Influence of the preliminary swelling of the dispersions of fibrous collagen on their ability of non‐covalent gel‐formation

E. A. Podorozhko, E. Kurskaya, L. M. Andreeva
{"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.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
纤维胶原分散体初期膨胀对其非共价凝胶形成能力的影响
结果表明,由于最大的膨胀(HCl, pH 3),从石灰牛皮肤分离的纤维胶原分散颗粒不可逆地改变其形态。这就改变了蛋白质的超分子包装的性质——膨胀的原纤维束转变成单独的原纤维。利用疏水探针十二烷基硫酸钠的吸附方法发现,在这些条件下,能够参与分子间相互作用的非极性蛋白质基团的数量显著增加。随后分散颗粒的膨胀能力降低(从每1克干燥胶原蛋白19克到2.2-2.5克紧密结合的溶剂)导致弹性大各向同性凝胶的形成。凝胶网结的疏水性通过其在水中直到62°C的稳定性和在尿素和盐酸胍的浓溶液中的破坏得到证实。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Identifizierung von Glucosinolaten in Rettich (Raphanus sativus L.) und Kreuzungen aus R. sativus L. x Brassica oleracea L. (Raphanobrassica) mittels LC-MS Melanoidin formation in L-ascorbic acid-α-amino acids interaction. A comparative study Factors affecting production of melon seed kernel protein: Yield, composition and protein isolates quality The effect of the fore-crop upon winter wheat milling and baking values Improvement of the functional properties of sorghum protein by protein-polysaccharide and protein-protein complexes
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1