Effects of partial substitution of NaCl on myofibrillar protein properties from pearl mussel Hyriopsis cumingii muscle: Structural characteristics and aggregation behaviors
•Paramyosin was the main component of MP from pearl mussel muscle.•MP showed excellent solubility and microstructure as NaCl increased to 0.6 M.•MgCl2 and CaCl2 at low replacement level could show acceptable protein properties.•The proper structure unfolding and aggregation of MP were good for its p...
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| Published in | Food chemistry Vol. 356; p. 129734 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier Ltd
15.09.2021
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| Subjects | |
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| Abstract | •Paramyosin was the main component of MP from pearl mussel muscle.•MP showed excellent solubility and microstructure as NaCl increased to 0.6 M.•MgCl2 and CaCl2 at low replacement level could show acceptable protein properties.•The proper structure unfolding and aggregation of MP were good for its properties.•Partial substitution of NaCl could be an alternative for pearl mussel meat product.
The effects of NaCl and its partial substitutes (KCl, MgCl2 and CaCl2) on solubility, structural characteristics and aggregation behaviors of myofibrillar protein (MP) from pearl mussel muscle were investigated and compared. MP at 0.6 M NaCl was beneficial to protein unfolding and showed excellent potential functional properties. When NaCl was substituted in low level, MPs also showed good solubility and ordered microstructure as well as NaCl, especially MgCl2 and CaCl2, due to the unfolding of α-helical structures and subsequently exposed tyrosine residues and hydrophobic groups. However, the obviously increased disulfide bonds and hydrophobic interactions in high substitution level indicated the excessive non-sodium salts had negative effects on molecular rearrangement, leading to irregular and overly tight of microstructure. Thus, NaCl partially substituted by KCl, MgCl2 and CaCl2 in low substitution level is promising to improve functional properties of MP in low-sodium meat products. |
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| AbstractList | •Paramyosin was the main component of MP from pearl mussel muscle.•MP showed excellent solubility and microstructure as NaCl increased to 0.6 M.•MgCl2 and CaCl2 at low replacement level could show acceptable protein properties.•The proper structure unfolding and aggregation of MP were good for its properties.•Partial substitution of NaCl could be an alternative for pearl mussel meat product.
The effects of NaCl and its partial substitutes (KCl, MgCl2 and CaCl2) on solubility, structural characteristics and aggregation behaviors of myofibrillar protein (MP) from pearl mussel muscle were investigated and compared. MP at 0.6 M NaCl was beneficial to protein unfolding and showed excellent potential functional properties. When NaCl was substituted in low level, MPs also showed good solubility and ordered microstructure as well as NaCl, especially MgCl2 and CaCl2, due to the unfolding of α-helical structures and subsequently exposed tyrosine residues and hydrophobic groups. However, the obviously increased disulfide bonds and hydrophobic interactions in high substitution level indicated the excessive non-sodium salts had negative effects on molecular rearrangement, leading to irregular and overly tight of microstructure. Thus, NaCl partially substituted by KCl, MgCl2 and CaCl2 in low substitution level is promising to improve functional properties of MP in low-sodium meat products. The effects of NaCl and its partial substitutes (KCl, MgCl and CaCl ) on solubility, structural characteristics and aggregation behaviors of myofibrillar protein (MP) from pearl mussel muscle were investigated and compared. MP at 0.6 M NaCl was beneficial to protein unfolding and showed excellent potential functional properties. When NaCl was substituted in low level, MPs also showed good solubility and ordered microstructure as well as NaCl, especially MgCl and CaCl , due to the unfolding of α-helical structures and subsequently exposed tyrosine residues and hydrophobic groups. However, the obviously increased disulfide bonds and hydrophobic interactions in high substitution level indicated the excessive non-sodium salts had negative effects on molecular rearrangement, leading to irregular and overly tight of microstructure. Thus, NaCl partially substituted by KCl, MgCl and CaCl in low substitution level is promising to improve functional properties of MP in low-sodium meat products. The effects of NaCl and its partial substitutes (KCl, MgCl₂ and CaCl₂) on solubility, structural characteristics and aggregation behaviors of myofibrillar protein (MP) from pearl mussel muscle were investigated and compared. MP at 0.6 M NaCl was beneficial to protein unfolding and showed excellent potential functional properties. When NaCl was substituted in low level, MPs also showed good solubility and ordered microstructure as well as NaCl, especially MgCl₂ and CaCl₂, due to the unfolding of α-helical structures and subsequently exposed tyrosine residues and hydrophobic groups. However, the obviously increased disulfide bonds and hydrophobic interactions in high substitution level indicated the excessive non-sodium salts had negative effects on molecular rearrangement, leading to irregular and overly tight of microstructure. Thus, NaCl partially substituted by KCl, MgCl₂ and CaCl₂ in low substitution level is promising to improve functional properties of MP in low-sodium meat products. The effects of NaCl and its partial substitutes (KCl, MgCl2 and CaCl2) on solubility, structural characteristics and aggregation behaviors of myofibrillar protein (MP) from pearl mussel muscle were investigated and compared. MP at 0.6 M NaCl was beneficial to protein unfolding and showed excellent potential functional properties. When NaCl was substituted in low level, MPs also showed good solubility and ordered microstructure as well as NaCl, especially MgCl2 and CaCl2, due to the unfolding of α-helical structures and subsequently exposed tyrosine residues and hydrophobic groups. However, the obviously increased disulfide bonds and hydrophobic interactions in high substitution level indicated the excessive non-sodium salts had negative effects on molecular rearrangement, leading to irregular and overly tight of microstructure. Thus, NaCl partially substituted by KCl, MgCl2 and CaCl2 in low substitution level is promising to improve functional properties of MP in low-sodium meat products.The effects of NaCl and its partial substitutes (KCl, MgCl2 and CaCl2) on solubility, structural characteristics and aggregation behaviors of myofibrillar protein (MP) from pearl mussel muscle were investigated and compared. MP at 0.6 M NaCl was beneficial to protein unfolding and showed excellent potential functional properties. When NaCl was substituted in low level, MPs also showed good solubility and ordered microstructure as well as NaCl, especially MgCl2 and CaCl2, due to the unfolding of α-helical structures and subsequently exposed tyrosine residues and hydrophobic groups. However, the obviously increased disulfide bonds and hydrophobic interactions in high substitution level indicated the excessive non-sodium salts had negative effects on molecular rearrangement, leading to irregular and overly tight of microstructure. Thus, NaCl partially substituted by KCl, MgCl2 and CaCl2 in low substitution level is promising to improve functional properties of MP in low-sodium meat products. |
| ArticleNumber | 129734 |
| Author | Yang, Huan-huan Li, Ya-ke Sun, Le-chang Zhong, Chan Chen, Hu Wu, Guo-ping |
| Author_xml | – sequence: 1 givenname: Huan-huan surname: Yang fullname: Yang, Huan-huan organization: College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China – sequence: 2 givenname: Chan surname: Zhong fullname: Zhong, Chan organization: College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China – sequence: 3 givenname: Le-chang surname: Sun fullname: Sun, Le-chang organization: Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361021, China – sequence: 4 givenname: Ya-ke surname: Li fullname: Li, Ya-ke organization: College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China – sequence: 5 givenname: Hu surname: Chen fullname: Chen, Hu organization: College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China – sequence: 6 givenname: Guo-ping surname: Wu fullname: Wu, Guo-ping email: jdwgp@163.com organization: College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China |
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| Keywords | Pearl mussel Myofibrillar protein NaCl substitution Aggregation behaviors Structural properties |
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| Snippet | •Paramyosin was the main component of MP from pearl mussel muscle.•MP showed excellent solubility and microstructure as NaCl increased to 0.6 M.•MgCl2 and... The effects of NaCl and its partial substitutes (KCl, MgCl and CaCl ) on solubility, structural characteristics and aggregation behaviors of myofibrillar... The effects of NaCl and its partial substitutes (KCl, MgCl2 and CaCl2) on solubility, structural characteristics and aggregation behaviors of myofibrillar... The effects of NaCl and its partial substitutes (KCl, MgCl₂ and CaCl₂) on solubility, structural characteristics and aggregation behaviors of myofibrillar... |
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| SubjectTerms | Aggregation behaviors disulfides food chemistry hydrophobicity Hyriopsis cumingii meat microstructure muscles Myofibrillar protein NaCl substitution Pearl mussel pearl mussels solubility Structural properties tyrosine |
| Title | Effects of partial substitution of NaCl on myofibrillar protein properties from pearl mussel Hyriopsis cumingii muscle: Structural characteristics and aggregation behaviors |
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