Involvement of Ovotransferrin in the Thermally Induced Gelation of Egg White at around 65℃
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概要
- 論文の詳細を見る
Egg white forms a soft opaque gel at around 65℃. An analysis of the turbidity appearance in the presence or absence of iron and polyacrylamide gel electrophoresis of the precipitated proteins after thermal treatment revealed ovotransferrin to be the major component involved in thermal gelation at around 65℃. The storage modulus of the thermally induced gel of purified ovotransferrin reinforced this conclusion.
- 社団法人日本農芸化学会の論文
- 1998-03-23
著者
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Hirose Masaaki
The Research Institute For Food Science Kyoto Univesity
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YAMASHITA Honami
The Research Institute for Food Science, Kyoto University
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Hirose Masaaki
The Research Institute For Food Science Kyoto University
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ISHIBASHI Junko
The Research Institute for Food Science, Kyoto University
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HONG Youn-Ho
Department of Food and Nutrition, Chonnam National University
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Hong Youn-ho
Department Of Food And Nutrition Chonnam National University
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Ishibashi Junko
The Research Institute For Food Science Kyoto University
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Yamashita Honami
The Research Institute For Food Science Kyoto University
関連論文
- Structural Characteristics of the Disulfide-reduced Ovotransferrin N-Lobe Analyzed by Protein Fragmentation
- Refolding of Urea-Denatured Ovalbumin That Comprises Non-Native Disulfide Isomers
- Role of the Intrachain Disulfide Bond of Ovalbumin during Conversion into S-Ovalbumin
- Periplasmic Secretion of Functional Ovotransferrin N-Lobe in Escherichia coli
- Structural Properties of Recombinant Ovalbumin and Its Transformation into a Thermostabilized Form by Alkaline Treatment
- Thiol-dependent Gelation of Conalbumin in the Presence of Denaturant(Food & Nutrition)
- Thiol-dependent Gelation of Conalbumin: Use of Thiosalicylic Acid and Its Removal from the Gel(Food & Nutrition)
- Effects of Anions on the Thiol-dependent Gelation of Conalbumin(Food & Nutrition)
- Conformation Changes and Subsequent Gelation of Conalbumin by a Thiol Reagent(Biological Chemistry)
- Limited Proteolysis of Disulfide-reduced Ovalbumin by Subtilisin
- Conformational State of Disulfide-Reduced Ovalbumin at Acidic pH
- Involvement of Ovotransferrin in the Thermally Induced Gelation of Egg White at around 65℃
- Thiol-dependent Gelation of the Domain I-truncated Fragment of Bovine Serum Albumin
- Highly Ordered Molten Globule-Like State of Ovalbumin at Acidic pH: Native-Like Fragmentation by Protease and Selective Modification of Cys367 with Dithiodipyridine
- The Structural Mechanism for Iron Uptake and Release by Transferrins
- Roles of the Domain I Segment in Emulsifying Properties of Bovine Serum Albumin