Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis
Heat facilitates aggregation and gel formation of soybean proteins. Ultrasonic reduces the size of protein aggregates. This study examined the impact of glycinin (11S) subunits on soybean lipophilic proteins (SLPs) gel formation and underlying mechanisms. Effects of protein dispersion pretreatment w...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-02-01
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| Series: | Ultrasonics Sonochemistry |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1350417725000185 |
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| author | Yuyang Huang Jiyuan Liu Yongping Li Yongsheng Zhu Gang Chen Baoning Zheng Yixin Zhang Yang Li Xiuqing Zhu |
| author_facet | Yuyang Huang Jiyuan Liu Yongping Li Yongsheng Zhu Gang Chen Baoning Zheng Yixin Zhang Yang Li Xiuqing Zhu |
| author_sort | Yuyang Huang |
| collection | DOAJ |
| description | Heat facilitates aggregation and gel formation of soybean proteins. Ultrasonic reduces the size of protein aggregates. This study examined the impact of glycinin (11S) subunits on soybean lipophilic proteins (SLPs) gel formation and underlying mechanisms. Effects of protein dispersion pretreatment with 400 W ultrasonic and associated mechanisms were assessed. Addition of the A- and B-subunits before and after ultrasonic minimally affected SLP secondary structure. A-subunit addition before ultrasonic negligibly affected SLP tertiary structure. Addition of the B-subunit after ultrasonic reduced hydrophobic thermal aggregation. However, the small B-subunit size was unfavorable for the formation of a gel matrix, which led to poor gel properties. In contrast, solubility of the A-subunit after ultrasonic was increased to 31.06 ± 1.62 %). Particle size was decreased to 43.33 ± 1.36 nm for A:SLP (1:2). Endogenous fluorescence spectroscopy demonstrated increased protein unfolding after ultrasonic and decreased disulfide bonds. These changes improved the gel state. Rheological and microstructural analyses revealed increased energy storage modulus and yield strain, accompanied by a more homogeneous microstructure following ultrasonic. Microscopic improvement resulted in increased encapsulated water within interstitial spaces of the A-SLP gel matrix. This enhanced water mobility in B-SLP gels, in turn weakening gel stability. The changes observed in B-SLP were primarily due to reduced hydrophobic interactions between the proteins. The findings clarify the effect of ultrasonic treatment on the formation of soybean globulin-SLP hybrid gels at the subunit level. The data provide a theoretical basis for the synergistic utilization of soybean proteins among different components. |
| format | Article |
| id | doaj-art-9039291afe91496cb2a0897b205969db |
| institution | Kabale University |
| issn | 1350-4177 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Ultrasonics Sonochemistry |
| spelling | doaj-art-9039291afe91496cb2a0897b205969db2025-02-01T04:11:39ZengElsevierUltrasonics Sonochemistry1350-41772025-02-01113107239Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysisYuyang Huang0Jiyuan Liu1Yongping Li2Yongsheng Zhu3Gang Chen4Baoning Zheng5Yixin Zhang6Yang Li7Xiuqing Zhu8Department of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, Harbin 150028, Heilongjiang, ChinaDepartment of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, Harbin 150028, Heilongjiang, ChinaSchool of Grain Engineering, Heilongjiang Communications Polytechnic, Harbin 150025, ChinaHEILONGJIANG JOYUNG SOYMILK CO.LTD, ChinaHEILONGJIANG JOYUNG SOYMILK CO.LTD, ChinaDepartment of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, Harbin 150028, Heilongjiang, ChinaDepartment of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, Harbin 150028, Heilongjiang, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaDepartment of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, Harbin 150028, Heilongjiang, China; Corresponding author at: at: No. 1, Xuehai Street, Songbei District, Harbin 150028, Heilongjiang, China.Heat facilitates aggregation and gel formation of soybean proteins. Ultrasonic reduces the size of protein aggregates. This study examined the impact of glycinin (11S) subunits on soybean lipophilic proteins (SLPs) gel formation and underlying mechanisms. Effects of protein dispersion pretreatment with 400 W ultrasonic and associated mechanisms were assessed. Addition of the A- and B-subunits before and after ultrasonic minimally affected SLP secondary structure. A-subunit addition before ultrasonic negligibly affected SLP tertiary structure. Addition of the B-subunit after ultrasonic reduced hydrophobic thermal aggregation. However, the small B-subunit size was unfavorable for the formation of a gel matrix, which led to poor gel properties. In contrast, solubility of the A-subunit after ultrasonic was increased to 31.06 ± 1.62 %). Particle size was decreased to 43.33 ± 1.36 nm for A:SLP (1:2). Endogenous fluorescence spectroscopy demonstrated increased protein unfolding after ultrasonic and decreased disulfide bonds. These changes improved the gel state. Rheological and microstructural analyses revealed increased energy storage modulus and yield strain, accompanied by a more homogeneous microstructure following ultrasonic. Microscopic improvement resulted in increased encapsulated water within interstitial spaces of the A-SLP gel matrix. This enhanced water mobility in B-SLP gels, in turn weakening gel stability. The changes observed in B-SLP were primarily due to reduced hydrophobic interactions between the proteins. The findings clarify the effect of ultrasonic treatment on the formation of soybean globulin-SLP hybrid gels at the subunit level. The data provide a theoretical basis for the synergistic utilization of soybean proteins among different components.http://www.sciencedirect.com/science/article/pii/S1350417725000185Soybean lipophilic proteinGlycinin subunitsUltrasonicStructureGel properties |
| spellingShingle | Yuyang Huang Jiyuan Liu Yongping Li Yongsheng Zhu Gang Chen Baoning Zheng Yixin Zhang Yang Li Xiuqing Zhu Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis Ultrasonics Sonochemistry Soybean lipophilic protein Glycinin subunits Ultrasonic Structure Gel properties |
| title | Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis |
| title_full | Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis |
| title_fullStr | Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis |
| title_full_unstemmed | Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis |
| title_short | Focusing on the mechanism of glycinin-soybean lipophilic protein hybrid gels: Effect of ultrasonic, subunit interactions, and formation process analysis |
| title_sort | focusing on the mechanism of glycinin soybean lipophilic protein hybrid gels effect of ultrasonic subunit interactions and formation process analysis |
| topic | Soybean lipophilic protein Glycinin subunits Ultrasonic Structure Gel properties |
| url | http://www.sciencedirect.com/science/article/pii/S1350417725000185 |
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