Comparative studies on thermal stability of poultry ovotransferrins
Author:
Affiliation:
1. Graduate School, Jumonji University
2. Institute of International Nutrition and Health, Jumonji University
3. Department of Food Science, Jumonji University
Publisher
Japanese Society for Food Science and Technology
Subject
Marketing,Industrial and Manufacturing Engineering,General Chemical Engineering,Food Science,Biotechnology
Link
https://www.jstage.jst.go.jp/article/fstr/28/6/28_FSTR-D-22-00101/_pdf
Reference21 articles.
1. Cunningham, F.E. and Lineweaver, H. (1965). Stabilization of egg white proteins to pasteurization temperatures above 60 °C. Food Technol. Biotechnol., 19, 1442-1447.
2. Donovan, J.W. and Ross, K.D. (1975). Iron binding to conalbumin calorimetric evidence for two distinct species with one bound iron atom. J. Biol. Chem., 250, 6026-6031.
3. Donovan, J.W., Mapes, C.J., Davis, J.G. and Garibaldi, J.G. (1975). A differential scanning calorimetric study of the stability of egg white to heat denaturation. J. Sci. Food Agric., 26, 73-83.
4. Feeney, R. E., Anderson, J. S., Azari, P. R., Bennett, N., Rhodes, M. B. (1960). The comparative biochemistry of avian egg white proteins. J. Biol. Chem., 235, 2307-2311.
5. Huynh, K. and Partch, C.L. (2016). Analysis of protein stability and ligand interactions by thermal shift assay. Curr. Protoc. Protein Sci., 79, 28.9.1-28.9.14.
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