Xuan Zhang , Yu Chen , Yu Hu , Jian Jin , Hui lin Shen , Chibuike C. Udenigwe
{"title":"双频超声场下花生和荞麦蛋白质在转谷氨酰胺酶介导下的交联:功能属性研究","authors":"Xuan Zhang , Yu Chen , Yu Hu , Jian Jin , Hui lin Shen , Chibuike C. Udenigwe","doi":"10.1016/j.foodp.2024.100019","DOIUrl":null,"url":null,"abstract":"<div><p>Peanut protein (PP)/buckwheat protein (BWP) mixture crosslinked by transglutaminase (TGase) under dual-frequency ultrasound (DFU) field was developed and its structural and functional properties were characterized. The results showed that the optimal DFU parameters for PP-BWP crosslinking were 25 kHz/40 kHz dual-frequency ultrasound working time ratio of 10:10 (s/s), a temperature of 45°C, ultrasonic power density of 125 W/L and time duration of 30 min, resulting in the degree of crosslinking (DC) of 37.7 %, which is 125 % higher than that of the control. The solubility at pH 7.0, oil-holding capacity, and emulsifying capacity of the protein aggregate (peanut protein-buckwheat protein crosslinked by TGase under dual-frequency ultrasound, U-TG-PP-BWP) was significantly (<em>P</em><0.05) improved compared with protein aggregates formed without ultrasound (TG-PP-BWP); however, the emulsion stability, foaming capacity and form stability decreased. Secondary structure analysis indicated no apparent difference between un-crosslinked protein and U-TG-PP-BWP. After ultrasound treatment, the α-helix decreased by 11.2 % and the β-sheet, β-turn and random coil increased by 7.7 %, 3.4 % and 4.7 %, respectively, in U-TG-PP-BWP compared to TG-PP-BWP. The microstructures showed that U-TG-PP-BWP formed a lamellar structure with many micropores while TG-PP-BWP aggregated into large and tight blocks. SDS-PAGE analysis showed that, compared to PP and BWP, the subunit bands of cross-linked TG-PP-BWP and U-TG-PP-BWP were altered at 14.4–116 kDa, yielding proteins larger than 116 kDa, suggesting covalent cross-linking of the two proteins. In conclusion, the enzymatic cross-linking of proteins can be promoted by DFU, providing a new approach to developing novel plant proteins.</p></div>","PeriodicalId":100545,"journal":{"name":"Food Physics","volume":"1 ","pages":"Article 100019"},"PeriodicalIF":0.0000,"publicationDate":"2024-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2950069924000136/pdfft?md5=081c15b748ec139d6e41097a2a6a19cb&pid=1-s2.0-S2950069924000136-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Transglutaminase mediated cross-linking of peanut and buckwheat proteins under dual-frequency ultrasound field: Functional attributes study\",\"authors\":\"Xuan Zhang , Yu Chen , Yu Hu , Jian Jin , Hui lin Shen , Chibuike C. Udenigwe\",\"doi\":\"10.1016/j.foodp.2024.100019\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Peanut protein (PP)/buckwheat protein (BWP) mixture crosslinked by transglutaminase (TGase) under dual-frequency ultrasound (DFU) field was developed and its structural and functional properties were characterized. The results showed that the optimal DFU parameters for PP-BWP crosslinking were 25 kHz/40 kHz dual-frequency ultrasound working time ratio of 10:10 (s/s), a temperature of 45°C, ultrasonic power density of 125 W/L and time duration of 30 min, resulting in the degree of crosslinking (DC) of 37.7 %, which is 125 % higher than that of the control. The solubility at pH 7.0, oil-holding capacity, and emulsifying capacity of the protein aggregate (peanut protein-buckwheat protein crosslinked by TGase under dual-frequency ultrasound, U-TG-PP-BWP) was significantly (<em>P</em><0.05) improved compared with protein aggregates formed without ultrasound (TG-PP-BWP); however, the emulsion stability, foaming capacity and form stability decreased. Secondary structure analysis indicated no apparent difference between un-crosslinked protein and U-TG-PP-BWP. After ultrasound treatment, the α-helix decreased by 11.2 % and the β-sheet, β-turn and random coil increased by 7.7 %, 3.4 % and 4.7 %, respectively, in U-TG-PP-BWP compared to TG-PP-BWP. The microstructures showed that U-TG-PP-BWP formed a lamellar structure with many micropores while TG-PP-BWP aggregated into large and tight blocks. SDS-PAGE analysis showed that, compared to PP and BWP, the subunit bands of cross-linked TG-PP-BWP and U-TG-PP-BWP were altered at 14.4–116 kDa, yielding proteins larger than 116 kDa, suggesting covalent cross-linking of the two proteins. In conclusion, the enzymatic cross-linking of proteins can be promoted by DFU, providing a new approach to developing novel plant proteins.</p></div>\",\"PeriodicalId\":100545,\"journal\":{\"name\":\"Food Physics\",\"volume\":\"1 \",\"pages\":\"Article 100019\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-07-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S2950069924000136/pdfft?md5=081c15b748ec139d6e41097a2a6a19cb&pid=1-s2.0-S2950069924000136-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Physics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2950069924000136\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Physics","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2950069924000136","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Transglutaminase mediated cross-linking of peanut and buckwheat proteins under dual-frequency ultrasound field: Functional attributes study
Peanut protein (PP)/buckwheat protein (BWP) mixture crosslinked by transglutaminase (TGase) under dual-frequency ultrasound (DFU) field was developed and its structural and functional properties were characterized. The results showed that the optimal DFU parameters for PP-BWP crosslinking were 25 kHz/40 kHz dual-frequency ultrasound working time ratio of 10:10 (s/s), a temperature of 45°C, ultrasonic power density of 125 W/L and time duration of 30 min, resulting in the degree of crosslinking (DC) of 37.7 %, which is 125 % higher than that of the control. The solubility at pH 7.0, oil-holding capacity, and emulsifying capacity of the protein aggregate (peanut protein-buckwheat protein crosslinked by TGase under dual-frequency ultrasound, U-TG-PP-BWP) was significantly (P<0.05) improved compared with protein aggregates formed without ultrasound (TG-PP-BWP); however, the emulsion stability, foaming capacity and form stability decreased. Secondary structure analysis indicated no apparent difference between un-crosslinked protein and U-TG-PP-BWP. After ultrasound treatment, the α-helix decreased by 11.2 % and the β-sheet, β-turn and random coil increased by 7.7 %, 3.4 % and 4.7 %, respectively, in U-TG-PP-BWP compared to TG-PP-BWP. The microstructures showed that U-TG-PP-BWP formed a lamellar structure with many micropores while TG-PP-BWP aggregated into large and tight blocks. SDS-PAGE analysis showed that, compared to PP and BWP, the subunit bands of cross-linked TG-PP-BWP and U-TG-PP-BWP were altered at 14.4–116 kDa, yielding proteins larger than 116 kDa, suggesting covalent cross-linking of the two proteins. In conclusion, the enzymatic cross-linking of proteins can be promoted by DFU, providing a new approach to developing novel plant proteins.