Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein
Problems with silver carp protein (SCP) include a strong fishy odor, low gel strength of SCP surimi, and susceptibility to gel degradation. The objective of this study was to improve the gel quality of SCP. The effects of the addition of native soy protein isolate (SPI) and SPI subjected to papain-r...
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MDPI AG
2023-05-01
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| Series: | Gels |
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| Online Access: | https://www.mdpi.com/2310-2861/9/5/420 |
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| author | Li Zheng Joe M. Regenstein Linyi Zhou Sayed Mohamed Mokhtar Zhongjiang Wang |
| author_facet | Li Zheng Joe M. Regenstein Linyi Zhou Sayed Mohamed Mokhtar Zhongjiang Wang |
| author_sort | Li Zheng |
| collection | DOAJ |
| description | Problems with silver carp protein (SCP) include a strong fishy odor, low gel strength of SCP surimi, and susceptibility to gel degradation. The objective of this study was to improve the gel quality of SCP. The effects of the addition of native soy protein isolate (SPI) and SPI subjected to papain-restricted hydrolysis on the gel characteristics and structural features of SCP were studied. The β-sheet structures in SPI increased after papain treatment. SPI treated with papain was crosslinked with SCP using glutamine transaminase (TG) to form a composite gel. Compared with the control, the addition of modified SPI increased the hardness, springiness, chewiness, cohesiveness, and water-holding capacity (WHC) of the protein gel (<i>p</i> < 0.05). In particular, the effects were most significant when the degree of SPI hydrolysis (DH) was 0.5% (i.e., gel sample M-2). The molecular force results demonstrated that hydrogen bonding, disulfide bonding, and hydrophobic association are important molecular forces in gel formation. The addition of the modified SPI increases the number of hydrogen bonds and the disulfide bonds. Scanning electron microscopy (SEM) analysis showed that the papain modifications allowed the formation of a composite gel with a complex, continuous, and uniform gel structure. However, the control of the DH is important as additional enzymatic hydrolysis of SPI decreased TG crosslinking. Overall, modified SPI has the potential to improve SCP gel texture and WHC. |
| first_indexed | 2024-03-11T03:42:38Z |
| format | Article |
| id | doaj.art-69be7925d9d340ad92dd8417bd27ccff |
| institution | Directory Open Access Journal |
| issn | 2310-2861 |
| language | English |
| last_indexed | 2024-03-11T03:42:38Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Gels |
| spelling | doaj.art-69be7925d9d340ad92dd8417bd27ccff2023-11-18T01:28:16ZengMDPI AGGels2310-28612023-05-019542010.3390/gels9050420Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp ProteinLi Zheng0Joe M. Regenstein1Linyi Zhou2Sayed Mohamed Mokhtar3Zhongjiang Wang4College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaDepartment of Food Science, Cornell University, Ithaca, NY 14853, USASchool of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaDepartment of Food Technology, Faculty of Agriculture, Suez Canal University, Ismailia 41522, EgyptCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaProblems with silver carp protein (SCP) include a strong fishy odor, low gel strength of SCP surimi, and susceptibility to gel degradation. The objective of this study was to improve the gel quality of SCP. The effects of the addition of native soy protein isolate (SPI) and SPI subjected to papain-restricted hydrolysis on the gel characteristics and structural features of SCP were studied. The β-sheet structures in SPI increased after papain treatment. SPI treated with papain was crosslinked with SCP using glutamine transaminase (TG) to form a composite gel. Compared with the control, the addition of modified SPI increased the hardness, springiness, chewiness, cohesiveness, and water-holding capacity (WHC) of the protein gel (<i>p</i> < 0.05). In particular, the effects were most significant when the degree of SPI hydrolysis (DH) was 0.5% (i.e., gel sample M-2). The molecular force results demonstrated that hydrogen bonding, disulfide bonding, and hydrophobic association are important molecular forces in gel formation. The addition of the modified SPI increases the number of hydrogen bonds and the disulfide bonds. Scanning electron microscopy (SEM) analysis showed that the papain modifications allowed the formation of a composite gel with a complex, continuous, and uniform gel structure. However, the control of the DH is important as additional enzymatic hydrolysis of SPI decreased TG crosslinking. Overall, modified SPI has the potential to improve SCP gel texture and WHC.https://www.mdpi.com/2310-2861/9/5/420soy protein isolatesilver carp proteinpapainglutamine transaminase<i>Glycine max</i><i>Hypophthalmichthys molitrix</i> |
| spellingShingle | Li Zheng Joe M. Regenstein Linyi Zhou Sayed Mohamed Mokhtar Zhongjiang Wang Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein Gels soy protein isolate silver carp protein papain glutamine transaminase <i>Glycine max</i> <i>Hypophthalmichthys molitrix</i> |
| title | Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein |
| title_full | Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein |
| title_fullStr | Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein |
| title_full_unstemmed | Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein |
| title_short | Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein |
| title_sort | gel properties and structural characteristics of composite gels of soy protein isolate and silver carp protein |
| topic | soy protein isolate silver carp protein papain glutamine transaminase <i>Glycine max</i> <i>Hypophthalmichthys molitrix</i> |
| url | https://www.mdpi.com/2310-2861/9/5/420 |
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