Effect of pH and Salt Concentration on Protein Solubility of Slaughtered and Non-Slaughtered Broiler Chicken Meat

Nahar, M.K.; Zakaria, Zaki Yamani; Hashim, U.; Bari, F. M. Shah NomanUl

doi:10.17576/jsm-2017-4605-06

Cited by 26 publications

(14 citation statements)

References 16 publications

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“…Similar results for protein solubility have been reported for sweet potato and chicken meat proteins [ 20 , 21 ].…”

Section: Resultssupporting

confidence: 86%

“…Further, the API showed significantly higher ( p < 0.05) solubility at pH 9 both in the presence of NaCl and CaCl 2 , followed by pH 7 and pH 3. The higher solubility of API in the presence of ionic salts at pH 9 and 7 is probably because the protein-positive and negative net charged molecules interact more with water, while at pH 3 there might be lower electrostatic forces which render most of the protein water interactions [ 20 ]. It is obvious that proteins show higher solubility above their isoelectric point in distilled water, where intermolecular repulsion enhances solubility by negative and positive charges.…”

Section: Resultsmentioning

confidence: 99%

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Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

et al. 2022

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This study was designed to evaluate the emulsifying and rheological properties of acorn protein isolate (API) in different pH mediums (pH 3, 7 and 9) and in the presence of ionic salts (1 M NaCl and 1 M CaCl2). API shows higher solubility in distilled water at pH 7, while at the same pH, a decrease in solubility was observed for API in the presence of CaCl2 (61.30%). A lower emulsifying activity index (EAI), lower stability index (ESI), larger droplet sizes and slight flocculation were observed for API in the presence of salts at different pHs. Importantly, CaCl2 treated samples showed relevantly higher EAI (252.67 m2/g) and ESI (152.67 min) values at all pH as compared to NaCl (221.76 m2/g), (111.82 min), respectively. A significant increase in interfacial protein concentration (4.61 mg/m2) was observed for emulsion at pH 9 with CaCl2, while the major fractions of API were observed in an interfacial layer after SDS-PAGE analysis. All of the emulsion shows shear thinning behavior (τc > 0 and n < 1), while the highest viscosity was observed for emulsion prepared with CaCl2 at pH 3 (11.03 ± 1.62). In conclusion, API, in the presence of ionic salts at acidic, neutral and basic pH, can produce natural emulsions, which could be substitutes for synthetic surfactants for such formulations.

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“…Similar results for protein solubility have been reported for sweet potato and chicken meat proteins [ 20 , 21 ].…”

Section: Resultssupporting

confidence: 86%

Section: Resultsmentioning

confidence: 99%

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

et al. 2022

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“…Gelation of proteins depends mainly on the electrostatic charge of molecules (Sun & Holley, 2011). At alkaline pH, the protein-water interactions increased, whereas protein-protein in-teractions decreased due to the presence of negative charge on protein surface, thereby enhancing electrostatic repulsion (Nahar, Zakaria, Hashim, & Bari, 2017;Zhu, Li, Li, Ning, & Zhou, 2019). Lys and Arg could augment the pH of mince paste to be higher than pI of myofibrillar proteins.…”

Section: Resultsmentioning

confidence: 99%

Effects of lysine and arginine on the properties of low‐salt mince gel from striped catfish (Pangasianodon hypophthalmus)

Buamard

Javith

Balange

et al. 2020

Journal of Food Science

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Effects of basic amino acids, lysine (Lys) and arginine (Arg), at different levels (0%, 0.5%, and 1%, based on mince weight) on properties of striped catfish (Pangasianodon hypophthalmus) mince gel containing low salt (LS) and high salt (HS) were investigated. Without Lys or Arg addition, HS gel had the higher textural properties including hardness, chewiness, as well as cohesiveness than LS gel (P < 0.05) and the highest values were achieved when 1% Arg was incorporated in both LS and HS gels (P < 0.05). Arg had no effect on acceptability of mince gel. However, whiteness was decreased in HS gel when Arg was applied. Autolysis of gel was lower in HS gel containing Arg. No differences in protein patterns among all gel samples were found. Addition of Arg could increase the gelling ability of both LS and HS mince during heating as evidenced by higher storage modulus (G′) and viscous modulus (G″). Mince gel added with Arg had orderly interconnected structure and their microstructure was finer than that without Arg. Therefore, Arg could be used in LS gel from striped catfish mince, in which quality of gel was equivalent to HS counterpart. Practical Application Basic amino acid, especially arginine (Arg) with guanidinium group, could increase repulsive force between protein molecules at low‐salt concentration (0.5%). This resulted in high solubilization of muscle proteins, whereas gel formation or gel strength was higher than that containing high salt (2.5% to 3.5%). Thus, Arg could be used for production of fish mince gel containing low salt with lowered health risk.

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“…In particular, myofibrillar proteins are categorized as salt-soluble proteins, as they are soluble in a solution with an ionic strength of more than 0.3 M [21]. In another study about salt concentration on protein solubility, increasing salt concentration improved the solubility of protein up to a certain level, but not continuously [22]. Myofibrillar proteins are soluble at higher ionic strength compared with sarcoplasmic protein, another type of protein in skeletal muscle, which is soluble at low ionic strength [23].…”

Section: Sodium Chloride Effectsmentioning

confidence: 99%

Effects of Various Extraction Factors on Protein Yield of Haliotis discus hannai (Abalone)

et al. 2021

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Abalone (Haliotis discus hannai) is a widely consumed seafood in Asian countries. Rich in protein, abalone is consumed for refreshment, pregnancy care, and vitality. Although many studies have found that abalone protein has beneficial effects, the efficiency of the protein extraction method for abalone has rarely been studied. Therefore, this study aimed to examine the effects of various factors of abalone protein extraction, including extraction buffer, sonication, salt (NaCl) concentration, surfactant, and heating. Phosphate buffer showed higher protein yield compared with Tris-HCl buffer. In addition, the highest protein yield for each factor was observed at 60 s of sonication (84.44 µg/mg dw), 0.6 M NaCl (141.9 µg/mg dw), and 16 mM sodium dodecyl sulfate (SDS) (253.15 µg/mg dw). However, a combined effect was not observed. Lower protein extraction efficiency was observed for sous vide-cooked abalone. The electrophoresis assay revealed myofibrillar proteins, including paramyosin, actin, and tropomyosin. Overall, our results demonstrate that various extract conditions affect the protein extraction of abalone.

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Effect of pH and Salt Concentration on Protein Solubility of Slaughtered and Non-Slaughtered Broiler Chicken Meat

Cited by 26 publications

References 16 publications

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

Effects of lysine and arginine on the properties of low‐salt mince gel from striped catfish (Pangasianodon hypophthalmus)

Effects of Various Extraction Factors on Protein Yield of Haliotis discus hannai (Abalone)

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