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Tytuł:
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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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Autorzy:
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Yang HH; College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China.
Zhong C; College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China.
Sun LC; Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361021, China; College of Food and Biological Engineering, Jimei University, Xiamen 361021, China.
Li YK; College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China.
Chen H; College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China.
Wu GP; College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 30045, China. Electronic address: .
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Źródło:
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Food chemistry [Food Chem] 2021 Sep 15; Vol. 356, pp. 129734. Date of Electronic Publication: 2021 Mar 31.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Publication: Barking : Elsevier Applied Science Publishers
Original Publication: Barking, Eng., Applied Science Publishers.
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MeSH Terms:
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Bivalvia*
Protein Aggregates*
Meat Products/*analysis
Muscle Proteins/*chemistry
Sodium Chloride/*chemistry
Animals ; Hydrophobic and Hydrophilic Interactions ; Protein Unfolding ; Seafood ; Solubility
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Contributed Indexing:
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Keywords: Aggregation behaviors; Myofibrillar protein; NaCl substitution; Pearl mussel; Structural properties
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Substance Nomenclature:
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0 (Muscle Proteins)
0 (Protein Aggregates)
451W47IQ8X (Sodium Chloride)
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Entry Date(s):
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Date Created: 20210410 Date Completed: 20210520 Latest Revision: 20210520
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Update Code:
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20240105
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DOI:
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10.1016/j.foodchem.2021.129734
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PMID:
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33838607
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The effects of NaCl and its partial substitutes (KCl, MgCl 2 and CaCl 2 ) 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 2 and CaCl 2 , 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 2 and CaCl 2 in low substitution level is promising to improve functional properties of MP in low-sodium meat products.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)
