{"title":"Influence of the preliminary swelling of the dispersions of fibrous collagen on their ability of non‐covalent gel‐formation","authors":"E. A. Podorozhko, E. Kurskaya, L. M. Andreeva","doi":"10.1002/(SICI)1521-3803(199808)42:03/04<257::AID-FOOD257>3.3.CO;2-E","DOIUrl":null,"url":null,"abstract":"It was established that as a result of the maximum swelling (HCl, pH 3) the dispersed particles of fibrous collagen isolated from limed bovine derma irreversibly change their morphology. This results in changing the nature of supramolecular packing of protein - the transition of swollen bunches of fibrils into separate fibrils. Using method of adsorption of hydrophobic probe sodium dodecylsulphate it was found that under these conditions the significant increase in number of non-polar protein groups, able to participate in intermolecular interactions, took place. Subsequent lowering of the swelling capacity of the dispersed particles (from 19 to 2.2-2.5 g of tightly bound solvent per I g of dry collagen) resulted in the formation ofthe elastic macroisotropic gels. Hydrophobic nature of knots of gel network was confirmed by their stability in water until 62°C and destruction in concentrated solutions of urea and guanidine hydrochloride.","PeriodicalId":18955,"journal":{"name":"Nahrung-food","volume":"316 1","pages":"257-259"},"PeriodicalIF":0.0000,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nahrung-food","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<257::AID-FOOD257>3.3.CO;2-E","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
It was established that as a result of the maximum swelling (HCl, pH 3) the dispersed particles of fibrous collagen isolated from limed bovine derma irreversibly change their morphology. This results in changing the nature of supramolecular packing of protein - the transition of swollen bunches of fibrils into separate fibrils. Using method of adsorption of hydrophobic probe sodium dodecylsulphate it was found that under these conditions the significant increase in number of non-polar protein groups, able to participate in intermolecular interactions, took place. Subsequent lowering of the swelling capacity of the dispersed particles (from 19 to 2.2-2.5 g of tightly bound solvent per I g of dry collagen) resulted in the formation ofthe elastic macroisotropic gels. Hydrophobic nature of knots of gel network was confirmed by their stability in water until 62°C and destruction in concentrated solutions of urea and guanidine hydrochloride.