Mikkel Madsen , Sanaullah Khan , Sonja Kunstmann , Finn L. Aachmann , Richard Ipsen , Peter Westh , Cecilia Emanuelsson , Birte Svensson
{"title":"乳清蛋白的无辅助高效转谷氨酰胺酶交联强烈影响海藻酸蛋白颗粒的形成和结构","authors":"Mikkel Madsen , Sanaullah Khan , Sonja Kunstmann , Finn L. Aachmann , Richard Ipsen , Peter Westh , Cecilia Emanuelsson , Birte Svensson","doi":"10.1016/j.fochms.2022.100137","DOIUrl":null,"url":null,"abstract":"<div><p>There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO<sub>3</sub>, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t<sub>1/2</sub> = 3 h, while the polymerization occurred with t<sub>1/2</sub> = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate.</p></div>","PeriodicalId":34477,"journal":{"name":"Food Chemistry Molecular Sciences","volume":"5 ","pages":"Article 100137"},"PeriodicalIF":4.1000,"publicationDate":"2022-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f7/16/main.PMC9508153.pdf","citationCount":"3","resultStr":"{\"title\":\"Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles\",\"authors\":\"Mikkel Madsen , Sanaullah Khan , Sonja Kunstmann , Finn L. Aachmann , Richard Ipsen , Peter Westh , Cecilia Emanuelsson , Birte Svensson\",\"doi\":\"10.1016/j.fochms.2022.100137\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO<sub>3</sub>, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t<sub>1/2</sub> = 3 h, while the polymerization occurred with t<sub>1/2</sub> = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate.</p></div>\",\"PeriodicalId\":34477,\"journal\":{\"name\":\"Food Chemistry Molecular Sciences\",\"volume\":\"5 \",\"pages\":\"Article 100137\"},\"PeriodicalIF\":4.1000,\"publicationDate\":\"2022-12-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f7/16/main.PMC9508153.pdf\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry Molecular Sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S266656622200065X\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry Molecular Sciences","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S266656622200065X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles
There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO3, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t1/2 = 3 h, while the polymerization occurred with t1/2 = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate.