Songmin Cao , Fanwei Xi , Ziye Wang , Hui He , Di Zhao , Miao Zhang
{"title":"超声处理提高了大豆-肌原纤维双蛋白系统的稳定性和消化性能。","authors":"Songmin Cao , Fanwei Xi , Ziye Wang , Hui He , Di Zhao , Miao Zhang","doi":"10.1016/j.ultsonch.2025.107613","DOIUrl":null,"url":null,"abstract":"<div><div>This study systematically investigated the effects of sono-processing treatment on the stability and digestive characteristics of soy protein isolate (SPI) and myofibrillar protein (MPN) mixed systems. The sono-processing intensity in the SPI-MPN4 group reached 37.58%, which was approximately 4.12 times higher than that of the SPI-MPN2 system (9.12%), indicating significantly greater efficiency in structural modification. Consequently, the SPI-MPN4 system exhibited the most pronounced structural transformation, leading to reduced disordered aggregation and improved system stability. To be specific, the system stability of the SPI-MPN4 system was enhanced by 28.94% when compared with that of the SPI-MPN2 group. Additionally, structural analyses revealed that ultrasound effectively disrupted hydrogen bonds, reduced α-helix content, and promoted the assembly of structurally ordered SPI–MPN complexes. Notably, the random coil contents in SPI-MPN4 increased by approximately 22.70%, facilitating trypsin accessibility. These findings highlighted that sono-processing intensity changes were critical factors governing the structural alteration of the dual-protein system. This insight was pivotal for designing targeted and energy-efficient processing strategies in the future.</div></div>","PeriodicalId":442,"journal":{"name":"Ultrasonics Sonochemistry","volume":"122 ","pages":"Article 107613"},"PeriodicalIF":9.7000,"publicationDate":"2025-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Sono-processing treatments enhanced the stability and digestive properties of soy-myofibrillar dual-protein systems\",\"authors\":\"Songmin Cao , Fanwei Xi , Ziye Wang , Hui He , Di Zhao , Miao Zhang\",\"doi\":\"10.1016/j.ultsonch.2025.107613\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>This study systematically investigated the effects of sono-processing treatment on the stability and digestive characteristics of soy protein isolate (SPI) and myofibrillar protein (MPN) mixed systems. The sono-processing intensity in the SPI-MPN4 group reached 37.58%, which was approximately 4.12 times higher than that of the SPI-MPN2 system (9.12%), indicating significantly greater efficiency in structural modification. Consequently, the SPI-MPN4 system exhibited the most pronounced structural transformation, leading to reduced disordered aggregation and improved system stability. To be specific, the system stability of the SPI-MPN4 system was enhanced by 28.94% when compared with that of the SPI-MPN2 group. Additionally, structural analyses revealed that ultrasound effectively disrupted hydrogen bonds, reduced α-helix content, and promoted the assembly of structurally ordered SPI–MPN complexes. Notably, the random coil contents in SPI-MPN4 increased by approximately 22.70%, facilitating trypsin accessibility. These findings highlighted that sono-processing intensity changes were critical factors governing the structural alteration of the dual-protein system. This insight was pivotal for designing targeted and energy-efficient processing strategies in the future.</div></div>\",\"PeriodicalId\":442,\"journal\":{\"name\":\"Ultrasonics Sonochemistry\",\"volume\":\"122 \",\"pages\":\"Article 107613\"},\"PeriodicalIF\":9.7000,\"publicationDate\":\"2025-10-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ultrasonics Sonochemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S135041772500392X\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"ACOUSTICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Ultrasonics Sonochemistry","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S135041772500392X","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ACOUSTICS","Score":null,"Total":0}
Sono-processing treatments enhanced the stability and digestive properties of soy-myofibrillar dual-protein systems
This study systematically investigated the effects of sono-processing treatment on the stability and digestive characteristics of soy protein isolate (SPI) and myofibrillar protein (MPN) mixed systems. The sono-processing intensity in the SPI-MPN4 group reached 37.58%, which was approximately 4.12 times higher than that of the SPI-MPN2 system (9.12%), indicating significantly greater efficiency in structural modification. Consequently, the SPI-MPN4 system exhibited the most pronounced structural transformation, leading to reduced disordered aggregation and improved system stability. To be specific, the system stability of the SPI-MPN4 system was enhanced by 28.94% when compared with that of the SPI-MPN2 group. Additionally, structural analyses revealed that ultrasound effectively disrupted hydrogen bonds, reduced α-helix content, and promoted the assembly of structurally ordered SPI–MPN complexes. Notably, the random coil contents in SPI-MPN4 increased by approximately 22.70%, facilitating trypsin accessibility. These findings highlighted that sono-processing intensity changes were critical factors governing the structural alteration of the dual-protein system. This insight was pivotal for designing targeted and energy-efficient processing strategies in the future.
期刊介绍:
Ultrasonics Sonochemistry stands as a premier international journal dedicated to the publication of high-quality research articles primarily focusing on chemical reactions and reactors induced by ultrasonic waves, known as sonochemistry. Beyond chemical reactions, the journal also welcomes contributions related to cavitation-induced events and processing, including sonoluminescence, and the transformation of materials on chemical, physical, and biological levels.
Since its inception in 1994, Ultrasonics Sonochemistry has consistently maintained a top ranking in the "Acoustics" category, reflecting its esteemed reputation in the field. The journal publishes exceptional papers covering various areas of ultrasonics and sonochemistry. Its contributions are highly regarded by both academia and industry stakeholders, demonstrating its relevance and impact in advancing research and innovation.