±1.81ºC and 104.7±2.85ºC.
  • The first (weaker) peak was attributed to the proteins molecules unfolding and refolding during heating below the molecule's glass-transition temperature.
  • The 2 different peaks may also be a result of the vicilin and legumin present in the pea protein, as these compounds tend to produce multiple endotherms and denaturation temperatures, due to their heterogeneity.
  • The source of the pea protein sample and treatment history may influence the thermogram results by denaturing the protein through previous high heat treatments, such as spray drying.
• The addition of pea protein to alginate resulted in increased denaturation enthalpy and denaturation temperature.
• Mixtures of alginate and pea protein were observed to be more thermally stable than both pure pea protein and pure alginate.
• Viscosity measurements were obtained using a computer software and shear rate of 0.01-10.00 per seconds.
• All samples were found to be shear-thinning.
• The viscosity should be low enough for extrusion ease, but high enough to hold shape without deformation.

Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study[edit | edit source]

Linyi Zhou, Yong Yang, Haibin Ren, Yan Zhao, Zhongjiang Wang, Fei Wu, Zhigang Xiao, "Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study", Journal of Chemistry, vol. 2016, Article ID 6898715, 8 pages, 2016

Abstract:

Rice bran protein (RBP) was extruded at various temperatures to investigate the validity of Raman spectroscopy in protein confirmation changes detection. DSC analysis determined RBP extrusion at 100ºC increased the denaturation temperature and decreased the denaturation enthalpy. Extrusion at 120ºC resulted in completely denatured RBP. The Raman study displayed an increase in unordered structure, and decrease in α-helix and β-sheet structure of extruded RBP. Microenvironment and polarity changes were indicated through decreased intensity of the band assigned to CH_n bending.

Summary:

• Rice bran extrusion temperatures were 100, 120, 140, and 160ºC.
• The DSC was performed in a temperature range of 25-120ºC at a heating rate of 5ºC/min.
• 60 mg of 8% rice bran protein (RBP) in distilled water was used for samples in the DSC.
• A denaturation temperature (T_d) non-extruded RBP was observed at 79.9ºC and an enthalpy of denaturation value of 1.70 J/g of protein.
• RBP extruded at 100ºC had an increased T_d to 82.3ºC, signifying a higher degree of thermal stability, and decreased enthalpy of 1.54 J/g.
  • This result implies that extrusion of 100ºC promotes partial denaturation of the RBP, in which the partially broken RBP's re-connect to form a more stable compound with a higher T_d.
  • Extrusions above 120ºC resulted in complete denaturation of RBP, signified by the disappearance of an endothermic peak in the DSC results.

Physical and flow properties of rice protein powders[edit | edit source]

L. Amagliani, J. O'Regan, A. L. Kelly, and J. A. O'Mahony, "Physical and flow properties of rice protein powders," Journal of Food Engineering, 190, 1-9, 2016

Abstract:

Three rice protein concentrates (RPC1, RPC2, RPC3), two rice bran protein hydrolysates (RBPH1, RBPH2) and two rice endosperm protein hydrolysates (RPH1, RPH2) were analyzed to determine their physical and flow properties. The properties were then compared to rice bran, rice flour, and various dairy protein powders. Particle size distribution particle shape, and surface characteristics were investigated. Analysis through differential scanning calorimetry (DSC) displayed lower thermal stability for RBPH samples than RPC and RPH samples. All proteins exhibited free-flowing behaviour.

Summary:

• Between the rice protein samples, protein concentrated varied from 32.0 to 78.2%.
• The DSC study was conducted using a Mettler Toledo DSC823e and the accompanying STARe software system.
• 30 mg of each powder sample was measured into the DSC pan, tempered at 5ºC for 5 minutes, and then heated to 100ºC using a 5ºC/min heating rate; A reference pan containing 30 mg calcined aluminum oxide was also measured.
• Across the samples the thermal denaturation temperature ranged from 53±0.55 ºC to 72.8±0.10 ºC.
• Across the samples, the denaturation enthalpy ranged from 0.87±0.03 ΔH to 3.45±0.15 ΔH.
• Rice bran exhibited 2 peaks with the first one potentially corresponding to starch gelatinisation, and the second to protein denaturation.

Microstructure and rheological properties of mixtures of acid-deamidated rice protein and dextran[edit | edit source]

Xianghong Li, Yongle Liu, Cuiping Yi, Yunhui Cheng, Sumei Zhou, Yufei Hua, "Microstructure and rheological properties of mixtures of acid-deamidated rice protein and dextran", Journal of Cereal Science, 51(1), 7-12, 2010

Abstract:

Acid-deamidated rice protein and dextran mixtures were analyzed in terms of rheological properties. Microstructures of the mixtures were investigated using confocal laser scanning microscopy (CLSM) which displayed protein network structures and association among ADRP molecules. Shear measurements performed by a rheometer demonstrated an increase in viscosity of mixtures with protein associations. Textural measurements exhibited differences in microstructure between mixture and single ADRP gel through fracture forces.

Summary:

• Sample was debris rice with a protein content of 7.8%.
• Protein was extracted from the rice flour and prepared into ADRP through suspension, centrifugal, precipitative, and freeze-drying techniques.
• Mixtures were prepared through suspension in distilled water at a concentration of 20% w/w. The suspensions were centrifuged and filtered to remove insoluble particles.
• ADRP-dextran mixtures were stirred in a controlled water bath, hermetically sealed, and placed in another water bath to reach a solid gel-like consistency.
• Viscosity measurement samples had a constant dextran concentration of 3%, and ADRP concentration of 1%, 4.5%, and 6%. Pure dextran and ADRP samples were also tested.
• Rheological measurements were conducted by minimizing interface effects and using a controlled temperature of 25ºC.
• Shear rate range of 10^-2-10² was used for steady shear viscosity measurements.
• All mixtures displayed shear-thinning behaviour (viscosity decreased with increased shear stress).
• Differences in viscosity were observed when the protein concentration increased to 4.5%, at lower protein concentrations the flow profile was similar.
  • Somewhat contradictive, pure ADRP had the lowest viscosity, followed by pure dextran.

Gelation of edible blue-green algae protein isolate (spirulina platensis strain Pacifica): Thermal transitions, rheological properties, and molecular forces involved[edit | edit source]

Ioannis S. Chronakis, "Gelation of edible blue-green algae protein isolate (spirulina platensis strain Pacifica): Thermal transitions, rheological properties, and molecular forces involved," Journal of Agricultural and Food Chemistry, 49(2), 888-898, 2001

Abstract:

Absorption, differential scanning calorimetry (DSC), rheological and viscometry studies were carried out to characterize blue-green algae Spirulina platensis protein isolates. Data collection revolved around thermal unfolding, denaturation, aggregation, and gelation. Thermal transitions were present at multiple temperatures. Viscosity was found to have relation to the dissociation-denaturation process and pH. Good gelling properties were observed. Hydrogen bonds reinforce the spirulina protein and were determined to effect the molecular association, aggregation, and gelation during thermal treatment.

Summary:

• Spirulina protein extracted by dissolution from spray-dried Spirulina platensis Pacifica strain algal powder.
• Seiko DSC 6200 calorimeter with a heating rate of 10ºC/min in a temperature range of 30 to 180ºC was used in the calorimetric measurements.
• 4 mg of the protein isolate powder and 20 mg of a buffer solution at varying pH and concentration were added to aluminum DSC pan and then hermetically sealed.
• For the sample with a 0.1 M Tris-HCl buffer solution pH of 7 the DSC thermogram illustrated a linear trend approximately between 75-80ºC and endothermic peaks at 66.9ºC and 108.7ºC.
• An increase in pH resulted in a decrease in temperature for the first peak, likely due to an increase in protein solubility that promotes dissociation of protein aggregates.
• The viscosity test samples were created by dissolving spirulina protein isolate in 0.01 M sodium phosphate buffer at pH of 5, 7.5, and 9, with 50 mM NaCl.
• A Schott Geräte capillary viscometer immersed in a Haake thermostat bath and connected to a Schott Geräte AVS 440 electronic device were used to determine the flow time and viscosity of the samples.
• 20 mL of the viscosity sample solutions were left for 30 minutes to reach equilibrium and the temperature of the thermostat bath before measurements were taken.
• Results displayed viscosity decreases with a temperature increase; however after 50ºC viscosity increased which may be attributed to thermal denaturation.
• Irreversible denaturation and change in viscosity was demonstrated to occur in temperatures around 60ºC, which was also reflected in the thermal data.

Thermal denaturation of soybean protein at low water contents[edit | edit source]

Naofumi Kitabatake, Mineo Tahara, Etsushiro Doi, "Thermal Denaturation of Soybean Protein at Low Water Contents", Agricultural and Biological Chemistry, 54(9), Issue 9, 2205–2212, 1990

Abstract:

The purpose of this study was to investigate the relationship between thermal denaturation and water content. The DSC thermogram of soybean protein at various water contents primarily exhibited two peaks with different denaturation temperatures because of 11S and 7S globulins. Decreased water concentration resulted in increased denaturation temperatures and only one peak.

Summary:

• Soybean protein isolate and soybean globulins were prepared from defatted soybean flour through centrifugation, suspension and precipitate collection, and neutralization methods.
• The DSC analysis was conducted using a DSC 100 calorimeter and adding 50 µL of a 60 mg/ml soybean protein powder and distilled water to silver pans. A heating rate of 5ºC/min between 25 and 200ºC were used.
• At low water conditions, the soybean protein solution underwent lyophilization and then had more distilled water added. The new substance was left for 24 hours, and then heated to 200ºC and cooled to 25ºC in the calorimeter at a rate of 5ºC/min.
• The 60 mg/mL protein isolate sample produced 2 endothermic peaks at 76.5ºC and 93.3ºC.
• At lower water concentrations (29% and 11%), peaks were not exhibited until past 160ºC.

DSC study on the thermal properties of soybean protein isolates/corn starch mixture[edit | edit source]

Li, S., Wei, Y., Fang, Y. et al, "DSC study on the thermal properties of soybean protein isolates/corn starch mixture" Journal of Thermal Analysis and Calorimetry, 115, 1633–1638, 2014

Abstract:

Soybean protein isolates (SPI) and corn starch (CS) were characterized by their thermal properties to be used in manufacturing. Starch mass fractions from 0 (pure SPI) to 100 (pure CS) at various water contents were investigated. Differential scanning calorimetry was used to determine onset and peak temperatures and enthalpy of starch gelatinization. No chemical reaction occurred between SPI and CS within the heating range. SPI lessened the degree of CS gelatinization; CS lessened the degree of SPI denaturation.

Summary:

• Soybean protein isolates (SPI) and corn starch (CS) mixtures were tested from 0% (no CS) starch to 100% starch (no SPI) at 30%, 50% and 70% water content.
• 8-10 mg of the samples were sealed in aluminum DSC pans.
• DSC used a heating rate of 5 and 10 ºC/min from 20 to 130ºC, and 50 mL/min of dry nitrogen as purge.
• Results demonstrated that a higher SPI concentration resulted in increased onset and peak temperatures.
• 100% SPI at 50% water content had a peak temperature of 106.48±6.62ºC and enthalpy of 3.68±1.03 J/g.
• An increase in water content resulted in a lower peak temperature for SPI.

Rheological properties of soy protein isolate solution for fibers and films[edit | edit source]

Pengchao Liu, Helan Xu, Yi Zhao, Yiqi Yang, "Rheological properties of soy protein isolate solution for fibers and films", Food Hydrocolloids­, 64, 149-156, 2017

Abstract:

The relationship between soy protein isolate (SPI) rheological properties and concentration, temperature, and shear rates were investigated. The SPI sample had high concentration for fibers and films. Viscosity was observed to decrease with increasing temperature. Thixotropic behavior was demonstrated in all solution samples. The trend between viscosity and time was studied under shear rates of 80-160 s^-1, and 18 wt% SPI solution. Various models were used to fit the rheological data, with the Weltman model being the best fit. The rheological properties were analyzed to determine optimum spinning conditions for wet spinning of SPI filament.

Summary:

• Source material was partially denatured SPI with a protein concentration of over 90%.
• The solution was prepared by SPI powder with 8 M urea solution with 1% w/w sodium sulfite on weight of SPI. The mixtures were swelled and stirred to ensure proper dissolution, centrifuged to degas, then hermetically stored at ambient temperature.
• Various SPI concentrations were tested (16%, 18%, 20%, 22%).
• A rotational rheometer was used for rheological analysis.
• Shear rate range was 0-240 s^-1, used to measure shear viscosity.
• Fresh SPI solution was used for each measurement.
• Paraffin oil was spread on exposed surfaces in measurement to prevent dehydration.
• Results demonstrated that viscosity increased with increasing SPI concentration.
  • Concentration of 22% was too viscous to measure and had a gel-like consistency.
  • Protein molecular entanglement is increased with concentration due to intermolecular friction (chain entanglement theory).
  • Protein-protein interactions become more dominant.
• All concentrations exhibit shear-thinning behavior (viscosity decreases with increased shear rate).
  • Characteristic result of pseudo-plastic polymer solutions.
• Solutions with lower concentration demonstrated less shear-thinning behavior.
  • Therefore, shear-thinning relates to molecular entanglement and the slope of shear viscosity versus shear rate (Kopperud & Hansen, 1998)
• Shear stress in shear rate increasing is bigger than in shear rate decreasing.
  • Determined that the SPI solution's shear-thinning behavior is time-dependent (thixotropic).
• Increasing temperature decreased viscosity, which aligns with synthetic polymer solution, implying that the urea/sodium mixture is a fine SPI solvent.
• Instead of forming a gel, the SPI solution is steady from 25ºC-70ºC.

Physicochemical and Spectroscopic Characterization of Yeast Extract Powder After the Biofield Energy Treatment[edit | edit source]

M. K. Trivedi, A. Branton, D. Trivedi, G. Nayak, K. Bairwa, and S. Jana, "Physicochemical and Spectroscopic Characterization of Yeast Extract Powder After the Biofield Energy Treatment," American Journal of LIfe Sciences, Science Publishing Group, 3(6), 387-394, 2015

Abstract:

A control group of yeast extract (YE) powder and a biofield energy treated yeast extract powder were analyzed to study the influence of the treatment. Analysis techniques and studies included X-ray diffractometry, surface area analysis, particle size analysis, differential scanning calorimetry (DSC), TGA/DTG analysis, Fourier transform infrared study, and UV-vis spectroscopy. The DSC analysis displayed a 41.64% increase in melting temperature from the control group for the treated YE powder. The treated sample also presented an increase in thermal degradation onset temperature and maximum thermal degradation temperature, compared to the control.

Summary:

• YE powder was obtained from a labratory, and the biofield energy treatment was performed by the author of the paper - Mahendra Kumar Trivedi.
• The DSC analysis used a Pyris 6 Perkin Elmer DSC.
• A reference aluminum pan and a sample aluminum pan with 50 µL YE powder underwent a heating rate of 10ºC/min with an air flux rate of 5 mL/min.
• The melting temperature for the control sample was 141.91ºC, and 201.11ºC for the treated sample.
• The increase in melting temperature, and therefore thermal stability, for the treated sample may be attribute to enhanced thermal stability, increased particle size, and stronger intermolecular forces due to the biofield treatment.
• Through X-ray diffractometry, the samples were determined to be amorphous.

Solid–liquid transitions in the rheology of a structured yeast extract paste, Marmite™[edit | edit source]

David E. White, Geoff D. Moggridge, D. Ian Wilson, "Solid–liquid transitions in the rheology of a structured yeast extract paste, Marmite™", Journal of Food Engineering, 88(3). 353-363, 2008

Abstract:

The rheology of yeast extract spread Marmite^TM was investigated using steady-state and non-steady-state techniques. The sample appeared to be structured and thixotropic at ambient temperature in the steady-state data. A dependence on stress and strain was observed. More Newtonian behaviour was exhibited at increased temperatures. Shear-thickening behaviour was demonstrated in the non-stead-state data. Potentially due to experimental limits, a true yield stress value was not observed.

Summary:

• Marmite^TM is commercially available and known to have thixotropic properties and be temperature sensitive.
• Lysis of brewer's yeast cells produced Marmite which is protein-rich and has a solid wt% of 70-75.
• At high concentrations, Marmite^TM has been known to demonstrate shear-thinning behaviour and thixotropy (non-Newtonian rheology).
• Substance becomes more Newtonian at lower concentrations and high temperatures.
• Samples used in viscosity testing had no added spices or adjustment for NaCl content, and contained 73.2 wt% solids.
• Rotational rheometer was used.
• Shear rate sweeps of 1 to 300 s^-1 and back were used to obtain apparent viscosity at 25ºC.
• Shear-thinning behavior was observed on the forward run, and Newtonian behavior was observed on the return leg.
  • This rheology transition is indicative of thixotropic behavior, which may be attributed to structures within the compound that break down upon shear and then have a quick recovery time.
• Increasing the temperature of the shear rate sweep experiment resulted in decreased apparent viscosity values.

Studies on the interaction of water with ethylcellulose: effect of polymer particle size[edit | edit source]

Agrawal AM, Manek RV, Kolling WM, Neau SH, "Studies on the interaction of water with ethylcellulose: effect of polymer particle size", AAPS PharmSciTech, 4(4), E60, 2003

Abstract:

The primary goal of this study was to observe the effects of particle size on the interaction of water and ethyl cellulose (EC) samples. Two sizes were investigated: Coarse particle ethyl cellulose (CPEC) and fine particle ethyl cellulose (FPEC). Differential scanning calorimetry (DSC) was used to determine the water distribution within the different sized ethyl cellulose samples. DSC was also used to determine the amount of non-freezing and freezing water in the hydrated samples. For both particle sizes, increased enthalpy of fusion of water was a result of an increase in water content. At low water contents, the different particle sizes did not affect the amount of non-freezing water. Equilibrium of 47% wt/wt water content was achieved within the hydrated sample after exposing the ethyl cellulose to water for 30 minutes.

Summary:

• The CPEC sample had an average particle size of 310 µm; the FPEC sample had an average particle size of 9.7 µm.
• The DSC samples were prepared in the following manner:
  • The ethyl cellulose samples were dried over a 3-day period in an oven at 120ºC.
  • Water and weighed EC measurements were manually mixed for 2 minutes in 3 mL glass vials with a steel spatula.
  • The initial water content of the samples ranged from 20-150 wt/wt of the dry polymer.
  • The wetted samples reached equilibrium in tightly capped vials at room temperature for 10, 30, 60, 90, or 1440 minutes for the equilibrium study and for 24 hours for the water content study.
• DSC method was conducted by weighing and sealing 10 mg of the in an aluminum DSC pan via crimping.
  • Rather than hermetically sealing the pan, crimping was used to prevent pressure buildup and to allow vapour escape during heating.
• DSC samples were chilled to -50ºC at 10ºC/min and hed at that temperature for 5 minutes; to obtain the endotherm temperature, the samples were scanned from 25 to 150ºC at 10ºC/min.
• Nitrogen flow rate of 20 mL/min was used as purge.
• Under the stated conditions, an endothermic peak temperature of approximately 3.85ºC was observed for pure water.
• Decreasing water content for both CPEC and FPEC resulted in lower endothermic peak temperatures, and smaller, less defined peaks.

Citations[edit | edit source]

1. Naofumi Kitabatake, Mineo Tahara, Etsushiro Doi, "Thermal Denaturation of Soybean Protein at Low Water Contents", Agricultural and Biological Chemistry, 54(9), Issue 9, 2205–2212, 1990
2. Ioannis S. Chronakis, "Gelation of edible blue-green algae protein isolate (spirulina platensis strain Pacifica): Thermal transitions, rheological properties, and molecular forces involved," Journal of Agricultural and Food Chemistry, 49(2), 888-898, 2001
3. Agrawal AM, Manek RV, Kolling WM, Neau SH, "Studies on the interaction of water with ethylcellulose: effect of polymer particle size", AAPS PharmSciTech, 4(4), E60, 2003
4. David E. White, Geoff D. Moggridge, D. Ian Wilson, "Solid–liquid transitions in the rheology of a structured yeast extract paste, Marmite™", Journal of Food Engineering, 88(3). 353-363, 2008
5. Xianghong Li, Yongle Liu, Cuiping Yi, Yunhui Cheng, Sumei Zhou, Yufei Hua, "Microstructure and rheological properties of mixtures of acid-deamidated rice protein and dextran", Journal of Cereal Science, 51(1), 7-12, 2010
6. Li, S., Wei, Y., Fang, Y. et al, "DSC study on the thermal properties of soybean protein isolates/corn starch mixture" Journal of Thermal Analysis and Calorimetry, 115, 1633–1638, 2014
7. M. K. Trivedi, A. Branton, D. Trivedi, G. Nayak, K. Bairwa, and S. Jana, "Physicochemical and Spectroscopic Characterization of Yeast Extract Powder After the Biofield Energy Treatment," Science Publishing Group, 3(6), 387-394, 2015
8. L. Amagliani, J. O'Regan, A. L. Kelly, and J. A. O'Mahony, "Physical and flow properties of rice protein powders," Journal of Food Engineering, 190, 1-9, 2016
9. Linyi Zhou, Yong Yang, Haibin Ren, Yan Zhao, Zhongjiang Wang, Fei Wu, Zhigang Xiao, "Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study", Journal of Chemistry, vol. 2016, Article ID 6898715, 8 pages, 2016
10. Yakoub Ladjal-Ettoumi, Hafid Boudries, Mohamed Chibane and Alberto Romero, "Pea, Chickpea and Lentil Protein Isolates: Physiochemical Characterization and Emulsifying Properties", Food Biophysics, 11(1), 43-51, 2016
11. Pengchao Liu, Helan Xu, Yi Zhao, Yiqi Yang, "Rheological properties of soy protein isolate solution for fibers and films", Food Hydrocolloids­, 64, 149-156, 2017
12. Timilehin Martins Oyinloye, Won Byong Yoon, "Stability of 3D printing using a mixture of pea protein and alginate: Precision and application of additive layer manufacturing simulation approach for stress distribution", Journal of Food Engineering, Volume 288, 2021, 110127, ISSN 0260-8774, 2020