Combined effect of CaCl2 and high pressure processing on the solubility of chicken breast myofibrillar proteins under sodium-reduced conditions

•HPP combined with CaCl2 (<40 mM) synergistically increased the solubility of MP.•CaCl2 at 100 mM could attenuate the solubilizing effect of HPP on MHC.•The changes of solubility could be related to the structural modification of MP.•The results are attractive for developing sodium-reduced meat p...

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Published inFood chemistry Vol. 269; pp. 236 - 243
Main Authors Wang, Yu, Zhou, Ying, Li, Pei-jun, Wang, Xi-xi, Cai, Ke-zhou, Chen, Cong-gui
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 15.12.2018
Subjects
CaCl2
High pressure processing (HPP)
Myofibrillar proteins (MP)
Solubility
Structural modification
High pressure processing (HPP)
Structural modification
Myofibrillar proteins (MP)
CaCl2
Solubility
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Abstract •HPP combined with CaCl2 (<40 mM) synergistically increased the solubility of MP.•CaCl2 at 100 mM could attenuate the solubilizing effect of HPP on MHC.•The changes of solubility could be related to the structural modification of MP.•The results are attractive for developing sodium-reduced meat products. The combined effect of calcium chloride (CaCl2) (20–100 mM) and high pressure processing (HPP, 200 MPa) on the solubility of myofibrillar proteins (MP) was investigated under sodium-reduced conditions (0.3 M sodium chloride). The results revealed that HPP combined with low concentrations (<40 mM) of CaCl2 synergistically increased the solubility of MP, but an antagonistic effect occurred when a high concentration (100 mM) of CaCl2 was present. This synergistic effect could be attributed to a mildly destabilized conformation of myosin, an increased surface hydrophobicity and the decreased total sulfhydryl group content of MP. However, CaCl2 at 100 mM destabilized myosin to a larger extent and induced non-disulfide covalent cross-linking of S-1 subfragment in pressurized MP, thus attenuating the solubilizing effect of HPP on the myosin heavy chain, resulting in the antagonistic effect. Therefore, HPP in combination with low-level CaCl2 (<40 mM) may improve the functional properties of sodium-reduced meat products.
AbstractList •HPP combined with CaCl2 (<40 mM) synergistically increased the solubility of MP.•CaCl2 at 100 mM could attenuate the solubilizing effect of HPP on MHC.•The changes of solubility could be related to the structural modification of MP.•The results are attractive for developing sodium-reduced meat products. The combined effect of calcium chloride (CaCl2) (20–100 mM) and high pressure processing (HPP, 200 MPa) on the solubility of myofibrillar proteins (MP) was investigated under sodium-reduced conditions (0.3 M sodium chloride). The results revealed that HPP combined with low concentrations (<40 mM) of CaCl2 synergistically increased the solubility of MP, but an antagonistic effect occurred when a high concentration (100 mM) of CaCl2 was present. This synergistic effect could be attributed to a mildly destabilized conformation of myosin, an increased surface hydrophobicity and the decreased total sulfhydryl group content of MP. However, CaCl2 at 100 mM destabilized myosin to a larger extent and induced non-disulfide covalent cross-linking of S-1 subfragment in pressurized MP, thus attenuating the solubilizing effect of HPP on the myosin heavy chain, resulting in the antagonistic effect. Therefore, HPP in combination with low-level CaCl2 (<40 mM) may improve the functional properties of sodium-reduced meat products.
The combined effect of calcium chloride (CaCl2) (20-100 mM) and high pressure processing (HPP, 200 MPa) on the solubility of myofibrillar proteins (MP) was investigated under sodium-reduced conditions (0.3 M sodium chloride). The results revealed that HPP combined with low concentrations (&lt;40 mM) of CaCl2 synergistically increased the solubility of MP, but an antagonistic effect occurred when a high concentration (100 mM) of CaCl2 was present. This synergistic effect could be attributed to a mildly destabilized conformation of myosin, an increased surface hydrophobicity and the decreased total sulfhydryl group content of MP. However, CaCl2 at 100 mM destabilized myosin to a larger extent and induced non-disulfide covalent cross-linking of S-1 subfragment in pressurized MP, thus attenuating the solubilizing effect of HPP on the myosin heavy chain, resulting in the antagonistic effect. Therefore, HPP in combination with low-level CaCl2 (&lt;40 mM) may improve the functional properties of sodium-reduced meat products.
Author Chen, Cong-gui
Wang, Yu
Wang, Xi-xi
Zhou, Ying
Cai, Ke-zhou
Li, Pei-jun
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  organization: School of Food Science and Engineering, Hefei University of Technology, Hefei 230009, Anhui Province, People’s Republic of China
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Keywords High pressure processing (HPP)
Structural modification
Myofibrillar proteins (MP)
CaCl2
Solubility
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Snippet •HPP combined with CaCl2 (<40 mM) synergistically increased the solubility of MP.•CaCl2 at 100 mM could attenuate the solubilizing effect of HPP on MHC.•The...
The combined effect of calcium chloride (CaCl2) (20-100 mM) and high pressure processing (HPP, 200 MPa) on the solubility of myofibrillar proteins (MP) was...
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StartPage 236
SubjectTerms CaCl2
High pressure processing (HPP)
Myofibrillar proteins (MP)
Solubility
Structural modification
Title Combined effect of CaCl2 and high pressure processing on the solubility of chicken breast myofibrillar proteins under sodium-reduced conditions
URI https://dx.doi.org/10.1016/j.foodchem.2018.06.107
https://search.proquest.com/docview/2087994014
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