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Whether ovalbumin performs as a particulate or polymeric emulsifier is largely determined by pH

文献类型: 外文期刊

作者: Xu, Yan-Teng 1 ; Wang, Yu-Han 1 ; Chen, Fei-Ping 2 ; Tang, Chuan-He 1 ;

作者机构: 1.South China Univ Technol, Dept Food Sci & Technol, Guangzhou 510640, Peoples R China

2.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Guangzhou, Peoples R China

3.Minist Agr & Rural Affairs, Key Lab Funct Foods, Guangzhou, Peoples R China

4.Guangdong Key Lab Agr Prod Proc, Guangzhou, Peoples R China

5.Overseas Expertise Intro Ctr Discipline Innovat F, Ctr 111, Guangzhou 510640, Peoples R China

关键词: Ovalbumin; Emulsification property; Interfacial stabilization; Pickering stabilizer; High internal phase emulsions (HIPEs)

期刊名称:FOOD HYDROCOLLOIDS ( 影响因子:9.147; 五年影响因子:9.169 )

ISSN: 0268-005X

年卷期: 2020 年 103 卷

页码:

收录情况: SCI

摘要: Although it has been recognized that the emulsifying properties of ovalbumin (OVA), an important glycoprotein in egg white, are affected by pH, its pH-dependent structural characteristics still remain undetermined. The work demonstrated that pH played a crucial role in the emulsification of OVA, as a polymeric or particulate emulsifier; and at pH below its isoelectric point, OVA acted as a particulate emulsifier, while at strong alkali pHs, it was more like a polymeric emulsifier. The structural and physicochemical properties of OVA at different pHs of 2.0-12.0 were first evaluated in terms of particle size (and morphology), zeta-potential, tertiary and secondary conformations, and solubility. The results indicated that at pH 3.0, OVA tended to form highly aggregated spheres with a strong structural integrity, while at pH 11.0, its structure became unfolded and flexible. The emulsification performance and interfacial stabilization of OVA at three selected pHs (3.0, 7.0 and 11.0) were evaluated on the emulsions at oil volume fractions of 0.3 and 0.8. It was demonstrated that in both the cases, aggregated OVA spheres at pH 3.0 exhibited much better emulsification performance and interfacial stabilization than OVA at pH 7.0, while the enhancement of conformation flexibility by increasing pH from 7.0 to 11.0 did not produce significant influence. The findings would be of great importance for extending the knowledge about the structural basis of the emulsification and interfacial behavior of OVA, as well as for guiding the development of food emulsion formulations with OVA or egg white as the emulsifier or stabilizer.

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