Call number: LD2668 .T4 1986 A53 / Master of Science / Chemical Engineering

Call number: LD2668 .T4 1985 Y67 / Master of Science

No description available.

The objective of this study was to improve canola protein gelation properties with the use of enzymes. Both cross-linking and limited proteolysis were explored. Enzyme treatments were performed prior to heat induced gelation. A texture analyzer, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and scanning electron microscopy were used to characterize the resulting networks. Enzymatic cross-linking with transglutaminase was shown to improve the gelation of canola protein isolate (CPI). To the contrary, proteolysis with trypsin, ficin and bromelin, did not enhance the gelation properties of CPI. / October 2006

The experiments performed for this research were completed to produce solid cerium oxide microspheres by an internal gelation sol-gel process. The motivation for this work was to develop a process that would enable the fabrication of a storage or transmutation form for the plutonium and transuranics (TRU) from the Uranium Extraction Plus (UREX ) used fuel reprocessing process. This process is being investigated by the Department of Energy (DOE) and the Advanced Fuel Cycles Initiative (AFCI) through the Nuclear Energy Research Initiative. The internal gelation production of cerium oxide involves the combination of hexamethylenetetramine (HMTA), urea, and cerium nitrate solutions at ~100oC. Microspheres were produced by injection of a broth solution into a flowing stream of hot silicone oil. The captured microspheres were aged, washed, and then underwent Thermogravimetric Analysis (TGA), Differential Scanning Calorimetry (DSC), and XRay Diffraction (XRD) analysis. The process variables examined in this study include the concentrations of HMTA, urea and cerium nitrate, the process temperature, the postgelation aging time, and the product washing conditions. Over a series of 70 experiments, it was determined that a broth solution containing a mixture of 1.45 M cerium nitrate and 1.65 M HMTA and urea (1:1 ratio) solutions produced the best cerium oxide microspheres. The spheres were aged for 30 to 60 minutes and then washed in hexane to remove the silicone oil and a subsequent series of ammonium hydroxide washes to remove unreacted product and to fully gel the microspheres. Through DSC analysis it was determined that excess wash or unreacted product may be removed by an exothermic reaction at approximately 200oC. The XRD analysis of unheated spheres showed the presence of cerium oxide with additional cerium-bearing organics. Following heating, the microspheres were completely converted to cerium oxide.

The current study attempts to improve the texture properties of a fermented product containing soymilk and milk. Preferred Attribute Elicitation (PAE) was examined as a novel sensory methodology for extracting important attributes influencing consumer liking. This method was applied on commercial yogurt products, and it was determined that texture was important to consumer acceptance, and that texture attributes such as graininess and runny texture were detrimental to consumer liking. Outcomes of the PAE method were compared to those obtained from a conventional trained panel method. It was determined that the PAE method was able to characterize the product textures in a meaningful way, resulting in a product map that closely resembled that obtained by the trained panel method. A mixed protein network was then generated, and simultaneous gelation of both soy and dairy proteins lead to an improved gel structure as compared to gelation of either soy or dairy proteins alone in the mixed system. In addition, it was determined that the presence of homogenized fat globules in the network resulted in fermented products with increased mouthcoating and thickness, particularly when cream was homogenized with dairy milk, with or without soymilk in the mix. It was noted that the order of homogenization (cream with either soymilk, milk alone or with the mix) affected the size and number of aggregates as well as number of interconnecting strands. Additionally, aggregation of milk proteins before soy proteins generated gels with higher slipperiness and fattiness perceptions than gels made from simultaneous milk and soy protein aggregation. This study suggested that it is possible to generate desirable texture properties from a mixture of soy protein and milk proteins, and that it is of fundamental importance to fine tune the structure within the matrix to obtain optimal texture perception. / NSERC, Soybean Utilization Fund

Variable-temperature Fourier transform infrared (VT-FTIR) and circular dichroism (far-UV CD) spectroscopy were employed to investigate the sequence of structural changes responsible for the thermally induced formation of myosin gels with various rheological properties, as measured by dynamic oscillatory rheology, as well as the effects of prior high-pressure processing (HPP) on thermally induced gel formation. The viscoelastic properties of the protein gels were monitored as a function of temperature and were also measured at three fixed temperatures (44, 48, and 68°C). Examination was done of changes in the secondary structure-sensitive amide l'band in the FTIR spectra of the protein in D2O buffer (0.6M KCl, pH 6.4) as a function of temperature, as well as far-UV CD spectra. Myosin solutions were exposed to increasing hydrostatic pressure (100--400 MPa for 10 min at 16°C). The extent of unfolding of the tail was shown to be proportional to the pressure treatment, suggesting that the slight increase of gel strength may partly originate from the facilitated tail-tail interaction. (Abstract shortened by UMI.)

Canola protein isolate (CPI) has tremendous potential as a protein alternative to soy within the global protein ingredient market. The overall goal of this thesis was to compare and contrast the gelling mechanism of CPI with a commercial soy protein isolate (SPI) ingredient. Specifically, the gelation properties of CPI and SPI were evaluated as a function of protein concentration (5.0–9.0%), destabilizing agent [0.1 – 5.0 M urea; 0.1 and 1.0% 2-mercaptoethanol], ionic strength (0.1, 0.5 M NaCl) and pH (3.0, 5.0, 7.0, 9.0). The fractal properties of CPI were evaluated as a function of protein concentration (5.0 – 9.0%) and pH (3.0, 5.0, 7.0, 9.0). In the first study, the gelling properties of CPI and SPI as a function of concentration were evaluated, along with the nature of the interactions within their respective gel networks. Overall, the magnitude of the storage modulus (G') of the gel was found to increase with increasing concentration at pH 7.0, whereas the gelling temperature (Tgel) remained constant at ~88ºC. As the NaCl level was increased from 0.1 to 0.5 M, the zeta potential was found to be reduced from ~-20 to -4 mV, but with little effect on Tgel or network strength. In the presence of 2-mercaptoethanol, networks became weaker, indicating the importance of disulfide bridging within the CPI network. Disulfide bridging, electrostatics and hydrogen bonding are all thought to have a role in CPI gelation. In the case of SPI, the magnitude of the storage modulus (G') and Tgel were found to increase and decrease (~80ºC to 73ºC), respectively, with increasing urea concentration at pH 7.0. Increases in NaCl from 0.1 to 0.5 M reduced the zeta potential from ~-44 to -13 mV and caused a shift in Tgel from ~84ºC to 67ºC, and increased G'. No gels were formed in the presence of 2-mercaptoethanol. In the second study, the effect of pH on the gelling properties of CPI and SPI was evaluated. Surface charge (i.e., zeta potential) measurements as a function of pH found CPI to be positively (+18.6 mV), neutral and negatively (-32 mV) charged at pH 3.0, ~5.6 and 9.0, respectively. On the other hand, SPI was observed to be positively (+35.4 mV), neutral and negatively (-51 mV) charged at pH 3.0, 5.0 and 9.0, respectively. An increases in NaCl concentration from 0 M to 0.1 M resulted in a reduction in surface charge at all pHs for both CPI and SPI. Differential scanning calorimetry was performed to determine the thermal properties of CPI. The gelation temperature was found to be above the onset temperature for denaturation. For CPI, the onset of denaturation was found to occur at ~68ºC and then increased to ~78-79ºC at pH 7.0-9.0. With respect to rheological properties, SPI did not gel at pH 9.0, and G' declined as pH increased from 3.0 to 7.0. CPI did not gel at pH 3.0, however the network formed at pH 5.0 became stronger (higher G') as pH increased. The SPI gelling temperature at pH 3.0, 5.0 and 7.0 was observed to be ~85.6, ~46 and ~81ºC, respectively. SPI gels formed at pH 5.0 earlier due to increased protein aggregation near its isoelectric point (pI). The gelation temperature for CPI at pH 5.0 and 7.0 were similar (~88ºC), then declined at pH 9.0 (~82ºC). Network structure of CPI as a function of pH also was investigated using confocal scanning light microscopy (CSLM). As the pH became more alkaline from pH 7.0 to pH 9.0, there was a decrease in lacunarity (~0.41->~0.25). However, the fractal dimension was found to increase (from ~1.54 to ~1.82) showing that increasing the pH resulted in a more compacted CPI network. In summary, protein-protein aggregation induced either by increasing concentration or changing the pH resulted in network formation for both CPI and SPI, where both networks were thought to be stabilized by disulfide bridging and hydrogen bonding. SPI underwent protein aggregation earlier than CPI near its pI value, whereas CPI gels formed the strongest networks away from its pI under alkaline conditions. In all cases, CPI grew in diffusion-limited cluster-cluster aggregation to from the gel network.

The objective of this study was to improve canola protein gelation properties with the use of enzymes. Both cross-linking and limited proteolysis were explored. Enzyme treatments were performed prior to heat induced gelation. A texture analyzer, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and scanning electron microscopy were used to characterize the resulting networks. Enzymatic cross-linking with transglutaminase was shown to improve the gelation of canola protein isolate (CPI). To the contrary, proteolysis with trypsin, ficin and bromelin, did not enhance the gelation properties of CPI.

No description available.