Thermostabilization of Ovotransferrin by Anions for Pasteurization of Liquid Egg White

Mizutani, Kimihiko; Chen, Yong; Yamashita, Honami; Hirose, Masaaki; Aibara, Shigeo

doi:10.1271/bbb.60003

Cited by 19 publications

(6 citation statements)

References 22 publications

(22 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The pH 8.0 ovotransferrin shows a denaturation temperature of 62°C and an enthalpy of 9.1 J/g (Table 1), which agrees with previous results of denaturation temperatures ranging from 60 to 64°C (Ibrahim, 2000;Mizutani, Chen, Yamashita, Hirose, & Aibara, 2006;Van Der Plancken et al, 2007a). The denaturation temperature of ovotransferrin shifted from 62.0°C (control) to 66.5°C (500 MPa), while the enthalphy decreased from 9.14 J/g (control) to 3.61 J/g (500 MPa), indicating a loss of protein structural integrity.…”

Section: Differential Scanning Calorimetry (Dsc)supporting

confidence: 91%

Effect of high pressure treatment on ovotransferrin

et al. 2012

View full text Add to dashboard Cite

Section: Differential Scanning Calorimetry (Dsc)supporting

confidence: 91%

Effect of high pressure treatment on ovotransferrin

et al. 2012

View full text Add to dashboard Cite

“…Wanatabe et al [23] and Matsudomi et al [24] have previously reported that heat-treated ovalbumin inhibited the aggregation of ovotransferrin, and the authors considered that the effect was derived from ionic interaction. In conclusion, the effects of anions on the thermostability of ovotransferrin, especially sulfate, repressed the heat aggregation of liquid egg white [25]. …”

Section: Discussionmentioning

confidence: 99%

Oral Challenge with Pasteurized Egg White from <i>Gallus domesticus</i>

Palomo

Fiandor-Román

Bobolea

et al. 2009

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Background: Since raw egg may cause digestive toxic infections, we assessed whether pasteurized raw egg white is as reliable as fresh raw egg white in the diagnosis of egg allergy. Methods: Thirty-two egg-allergic children were challenged with both pasteurized and fresh raw egg white. Open challenges were carried out with increasing doses of pasteurized raw egg white and fresh raw egg white administered every 60 min. Results: Eleven children (34.4%) had positive challenges with pasteurized raw egg white. Twenty-one children (65.62%) who tolerated pasteurized raw egg white also had a negative challenge with fresh raw egg white. If the challenge with pasteurized raw egg white resulted positive, the study was stopped. The protein profile and IgE-binding capacity of both pasteurized and fresh egg white were almost identical as observed by SDS-PAGE and IgE immunoblotting. In the IgE immunoblotting-inhibition and ImmunoCAP-inhibition assays, both extracts behaved in a similar way. Conclusions: We did not find any relevant allergenic differences between fresh and pasteurized egg white. This study supports the use of pasteurized egg white in the diagnosis of allergy to fresh raw egg proteins.

show abstract

“…Other inorganic anions are able to bind to apo-ovotransferrin including sulfate and phosphate [71][72][73][74] and to modify the temperature T m causing aggregation of ovotransferrin. This is also the case for citrate which could raise temperature T m of ovotransferrin about 5-7°C at neutral pH [75]. At pH 4.0 in citrate value of T m is close to T m in the diferric form (82°C at pH 7.5) [76].…”

Section: Discussionmentioning

confidence: 67%

Moderate conformational impact of citrate on ovotransferrin considerably increases its capacity to self-assemble at the interface

Floch-Fouéré

Pezennec

Pasco

et al. 2015

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

We have compared the behavior of ovotransferrin at the air-solution interface in the presence of a monovalent ion (acetate), or a divalent ion (citrate), the latter being known to induce conformational changes of this protein upon interaction with its iron-binding sites. We have characterised the adsorption layer at the air-water interface in terms of homogeneity, surface concentration excess and rheological properties at pH 4.0. Besides we have investigated the bulk conformation in the presence of the two anions. In the presence of citrate only, interfacial layers display well-defined domains of higher overall surface concentration suggesting multilayers adsorption. Citrate also induces higher helical content and stabilizes the protein against thermal denaturation. Hence we propose that these changes are involved in the propensity of ovotransferrin to self-assemble at the air-water interface resulting in thick and heterogeneous interfacial layer.

show abstract

Thermostabilization of Ovotransferrin by Anions for Pasteurization of Liquid Egg White

Cited by 19 publications

References 22 publications

Effect of high pressure treatment on ovotransferrin

Effect of high pressure treatment on ovotransferrin

Oral Challenge with Pasteurized Egg White from <i>Gallus domesticus</i>

Moderate conformational impact of citrate on ovotransferrin considerably increases its capacity to self-assemble at the interface

Contact Info

Product

Resources

About