Globular proteins as soft particles for stabilizing emulsions: Concepts and strategies

被引:144
作者
Tang, Chuan-He [1 ,2 ]
机构
[1] South China Univ Technol, Dept Food Sci & Technol, Guangzhou 510640, Peoples R China
[2] BTBU, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Beijing, Peoples R China
基金
中国国家自然科学基金;
关键词
Globular proteins; Soft particles; Pickering emulsions; Emulsification performance; Interfacial stabilization; High internal phase emulsions (HIPEs); Structural stability; IN-WATER EMULSIONS; EMULSIFYING PROPERTIES; SOY PROTEIN; CONFORMATIONAL-CHANGES; INTERFACIAL PROPERTIES; RHEOLOGICAL PROPERTIES; BETA-LACTOGLOBULIN; ALPHA-LACTALBUMIN; CRYSTAL-STRUCTURE; FOOD;
D O I
10.1016/j.foodhyd.2020.105664
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Many globular proteins are good emulsifiers or stabilizers for oil-in-water emulsions. It is generally recognized in the field that globular proteins tend to undergo a structural unfolding and rearrangement when adsorbed at oilwater interface, and as a result, a viscoelastic interfacial film is formed. However, more evidences are fast accumulating in recent years to show that globular proteins exhibit a great potential to perform as soft particles for stabilizing emulsions. This review mainly presents the state-of-the-art knowledge about the emulsification performance and interfacial stabilization of globular proteins, achieved in the recent several years, especially by our research group. A critical summary of current understanding about the emulsification and interfacial properties of globular proteins, as well as some limitations existing for the knowledge, is first presented. Then, the concepts, structural requirements and strategies for globular proteins as soft particles for stabilizing emulsions or high internal phase emulsions (HIPEs) are introduced in details. The effective strategies include, but are not limited to, choosing native glycated globular proteins or glycation with carbohydrates, strengthening structural stability of globular proteins by polyols (dissaccharides in particular), and pH adjustment. Finally, some advantages and limitations of globular proteins as soft particles for stabilizing emulsions or HIPEs are discussed. Due to the increasing interests from food industry and health wareness from consumers in developing safe emulsifiers, this review is of crucial importance for the understanding of the role of structural characteristics in emlusification and emulsion stabilization of globular proteins, as well as their ultilization as emulsifers/stabilizers in food industry.
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页数:15
相关论文
共 95 条
[1]   Molecular Effects of Concentrated Solutes on Protein Hydration, Dynamics, and Electrostatics [J].
Abriata, Luciano A. ;
Spiga, Enrico ;
Dal Peraro, Matteo .
BIOPHYSICAL JOURNAL, 2016, 111 (04) :743-755
[2]  
ACHARYA KR, 1991, J MOL BIOL, V221, P571
[3]   Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering [J].
Ajito, Satoshi ;
Hirai, Mitsuhiro ;
Iwase, Hiroki ;
Shimizu, Nobutaka ;
Igarashi, Noriyuki ;
Ohta, Noboru .
PHYSICA B-CONDENSED MATTER, 2018, 551 :249-255
[4]   Sugar-Mediated Stabilization of Protein against Chemical or Thermal Denaturation [J].
Ajito, Satoshi ;
Iwase, Hiroki ;
Takata, Shin-ichi ;
Hirai, Mitsuhiro .
JOURNAL OF PHYSICAL CHEMISTRY B, 2018, 122 (37) :8685-8697
[5]   EMULSIFYING PROPERTIES OF SOY PROTEIN - CHARACTERISTICS OF 7S AND 11S PROTEINS [J].
AOKI, H ;
TANEYAMA, O ;
INAMI, M .
JOURNAL OF FOOD SCIENCE, 1980, 45 (03) :534-&
[6]   Emulsions stabilised solely by colloidal particles [J].
Aveyard, R ;
Binks, BP ;
Clint, JH .
ADVANCES IN COLLOID AND INTERFACE SCIENCE, 2003, 100 :503-546
[7]   Stabilization of beta-lactoglobulin by polyols and sugars against temperature-induced denaturation involves diverse and specific structural regions of the protein [J].
Barbiroli, Alberto ;
Marengo, Mauro ;
Fessas, Dimitrios ;
Ragg, Enzio ;
Renzetti, Stefano ;
Bonomi, Francesco ;
Iametti, Stefania .
FOOD CHEMISTRY, 2017, 234 :155-162
[8]   STABILITY-CRITERIA FOR EMULSIONS [J].
BIBETTE, J ;
MORSE, DC ;
WITTEN, TA ;
WEITZ, DA .
PHYSICAL REVIEW LETTERS, 1992, 69 (16) :2439-2442
[9]   Particles as surfactants - similarities and differences [J].
Binks, BP .
CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 2002, 7 (1-2) :21-41
[10]   STRUCTURE OF HEN EGG-WHITE LYSOZYME - A 3-DIMENSIONAL FOURIER SYNTHESIS AT 2A RESOLUTION [J].
BLAKE, CCF ;
KOENIG, DF ;
MAIR, GA ;
NORTH, ACT ;
PHILLIPS, DC ;
SARMA, VR .
NATURE, 1965, 206 (4986) :757-&