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Guanghong Zhou - One of the best experts on this subject based on the ideXlab platform.
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oxidative stability of isoelectric solubilization precipitation isolated pse like chicken protein
Food Chemistry, 2019Co-Authors: Xue Zhao, Tong Xing, Peng Wang, Guanghong ZhouAbstract:Abstract The effects of a hydroxyl radical generating system (Fe3+/H2O2) at different H2O2 concentrations (0, 1 and 10 mM) on the chemical and structural properties of isoelectric solubilization/precipitation (ISP)-isolated PSE (pale, soft, exudative)-like chicken protein were investigated. Both acid and alkaline treatments effectively reduced the pro-oxidant contents in PSE-like Meat systems, such as lipids, pigments and myoglobins. The ISP samples generated less carbonyl derivatives and Schiff base but yielded higher sulfhydryl and free amine loss in response to oxidation. Correspondingly, sulfur-contained amino acids in ISP samples were more easily converted, even at the 1-mM H2O2 concentration, than in the PSE-like Meat Paste. Moreover, the ISP-isolated proteins have possibly maintained their gelling properties after oxidation compared to the PSE-like Meat Paste. In regards to chemical and structural modification, the ISP treated protein showed a different susceptibility to oxidation in vitro.
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use of an isoelectric solubilization precipitation process to modify the functional properties of pse pale soft exudative like chicken Meat protein a mechanistic approach
Food Chemistry, 2018Co-Authors: Xue Zhao, Tong Xing, Yun Bai, Guanghong ZhouAbstract:Abstract The functionality of pale, soft, exudative (PSE)-like chicken protein was improved by isoelectric solubilization/precipitation (ISP) treatment. PSE-like chicken proteins were solubilized at an acidic pH 3.5 or an alkaline pH 11.0, followed by precipitating at pH 5.5 and 6.2. PSE-like Meat Paste was treated as control (CON). Precipitated at pH 6.2 led to a more elastic gel than at pH 5.5. Water distribution of ISP-isolated protein was affected by precipitation pH. More tryptophan residues exposed and –SH was partially oxidized to disulfide bond after ISP treatment, which led to large aggregates formation and higher viscosity of ISP isolated proteins than of CON. Absolute zeta potential of alkali-treated protein was higher than other counterparts, indicating stronger electric repulsion. ISP treatments could convert α-helix structure to relatively irregular structures. Overall, solubilizing at pH 11.0, combined with a precipitation pH 6.2 ISP treatment offers a potential for enhanced functionality of PSE-like chicken protein.
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changes of molecular forces during thermo gelling of protein isolated from pse like chicken breast by various isoelectric solubilization precipitation extraction strategies
Food and Bioprocess Technology, 2017Co-Authors: Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Shaolin Deng, Guanghong ZhouAbstract:Changes in protein intermolecular interactions during thermo-gelling were measured to compare the gelation properties of isoelectric solubilization/precipitation (ISP)-isolated protein extracted (solubilized at 3.5 and 11.0, precipitated at 5.5 and 6.2) from pale, soft, and exudative (PSE)-like chicken breast Meat with raw Meat Paste. The solubility of both in water and salt (0.6 M NaCl) decreased significantly after ISP treatments. Protein profile analysis revealed that precipitation pH showed little influence on protein profile. Under pH 3.5 and pH 11.0 solubility conditions, the recovered protein at pH 6.2 showed significantly higher gel hardness than that at pH 5.5, which can be induced by hydrophobic change. Surface hydrophobicity (SH0) and hydrophobic interactions at 25 °C presented similar results, indicating that the soluble protein at pH 11.0 exhibited a higher value after precipitation at pH 6.2 than that at pH 5.5, and the hydrophobicity of pH 3.5 isolates was higher than that of the pH 11.0 groups. However, the maximum hydrophobicity upon heating was inconsistent with initial tendencies. Given that the hydrophobic residues were exposed sufficiently during the ISP process, the ISP-treated proteins, particularly the samples extracted at pH 3.5, might be less susceptible to heat-induced exposure. The gelation behavior of the ISP-treated proteins had been modified on the basis of the intermolecular bonds during heating. In conclusion, the precipitation condition demonstrated excellent relevance for product development based on functionality.
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precipitation and ultimate ph effect on chemical and gelation properties of protein prepared by isoelectric solubilization precipitation process from pale soft exudative pse like chicken breast Meat
Poultry Science, 2016Co-Authors: Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Guanghong ZhouAbstract:Abstract Pale, soft, exudative (PSE)-like chicken breast is considered deteriorated raw material in the poultry Meat industry that has inferior processing ability. The chemical and gelation properties of PSE-like chicken breast Meat Paste were studied. These Pastes were prepared by the pH adjustment method and protein isolation using the isoelectric solubilization/precipitation (ISP) process from PSE-like chicken Meat. The ISP-isolated samples were solubilized at pH 11.0 and recovered at pH 5.5 and 6.2. The ultimate pH of the ISP-isolated protein and Meat Paste was adjusted to 6.2 and 7.0. The ultimate pH in this article referred to the final pH of the extracted protein and Meat Paste. Higher reactive sulfhydryl content and surface hydrophobicity were found in the precipitation at pH 6.2 than at pH 5.5. However, various ultimate pH values showed no significant influence on the surface hydrophobicity. The hardness of gel, as measured by textural profile analysis, was improved using 6.2 as the precipitation pH compared with pH 5.5. The viscoelastic modulus (G′) of gel Pastes prior to the thermal gelation was higher with ISP treatment. However, lower G′ was seen after thermal gelation compared with the control. Dynamic rheological measurement demonstrated a different gel-forming mechanism for protein precipitated at pH values of 5.5 and 6.2 compared with the Meat Paste. The cooking loss showed that the recovered protein failed to form a gel with good water-retention capacity unless the ultimate pH was adjusted to 7.0. Gels made from protein extracted by the ISP method had higher yellowness and lower redness values, probably due to protein denaturation. Precipitation at pH 6.2 formed a harder gel with lower water-retention ability than that at pH 5.5, and this result was possibly due to higher surface hydrophobicity and S-S bridge formation. Overall, network characteristics of ISP-treated protein gels were strongly dependent on precipitation pH and ultimate pH.
Xue Zhao - One of the best experts on this subject based on the ideXlab platform.
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oxidative stability of isoelectric solubilization precipitation isolated pse like chicken protein
Food Chemistry, 2019Co-Authors: Xue Zhao, Tong Xing, Peng Wang, Guanghong ZhouAbstract:Abstract The effects of a hydroxyl radical generating system (Fe3+/H2O2) at different H2O2 concentrations (0, 1 and 10 mM) on the chemical and structural properties of isoelectric solubilization/precipitation (ISP)-isolated PSE (pale, soft, exudative)-like chicken protein were investigated. Both acid and alkaline treatments effectively reduced the pro-oxidant contents in PSE-like Meat systems, such as lipids, pigments and myoglobins. The ISP samples generated less carbonyl derivatives and Schiff base but yielded higher sulfhydryl and free amine loss in response to oxidation. Correspondingly, sulfur-contained amino acids in ISP samples were more easily converted, even at the 1-mM H2O2 concentration, than in the PSE-like Meat Paste. Moreover, the ISP-isolated proteins have possibly maintained their gelling properties after oxidation compared to the PSE-like Meat Paste. In regards to chemical and structural modification, the ISP treated protein showed a different susceptibility to oxidation in vitro.
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use of an isoelectric solubilization precipitation process to modify the functional properties of pse pale soft exudative like chicken Meat protein a mechanistic approach
Food Chemistry, 2018Co-Authors: Xue Zhao, Tong Xing, Yun Bai, Guanghong ZhouAbstract:Abstract The functionality of pale, soft, exudative (PSE)-like chicken protein was improved by isoelectric solubilization/precipitation (ISP) treatment. PSE-like chicken proteins were solubilized at an acidic pH 3.5 or an alkaline pH 11.0, followed by precipitating at pH 5.5 and 6.2. PSE-like Meat Paste was treated as control (CON). Precipitated at pH 6.2 led to a more elastic gel than at pH 5.5. Water distribution of ISP-isolated protein was affected by precipitation pH. More tryptophan residues exposed and –SH was partially oxidized to disulfide bond after ISP treatment, which led to large aggregates formation and higher viscosity of ISP isolated proteins than of CON. Absolute zeta potential of alkali-treated protein was higher than other counterparts, indicating stronger electric repulsion. ISP treatments could convert α-helix structure to relatively irregular structures. Overall, solubilizing at pH 11.0, combined with a precipitation pH 6.2 ISP treatment offers a potential for enhanced functionality of PSE-like chicken protein.
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changes of molecular forces during thermo gelling of protein isolated from pse like chicken breast by various isoelectric solubilization precipitation extraction strategies
Food and Bioprocess Technology, 2017Co-Authors: Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Shaolin Deng, Guanghong ZhouAbstract:Changes in protein intermolecular interactions during thermo-gelling were measured to compare the gelation properties of isoelectric solubilization/precipitation (ISP)-isolated protein extracted (solubilized at 3.5 and 11.0, precipitated at 5.5 and 6.2) from pale, soft, and exudative (PSE)-like chicken breast Meat with raw Meat Paste. The solubility of both in water and salt (0.6 M NaCl) decreased significantly after ISP treatments. Protein profile analysis revealed that precipitation pH showed little influence on protein profile. Under pH 3.5 and pH 11.0 solubility conditions, the recovered protein at pH 6.2 showed significantly higher gel hardness than that at pH 5.5, which can be induced by hydrophobic change. Surface hydrophobicity (SH0) and hydrophobic interactions at 25 °C presented similar results, indicating that the soluble protein at pH 11.0 exhibited a higher value after precipitation at pH 6.2 than that at pH 5.5, and the hydrophobicity of pH 3.5 isolates was higher than that of the pH 11.0 groups. However, the maximum hydrophobicity upon heating was inconsistent with initial tendencies. Given that the hydrophobic residues were exposed sufficiently during the ISP process, the ISP-treated proteins, particularly the samples extracted at pH 3.5, might be less susceptible to heat-induced exposure. The gelation behavior of the ISP-treated proteins had been modified on the basis of the intermolecular bonds during heating. In conclusion, the precipitation condition demonstrated excellent relevance for product development based on functionality.
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precipitation and ultimate ph effect on chemical and gelation properties of protein prepared by isoelectric solubilization precipitation process from pale soft exudative pse like chicken breast Meat
Poultry Science, 2016Co-Authors: Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Guanghong ZhouAbstract:Abstract Pale, soft, exudative (PSE)-like chicken breast is considered deteriorated raw material in the poultry Meat industry that has inferior processing ability. The chemical and gelation properties of PSE-like chicken breast Meat Paste were studied. These Pastes were prepared by the pH adjustment method and protein isolation using the isoelectric solubilization/precipitation (ISP) process from PSE-like chicken Meat. The ISP-isolated samples were solubilized at pH 11.0 and recovered at pH 5.5 and 6.2. The ultimate pH of the ISP-isolated protein and Meat Paste was adjusted to 6.2 and 7.0. The ultimate pH in this article referred to the final pH of the extracted protein and Meat Paste. Higher reactive sulfhydryl content and surface hydrophobicity were found in the precipitation at pH 6.2 than at pH 5.5. However, various ultimate pH values showed no significant influence on the surface hydrophobicity. The hardness of gel, as measured by textural profile analysis, was improved using 6.2 as the precipitation pH compared with pH 5.5. The viscoelastic modulus (G′) of gel Pastes prior to the thermal gelation was higher with ISP treatment. However, lower G′ was seen after thermal gelation compared with the control. Dynamic rheological measurement demonstrated a different gel-forming mechanism for protein precipitated at pH values of 5.5 and 6.2 compared with the Meat Paste. The cooking loss showed that the recovered protein failed to form a gel with good water-retention capacity unless the ultimate pH was adjusted to 7.0. Gels made from protein extracted by the ISP method had higher yellowness and lower redness values, probably due to protein denaturation. Precipitation at pH 6.2 formed a harder gel with lower water-retention ability than that at pH 5.5, and this result was possibly due to higher surface hydrophobicity and S-S bridge formation. Overall, network characteristics of ISP-treated protein gels were strongly dependent on precipitation pH and ultimate pH.
Shiguo Chen - One of the best experts on this subject based on the ideXlab platform.
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γ pga and mtgase improve the formation of e γ glutamyl lysine cross links within hairtail trichiurus haumela surimi protein
Food Chemistry, 2018Co-Authors: Ying Shao, Chunhong Yuan, Gakushi Ishimura, Wenjuan Liu, Shiguo ChenAbstract:The present study investigated the mechanism of e-(γ-glutamyl) lysine cross-links within hairtail (Trichiurus haumela) surimi protein via γ-polyglutamic acid (γ-PGA) and MTGase. The results indicated that the addition of MTGase and γ-PGA markedly improved the gelation properties of hairtail surimi protein, including its maximum breaking force and deformation, water holding capacity and gel strength. The maximum improvements were achieved by adding 0.5units MTGase/g Meat Paste in combination with 0.06% γ-PGA. SDS-PAGE showed that the band intensity of cross-linked proteins increased, whereas that of myosin heavy chain decreased after treatments. Further scanning electron microscopy (SEM) analysis showed the formation of a denser gel matrix, which was caused by much stronger and more inter- and intra-molecular cross-linking of proteins, via MTGase catalysing e-(γ-glutamyl) lysine cross-links formed between lysine residues in the gel protein and glutamic residues in the hydrolytic γ-PGA. The results provide reliable guidance for the improvement of hairtail surimi protein gelation properties.
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enhancement of the gelation properties of hairtail trichiurus haumela muscle protein with curdlan and transglutaminase
Food Chemistry, 2015Co-Authors: Yaqin Hu, Chunhong Yuan, Katsuji Morioka, Shiguo Chen, Xingqian YeAbstract:Abstract The effects of curdlan in combination with microbial transglutaminase on the gelling properties of hairtail muscle protein were investigated. When curdlan of 4 g/100 g Paste was combined with transglutaminase at a concentration of 0.4 units/g Meat Paste, the gel strength, water holding capacity and the whiteness of the heated gel were improved. Textural profiles, such as hardness, springiness, cohesiveness, guminess and chewiness, reached their peaks as well. The increased band intensity of cross-linked proteins, accompanied by weakened myosin heavy chain, was observed from the SDS–PAGE pattern, indicating that curdlan might activate the formation of more e-(γ-glutamyl) lysine cross-links induced by transglutaminase, especially at the level of 0.4 units/g Paste, leading to a denser gel matrix.
Shugo Watabe - One of the best experts on this subject based on the ideXlab platform.
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rheological properties of selected fish Paste at selected temperature pertaining to shaping of surimi based products
Journal of Food Engineering, 2007Co-Authors: Hideto Fukushima, Emiko Okazaki, Yutaka Fukuda, Shugo WatabeAbstract:Abstract The rheological properties of fish Meat Pastes were investigated by dynamic rheological measurement in a range of 5–30 °C, in order to establish the optimum temperatures for shaping. Storage moduli (G′) on temperature sweep analysis for walleye pollack, white croaker and threadfin bream Meat Pastes were considerably higher than loss moduli (G″) and showed maximum at 20, 27 and 28 °C, respectively. Frequency sweep analysis and SDS–PAGE revealed that all Meat Pastes hardly formed suwari gels upon heating until 30 °C. The maximal degrees of recovered G′ were observed at 20 and 30 °C for walleye pollack and threadfin bream Meat Pastes by interval thixotropy analysis, respectively. On the other hand, the G′ recovery of white croaker Meat Paste was almost constant in a range of 5–25 °C, but markedly decreased at 30 °C. These results suggest that the rheological properties of walleye pollack, white croaker and threadfin bream Meat Pastes are species-specific and their optimum temperatures for shaping are at 20 °C, below 25 °C and at 28 °C, respectively.
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quantitative estimation of dark muscle content in the mackerel Meat Paste and its products using antisera against myosin light chains
Journal of Food Science, 2001Co-Authors: Yoshihiro Ochiai, L Ochiai, Kanehisa Hashimoto, Shugo WatabeAbstract:Based on the high level of extractability of myosin subunits (light chains), even after prolonged heat treatment of muscle, a new method to evaluate the dark muscle content in the fish Meat and products of mackerel is proposed. Tissue-specific rabbit antisera with myosin light chains (Al from ordinary muscle and D1 from dark muscle) from mackerel Scomber japonicus were obtained. Mackerel Meat Paste (surimi) was dissolved in 8 M urea containing 1% SDS, and diffused on agar plates containing antiserum against A1 or Dl by single radial immunodiffusion (SRID). The results obtained showed that the area of halos formed in the plates was quite proportional to the content of dark muscle. Basee sur l'importante extractabilite de sous-unites de myosine (chaines legeres), une nouvelle methode immunochimique pour evaluer la teneur en muscle rouge dans le surimi et le kamaboko de maquereau (Scomber japonicus) est proposee. Le gel de maquereau est dissous dans une solution d'uree et de SDS, et diffuse, par immunodiffusion radiale simple, sur des boites de gelose contenant des antisera specifiques aux chaines legeres de myosine de muscle ordinaire ou de muscle rouge. Les surfaces des halos formes sont proportionnelles aux teneurs en muscle rouge.
Tong Xing - One of the best experts on this subject based on the ideXlab platform.
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oxidative stability of isoelectric solubilization precipitation isolated pse like chicken protein
Food Chemistry, 2019Co-Authors: Xue Zhao, Tong Xing, Peng Wang, Guanghong ZhouAbstract:Abstract The effects of a hydroxyl radical generating system (Fe3+/H2O2) at different H2O2 concentrations (0, 1 and 10 mM) on the chemical and structural properties of isoelectric solubilization/precipitation (ISP)-isolated PSE (pale, soft, exudative)-like chicken protein were investigated. Both acid and alkaline treatments effectively reduced the pro-oxidant contents in PSE-like Meat systems, such as lipids, pigments and myoglobins. The ISP samples generated less carbonyl derivatives and Schiff base but yielded higher sulfhydryl and free amine loss in response to oxidation. Correspondingly, sulfur-contained amino acids in ISP samples were more easily converted, even at the 1-mM H2O2 concentration, than in the PSE-like Meat Paste. Moreover, the ISP-isolated proteins have possibly maintained their gelling properties after oxidation compared to the PSE-like Meat Paste. In regards to chemical and structural modification, the ISP treated protein showed a different susceptibility to oxidation in vitro.
-
use of an isoelectric solubilization precipitation process to modify the functional properties of pse pale soft exudative like chicken Meat protein a mechanistic approach
Food Chemistry, 2018Co-Authors: Xue Zhao, Tong Xing, Yun Bai, Guanghong ZhouAbstract:Abstract The functionality of pale, soft, exudative (PSE)-like chicken protein was improved by isoelectric solubilization/precipitation (ISP) treatment. PSE-like chicken proteins were solubilized at an acidic pH 3.5 or an alkaline pH 11.0, followed by precipitating at pH 5.5 and 6.2. PSE-like Meat Paste was treated as control (CON). Precipitated at pH 6.2 led to a more elastic gel than at pH 5.5. Water distribution of ISP-isolated protein was affected by precipitation pH. More tryptophan residues exposed and –SH was partially oxidized to disulfide bond after ISP treatment, which led to large aggregates formation and higher viscosity of ISP isolated proteins than of CON. Absolute zeta potential of alkali-treated protein was higher than other counterparts, indicating stronger electric repulsion. ISP treatments could convert α-helix structure to relatively irregular structures. Overall, solubilizing at pH 11.0, combined with a precipitation pH 6.2 ISP treatment offers a potential for enhanced functionality of PSE-like chicken protein.
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changes of molecular forces during thermo gelling of protein isolated from pse like chicken breast by various isoelectric solubilization precipitation extraction strategies
Food and Bioprocess Technology, 2017Co-Authors: Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Shaolin Deng, Guanghong ZhouAbstract:Changes in protein intermolecular interactions during thermo-gelling were measured to compare the gelation properties of isoelectric solubilization/precipitation (ISP)-isolated protein extracted (solubilized at 3.5 and 11.0, precipitated at 5.5 and 6.2) from pale, soft, and exudative (PSE)-like chicken breast Meat with raw Meat Paste. The solubility of both in water and salt (0.6 M NaCl) decreased significantly after ISP treatments. Protein profile analysis revealed that precipitation pH showed little influence on protein profile. Under pH 3.5 and pH 11.0 solubility conditions, the recovered protein at pH 6.2 showed significantly higher gel hardness than that at pH 5.5, which can be induced by hydrophobic change. Surface hydrophobicity (SH0) and hydrophobic interactions at 25 °C presented similar results, indicating that the soluble protein at pH 11.0 exhibited a higher value after precipitation at pH 6.2 than that at pH 5.5, and the hydrophobicity of pH 3.5 isolates was higher than that of the pH 11.0 groups. However, the maximum hydrophobicity upon heating was inconsistent with initial tendencies. Given that the hydrophobic residues were exposed sufficiently during the ISP process, the ISP-treated proteins, particularly the samples extracted at pH 3.5, might be less susceptible to heat-induced exposure. The gelation behavior of the ISP-treated proteins had been modified on the basis of the intermolecular bonds during heating. In conclusion, the precipitation condition demonstrated excellent relevance for product development based on functionality.
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precipitation and ultimate ph effect on chemical and gelation properties of protein prepared by isoelectric solubilization precipitation process from pale soft exudative pse like chicken breast Meat
Poultry Science, 2016Co-Authors: Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Guanghong ZhouAbstract:Abstract Pale, soft, exudative (PSE)-like chicken breast is considered deteriorated raw material in the poultry Meat industry that has inferior processing ability. The chemical and gelation properties of PSE-like chicken breast Meat Paste were studied. These Pastes were prepared by the pH adjustment method and protein isolation using the isoelectric solubilization/precipitation (ISP) process from PSE-like chicken Meat. The ISP-isolated samples were solubilized at pH 11.0 and recovered at pH 5.5 and 6.2. The ultimate pH of the ISP-isolated protein and Meat Paste was adjusted to 6.2 and 7.0. The ultimate pH in this article referred to the final pH of the extracted protein and Meat Paste. Higher reactive sulfhydryl content and surface hydrophobicity were found in the precipitation at pH 6.2 than at pH 5.5. However, various ultimate pH values showed no significant influence on the surface hydrophobicity. The hardness of gel, as measured by textural profile analysis, was improved using 6.2 as the precipitation pH compared with pH 5.5. The viscoelastic modulus (G′) of gel Pastes prior to the thermal gelation was higher with ISP treatment. However, lower G′ was seen after thermal gelation compared with the control. Dynamic rheological measurement demonstrated a different gel-forming mechanism for protein precipitated at pH values of 5.5 and 6.2 compared with the Meat Paste. The cooking loss showed that the recovered protein failed to form a gel with good water-retention capacity unless the ultimate pH was adjusted to 7.0. Gels made from protein extracted by the ISP method had higher yellowness and lower redness values, probably due to protein denaturation. Precipitation at pH 6.2 formed a harder gel with lower water-retention ability than that at pH 5.5, and this result was possibly due to higher surface hydrophobicity and S-S bridge formation. Overall, network characteristics of ISP-treated protein gels were strongly dependent on precipitation pH and ultimate pH.