Protein Aggregate

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Ijaz Ahmad - One of the best experts on this subject based on the ideXlab platform.

Chuanhe Tang - One of the best experts on this subject based on the ideXlab platform.

  • the influence of ionic strength on the characteristics of heat induced soy Protein Aggregate nanoparticles and the freeze thaw stability of the resultant pickering emulsions
    Food & Function, 2017
    Co-Authors: Xuefeng Zhu, Jie Zheng, Fu Liu, Chaoying Qiu, Weifeng Lin, Chuanhe Tang
    Abstract:

    The improvement of the freeze–thaw stability of emulsions by interfacial engineering has attracted increasing attention in recent years. The present work investigated the potential of using soy Protein isolate (SPI) Aggregate nanoparticles as the Pickering stabilizers to improve the freeze–thaw stability of the resultant emulsions. SPI nanoparticles with different particle sizes and surface properties were fabricated through heating the SPI solutions (at a constant Protein concentration of 2%, w/v) at 95 °C for 15 min, by varying the ionic strength (I) in the range of 0–500 mM. The nanoparticles fabricated at I values of 100–500 mM exhibited larger particle sizes and higher surface hydrophobicity, but poorer emulsification efficiency than those at I = 0.05 mM. The presence of NaCl during the nanoparticle fabrication resulted in the formation of a kind of gel-like emulsion with a high extent of droplet flocculation. The emulsion stabilized by SPI nanoparticles at I = 0.05 mM was highly susceptible to coalescence, flocculation and creaming upon freeze–thaw treatment, while those in the presence of NaCl exhibited excellent freeze–thaw stability. The much better freeze–thaw stability of the emulsions in the presence of NaCl (relative to that at I = 0.05 mM) was largely attributed to the gel-like network formation, rather than the salt itself. The results indicated that a kind of Pickering emulsion with excellent freeze–thaw stability, stabilized by heat-induced SPI nanoparticles, could be fabricated by heating the SPI solutions at I values of 100–500 mM. The findings would be of great relevance for providing important information about the development of food grade Pickering emulsions stabilized by Protein-based particles, with potential applications in frozen food, or functional food formulations.

  • preparation of soluble soybean Protein Aggregates sspa from insoluble soybean Protein concentrates spc and its functional properties
    Food Research International, 2008
    Co-Authors: Hengguang Zheng, Xiaoquan Yang, Chuanhe Tang, Lin Li, Ijaz Ahmad
    Abstract:

    Abstract Soluble soybean Protein Aggregate (SSPA) was efficiently prepared from alcohol-washed insoluble soybean Protein concentrate (SPC) by the method of hydrothermal cooking (HTC) with high pressure homogenization and evaluated by differential scanning calorimetry (DSC), SDS-PAGE, gel filtration chromatography and texture analyzer. The conditions of low ionic strength and low concentration of Protein (

  • Preparation of soluble soybean Protein Aggregates (SSPA) from insoluble soybean Protein concentrates (SPC) and its functional properties
    Food Research International, 2008
    Co-Authors: Hengguang Zheng, Xiaoquan Yang, Chuanhe Tang, Ijaz Ahmad
    Abstract:

    Abstract Soluble soybean Protein Aggregate (SSPA) was efficiently prepared from alcohol-washed insoluble soybean Protein concentrate (SPC) by the method of hydrothermal cooking (HTC) with high pressure homogenization and evaluated by differential scanning calorimetry (DSC), SDS-PAGE, gel filtration chromatography and texture analyzer. The conditions of low ionic strength and low concentration of Protein (

Hengguang Zheng - One of the best experts on this subject based on the ideXlab platform.

Yufei Hua - One of the best experts on this subject based on the ideXlab platform.

  • heat induced inactivation mechanisms of kunitz trypsin inhibitor and bowman birk inhibitor in soymilk processing
    Food Chemistry, 2014
    Co-Authors: Yeming Chen, Caimeng Zhang, Xiangzhen Kong, Yufei Hua
    Abstract:

    Trypsin inhibitor activity (TIA) is an important antinutritional factor in soymilk. In this study, the effects of NaCl preaddition on TIA and the heat-induced TIA inactivation mechanisms were examined. The results showed that Kunitz trypsin inhibitor (KTI) and Bowman-Birk inhibitor (BBI) contributed 74% and 26% to raw soymilk TIA, respectively. The heat-induced quick KTI incorporation into Protein Aggregates was the reason for its quick TIA inactivation. The heat-induced slow cleavage of one BBI peptide bond was the reason for its slow TIA inactivation. Heat-induced Protein Aggregate formation had little effect on BBI inactivation owing to the fact that BBI and its degradation product tended to remain in the supernatant (197,000g, 1h) in all conditions used in this study. NaCl could accelerate the KTI incorporation into Protein Aggregates and the cleavage of one BBI peptide bond, which supplied a simple and quick method for low TIA soymilk processing.

  • the heat induced Protein Aggregate correlated with trypsin inhibitor inactivation in soymilk processing
    Journal of Agricultural and Food Chemistry, 2012
    Co-Authors: Yeming Chen, Caimeng Zhang, Xiangzhen Kong, Yufei Hua
    Abstract:

    Kunitz trypsin inhibitor (KTI) and Bowman–Birk inhibitor (BBI) have trypsin inhibitor activities (TIA), which could cause pancreatic disease if at a high level. It is not clear why some KTI and BBI lose TIA and some does not in the soymilk processing. This would be examined in this study. TIA assay showed residual TIA was decreased with elevated temperature and TIA was decreased quickly in the beginning and then slowly in boiling water bath. Interestingly, ultracentrifugation showed low residual TIA soymilk had more precipitate than high residual TIA soymilk and soymilk TIA loss had a high correlation coefficient (R2 > 0.9) with precipitate amount. In addition, the TIAs of floating, supernatant, and precipitate obtained by ultracentrifugation were assayed and >80% residual TIA was concentrated in the supernatant. Tricine-SDS-PAGE showed KTI in supernatant was mainly a noncovalent bound form which might exist as itself and/or incorporated into a small Protein Aggregate, while KTI in precipitate was incorpo...

  • effect of ionic strength on the heat induced soy Protein aggregation and the phase separation of soy Protein Aggregate dextran mixtures
    Food Hydrocolloids, 2009
    Co-Authors: Yunhui Cheng, Yufei Hua, Cheng Yang, Steve W Cui
    Abstract:

    Abstract The effects of ionic strength on heat-induced aggregation of soy Protein and phase separation of different soy Protein Aggregates with dextran were investigated. The increase of ionic strength accelerated Protein aggregation as shown by an increase in turbidity, Aggregate fraction and particle size of salt-induced Aggregates (SA). Adding salt (NaCl) to the Aggregates formed at the ionic strength of zero (non-salt Aggregates, non-SA), the increase of Aggregate size was also found. Zeta potential results evidenced the charge screening effects of NaCl. The results of phase diagrams indicated that the compatibility of mixtures at higher ionic strength was lower than those at lower ionic strength, and SA was more incompatible with dextran than non-SA. The effects of the increase of Aggregate size on the phase separation outweighed the ionic strength, which indicated that the depletion interaction also played an important role in the phase separation of soy Protein Aggregates and dextran. CLSM (Confocal Laser Scanning Microscopy) and rheological observations provided additional information of the microstructures of the mixtures.

Xiaoquan Yang - One of the best experts on this subject based on the ideXlab platform.

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