Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan
The purpose of this study is to explain the mechanism of porcine myofibrillar protein gel properties modulated by κ-carrageenan. The textural properties results showed that the stress at fracture of the composite gel with 0.4% κ-carrageenan had the highest value (91.33 g), which suggested that the 0...
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| Format: | Article |
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MDPI AG
2023-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/7/1444 |
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| author | Zhi Chen Cheng Luo Kangxu Wang Yinji Chen Xinbo Zhuang |
| author_facet | Zhi Chen Cheng Luo Kangxu Wang Yinji Chen Xinbo Zhuang |
| author_sort | Zhi Chen |
| collection | DOAJ |
| description | The purpose of this study is to explain the mechanism of porcine myofibrillar protein gel properties modulated by κ-carrageenan. The textural properties results showed that the stress at fracture of the composite gel with 0.4% κ-carrageenan had the highest value (91.33 g), which suggested that the 0.4% κ-carrageenan addition was the limitation. The strain at fracture was significantly reduced with κ-carrageenan addition. The composite gel with 0.4% κ-carrageenan had the lowest proportion of T22 (7.85%) and the shortest T21 relaxation time (252.81 ms). The paraffin section showed that the phase separation behavior of the composite gel transformed from single-phase behavior to dispersed phase behavior to bi-continuous phase behavior, and the ratio of CG/MP phase area significantly increased from 0.06 to 1.73. The SEM showed that the three-dimensional network of myofibrillar protein transformed from a loose structure to a compact structure to an unaggregated structure with κ-carrageenan addition. The myofibrillar protein network of the treatment with 0.4% κ-carrageenan had the highest DF value (1.7858) and lowest lacunary value (0.452). The principal component analysis was performed on the data of microstructure and textural properties, and the results showed that the dispersed phase behavior and moisture stabilization promoted the aggregation of myofibrillar protein and the composite gel had better water holding capacity and textural properties, while bi-continuous phase behavior hindered the aggregation of myofibrillar protein and the composite gel had worse water holding capacity and textural properties. |
| first_indexed | 2024-03-11T05:37:28Z |
| format | Article |
| id | doaj.art-151f6c87cf414b6d83cc23873f5c9f57 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T05:37:28Z |
| publishDate | 2023-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-151f6c87cf414b6d83cc23873f5c9f572023-11-17T16:41:22ZengMDPI AGFoods2304-81582023-03-01127144410.3390/foods12071444Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-CarrageenanZhi Chen0Cheng Luo1Kangxu Wang2Yinji Chen3Xinbo Zhuang4College of Biological Science and Agriculture, Qiannan Normal University for Nationalities, Duyun 558000, ChinaCollege of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, ChinaCollege of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, ChinaCollege of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, ChinaCollege of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, ChinaThe purpose of this study is to explain the mechanism of porcine myofibrillar protein gel properties modulated by κ-carrageenan. The textural properties results showed that the stress at fracture of the composite gel with 0.4% κ-carrageenan had the highest value (91.33 g), which suggested that the 0.4% κ-carrageenan addition was the limitation. The strain at fracture was significantly reduced with κ-carrageenan addition. The composite gel with 0.4% κ-carrageenan had the lowest proportion of T22 (7.85%) and the shortest T21 relaxation time (252.81 ms). The paraffin section showed that the phase separation behavior of the composite gel transformed from single-phase behavior to dispersed phase behavior to bi-continuous phase behavior, and the ratio of CG/MP phase area significantly increased from 0.06 to 1.73. The SEM showed that the three-dimensional network of myofibrillar protein transformed from a loose structure to a compact structure to an unaggregated structure with κ-carrageenan addition. The myofibrillar protein network of the treatment with 0.4% κ-carrageenan had the highest DF value (1.7858) and lowest lacunary value (0.452). The principal component analysis was performed on the data of microstructure and textural properties, and the results showed that the dispersed phase behavior and moisture stabilization promoted the aggregation of myofibrillar protein and the composite gel had better water holding capacity and textural properties, while bi-continuous phase behavior hindered the aggregation of myofibrillar protein and the composite gel had worse water holding capacity and textural properties.https://www.mdpi.com/2304-8158/12/7/1444fracture propertymicrostructureprotein gelationκ-carrageenan |
| spellingShingle | Zhi Chen Cheng Luo Kangxu Wang Yinji Chen Xinbo Zhuang Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan Foods fracture property microstructure protein gelation κ-carrageenan |
| title | Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan |
| title_full | Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan |
| title_fullStr | Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan |
| title_full_unstemmed | Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan |
| title_short | Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan |
| title_sort | insight into the mechanism of porcine myofibrillar protein gel properties modulated by κ carrageenan |
| topic | fracture property microstructure protein gelation κ-carrageenan |
| url | https://www.mdpi.com/2304-8158/12/7/1444 |
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