1981
DOI: 10.1080/00021369.1981.10864759
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Temperature-induced Structural Changes in Chicken Egg White Ovomucoid

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Cited by 4 publications
(9 citation statements)
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“…Antigenic and allergenic properties of egg white proteins have been intensively investigated from the viewpoints of food science, immunology, and clinical allergology ( ). Among the major egg white proteins, ovomucoid (OM) has been identified as a main causative antigen in egg allergy and this strong allegenicity is believed to depend on the stability of OM against denaturation, aggregation, and proteolytic degradation ( ).…”
Section: Introductionmentioning
confidence: 99%
“…Antigenic and allergenic properties of egg white proteins have been intensively investigated from the viewpoints of food science, immunology, and clinical allergology ( ). Among the major egg white proteins, ovomucoid (OM) has been identified as a main causative antigen in egg allergy and this strong allegenicity is believed to depend on the stability of OM against denaturation, aggregation, and proteolytic degradation ( ).…”
Section: Introductionmentioning
confidence: 99%
“…The two‐state models are typical for thermal denaturation of small compact globular proteins, involving the transition between two molecular states, usually from the native to the unfolded one. However, Matsuda et al . suggested that the simple two‐state assumption for the thermal transition of OVM must be treated with caution.…”
Section: Resultsmentioning
confidence: 99%
“…Out of the three antiparallel β bulges located in each domain of the protein model at 25 °C, the one involving Cys 95 residue (domain II) disappeared when treating the protein at 80 °C, and only the one located in domain III was identified at 100 °C. The OVM model used for the in silico investigations contains five disulfide bridges, two in each of the domains I (Cys–Cys 41 and Cys–Cys 62 ) and III (Cys 146 ‐Cys 165 and Cys 154 ‐Cys 186 ), and one in domain II (Cys 95 ‐Cys 127 ), contributing in a cooperative manner to the high stability of the protein structure at thermal treatment. The root mean square deviation (RMSD) values computed after superimposing the models treated at different temperatures were used to estimate the extent to which the stability of each domain of OVM molecule was affect.…”
Section: Resultsmentioning
confidence: 99%
“…OVA aggregation is rapid and results in the formation of thin strands (linear aggregates) or denser particles depending on the physicochemical conditions used during heating (pH, ionic strength, protein concentration) 12,14,48 . In contrast to the heat‐labile nature of OVA, OVM is highly resistant to heat thanks to its conformation of three tandem domains with intra‐ but not inter‐domain disulphide bonds 8,44,49 . Only prolonged heating at temperatures above 90°C (e.g.…”
Section: Why Do Some Patients Tolerate Heated Egg?mentioning
confidence: 99%
“…Only prolonged heating at temperatures above 90°C (e.g. boiling >30 min) results in the formation of an irreversible denatured state, indicating that OVM will remain in a natural state in more transiently heated forms of egg 8,50 . One particular situation in which OVM does aggregate is when OVM is heated in the presence of wheat.…”
Section: Why Do Some Patients Tolerate Heated Egg?mentioning
confidence: 99%