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JOURNAL OF FOOD SCIENCE · 2024 ·Vol. 89 ·期 12 ·9060-9072 · IF 3.2

Effect of NaCl replacement by other salt mixtures on myofibrillar proteins: Underlining protein structure, gel formation, and chewing properties

Haibo Shi,Yongjie Li,Jiabao Zheng,Xianqi Yao,Wei Wang,Igor Tomasevic,Weizheng Sun

The protein structure, gel changes, and chewing properties of low-sodium myofibrillar protein (MP) prepared by compound chloride salts (KCl/MgCl 2 , KCl/CaCl 2 , and KCl/MgCl 2 /CaCl 2 ) and different substitution degrees (10%, 25%, and 40%) at same ionic strength (0.6 M) were investigated. The results revealed that the low-sodium MP gels containing CaCl 2 manifested more liquid loss and less moisture content accompanied by obvious morphological shrinkage, while KCl/MgCl 2 contributed to the gel juiciness. At high substitution degree of 40%, KCl/CaCl 2 substitution rendered the gel with dense structure and highest strength, but worse water retention capacity. Using other compound chloride salts influenced the chewing efficiency, and CaCl 2 substitution made the gel relatively hard to chew. The inhomogeneous structure accompanied by cluster blocks in KCl/CaCl 2 -substituted MP gel accelerated the overall fracture rate. During heating process, more proteins in CaCl 2 -substituted MP did not participate in gel formation, intervening the final gel properties. The chloride salt mixtures containing MgCl 2 , rather than CaCl 2 , avoided or alleviated the liquid loss and shrinkage of low-sodium MP gel within the substitution degree of 10%–40%, and substitution degree not exceeding 25% was more reasonable for the controlled qualities.

研究领域: 食品科学 · 蛋白质化学
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Foods · 2024 ·Vol. 13 ·期 5 ·737 · IF 4.7

Characterization of the Effects of Low-Sodium Salt Substitution on Sensory Quality, Protein Oxidation, and Hydrolysis of Air-Dried Chicken Meat and Its Molecular Mechanisms Based on Tandem Mass Tagging-Labeled Quantitative Proteomics

Jianhao Li,Zihang Shi,Xiankang Fan,Lihui Du,Qiang Xia,Changyu Zhou,Yangying Sun,Baocai Xu,Daodong Pan

The effects of low-sodium salt mixture substitution on the sensory quality, protein oxidation, and hydrolysis of air-dried chicken and its molecular mechanisms were investigated based on tandem mass tagging (TMT) quantitative proteomics. The composite salt formulated with 1.6% KCl, 0.8% MgCl2, and 5.6% NaCl was found to improve the freshness and texture quality scores. Low-sodium salt mixture substitution significantly decreased the carbonyl content (1.52 nmol/mg), surface hydrophobicity (102.58 μg), and dimeric tyrosine content (2.69 A.U.), and significantly increased the sulfhydryl content (74.46 nmol/mg) and tryptophan fluorescence intensity, suggesting that protein oxidation was inhibited. Furthermore, low-sodium salt mixture substitution significantly increased the protein hydrolysis index (0.067), and cathepsin B and L activities (102.13 U/g and 349.25 U/g), suggesting that protein hydrolysis was facilitated. The correlation results showed that changes in the degree of protein hydrolysis and protein oxidation were closely related to sensory quality. TMT quantitative proteomics indicated that the degradation of myosin and titin as well as changes in the activities of the enzymes, CNDP2, DPP7, ABHD12B, FADH2A, and AASS, were responsible for the changes in the taste quality. In addition, CNDP2, ALDH1A1, and NMNAT1 are key enzymes that reduce protein oxidation. Overall, KCl and MgCl2composite salt substitution is an effective method for producing low-sodium air-dried chicken.

CAS / MDL: 69-78-3 50-01-1
研究领域: 食品科学 · 蛋白质组学 · 感官评价 · 生物化学
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