Chemical and structural changes in preserved white egg during pickled by vacuum technology

Food Science and Technology International

Volumn 19, Issue 2, 2013, Pages 123-131

  Ji, Ling ^a   Liu, Huiping ^a   Cao, Chunling ^a   Liu, Pingwei ^a   Wang, Hao ^a   Wang, Hongni ^a  

^a TIANJIN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

chemical properties; circular dichroism; Fourier transformation infrared spectroscopy; Preserved egg white; secondary structure

Indexed keywords

ALKALINE SOLUTIONS; EGG WHITE; FOURIER TRANSFORMATIONS; SECONDARY STRUCTURAL ELEMENTS; SECONDARY STRUCTURES; SIGNIFICANT DIFFERENCES; SURFACE HYDROPHOBICITY; UNORDERED STRUCTURE;

ALKALINITY; CHEMICAL PROPERTIES; COVALENT BONDS; DICHROISM; ELECTROPHORESIS; FOURIER TRANSFORMS; HYDROPHOBICITY; INFRARED SPECTROSCOPY; PROTEINS; VACUUM TECHNOLOGY;

FOOD PRESERVATION;

DISULFIDE; EGG WHITE; OVALBUMIN;

ANIMAL; ARTICLE; CHEMICAL PHENOMENA; CHEMISTRY; CIRCULAR DICHROISM; DUCK; EGG; FOOD HANDLING; FOOD PRESERVATION; INFRARED SPECTROSCOPY; METHODOLOGY; PH; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY; VACUUM;

ANIMALS; CIRCULAR DICHROISM; DISULFIDES; DUCKS; EGG WHITE; EGGS; FOOD PRESERVATION; FOOD TECHNOLOGY; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; OVALBUMIN; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; VACUUM;

MLCS; MLOWN;

EID: 84875699522     PISSN: 10820132     EISSN: 15321738     Source Type: Journal    
DOI: 10.1177/1082013212442186     Document Type: Article

References (23)

1. Alizadeh-Pasdar N, Li-Chan ECY. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agriculture and Food Chemistry. 2000 ; 48 (2). 328-334
2. Alomirah HF, Alli I, Gibbs BF, Konishi Y. Identification of proteolytic products as indicators of quality in ground and whole meat. Journal of Food Quality. 1998 ; 21 (4). 299-316
3. Belitz HD, Grosch W, Schieberle P Food Chemistry. Belitz HD Grosch W Schieberle P, ed. Heidelberg: Springer ; 2009: 546-561.
4. Benjakul S, Visessanguan W, Ishizaki S, Tanaka M. Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. Journal of Food Science. 2001 ; 66 (9). 1311-1318
5. Chi SP, Tseng KH. Physicochemical properties of salted pickled yolk from duck and chicken eggs. Journal of Food Science. 1998 ; 63 (1). 27-30
6. De Jongh HH, Goormaghtigh EJ, Ruysschaert M. Association and interactions of pulmonary surfactant lipids and proteins in model membranes at the air-water interface. Analytical Biochemistry. 1996 ; 242 (3). 95-103
7. Ellman GL. Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics. 1959 ; 82 (1). 70-77
8. Goormaghtigh E, Cabiaux V, Ruysschaert JM. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. European Journal of Biochemistry. 1990 ; 193 (2). 409-420
9. Kalab M. Factors affecting the Ellman determination of sulfhydryl groups in skimmilk powder and gels. Journal of Dairy Science. 1970 ; 53 (6). 711-718
10. Lai KM, Chi SP, Ko WC. Changes in yolk states of duck egg during long-term brining. Journal of Agricultural and Food Chemistry. 1999 ; 47 (2). 733-736
11. Lai KM, Chuang YS, Chou YC, Hsu YC, Cheng YC, Shi CY, et al. Changes in physicochemical properties of egg white and yolk proteins from duck shell eggs due to hydrostatic pressure treatment. Poultry science. 2010 ; 89 (4). 729-737
12. Li J, Hsieh YP. Traditional Chinese food technology and cuisine. Asia Pacific Journal of Clinical Nutrition. 2004 ; 13 (2). 147-155
13. Linden G, Lorient D New Ingredients in Food Processing: Biochemistry and Agriculture. Boca Raton, FL: RC Press ; 2000 :
14. Matsuo K, Sakurada Y, Yonehara R, Kataoka M, Gekko K. Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy. Biophysical Journal. 2007 ; 92 (11). 4088-4096
15. Mine Y. Recent advances in the understanding of egg white protein functionality. Trends in Food Science and Technology. 1995 ; 6 (7). 225-232
16. Onda M, Tatsumi E, Takahashi N, Hirose M. Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Journal of Biochemistry. 1997 ; 122 (1). 83-89
17. Osuga DT, Feeney RE Toxic Constituents of Animal Foodstuffs. Liencr IE, ed. New York: Academic Press ; 1974: 39-71.
18. Plancken I, Van Loey A, Hendrickx ME. Effect of heat-treatment on the physico-chemical properties of egg white proteins: a kinetic study. Journal of Agricultural and Food Chemistry. 2006 ; 53 (14). 5726-5733
19. Prestrelski S, Tedeschi N, Arakawa T, Carpenter J. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophysical Journal. 1993 ; 65 (2). 661-671
20. Silva JL, Weber G. Pressure stability of proteins. Annual Review of Physical Chemistry. 1993 ; 44 (1). 89-113
21. Smith D, Galazka VB, Wellner N, Sumner IG. High pressure unfolding of ovalbumin. Internatonal Journal of Food Science and Technology. 2000 ; 35 (4). 361-370
22. Sun Y, Hayakawa S. Thermally induced aggregation in mixtures of α-lactalbumin with ovobumins from different avian species. Journal of Agricultural and Food Chemistry. 2001 ; 49 (5). 2511-2517
23. Van der Plancken I, Van Loey A, Hendrickx MEG. Changes in sulfhydryl content of egg white proteins due to heat and pressure treatment. Journal of Agriculture and Food Chemistry. 2005 ; 53 (14). 5726-5733