Succinylation Modified Ovalbumin: Structural, Interfacial, and Functional Properties

被引：23
作者：
Hu, Gan [1 ]
Zhang, Jiemin [1 ]
Wang, Qi [1 ]
Ma, Meihu [1 ]
Ma, Lulu [2 ]
Li, Shugang [2 ]
机构：
[1] Huazhong Agr Univ, Coll Food Sci & Technol, Natl Res & Dev Ctr Egg Proc, Wuhan 430070, Peoples R China
[2] Hefei Univ Technol, Sch Food & Biol Engn, Hefei 230009, Peoples R China
来源：
FOODS | 2022年 / 11卷 / 18期
关键词：
ovalbumin; succinylation; physicochemical property; structure; functional property; HIGH-INTENSITY ULTRASOUND; PHYSICOCHEMICAL PROPERTIES; PROTEIN ISOLATE; SOY PROTEIN; IMPROVEMENT; MECHANISM;
D O I：
10.3390/foods11182724
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
In this study, ovalbumin (OVA) was succinylated with the addition of different levels of succinic anhydride, and the structural and functional properties of succinylated OVA (SOVA) were investigated. SDS-PAGE and FTIR spectrum confirmed the covalent attachment of the succinyl group to OVA. Thermal stability and the absolute value of zeta potential (pH 6.0) of SOVA were enhanced by 14.90% and 76.77% higher than that of the native OVA (NOVA), respectively. Circular dichroism (CD) spectra demonstrated that the succinylation decreased the alpha-helix and increased beta-sheet content to 21.31% and 43.28%, respectively. The content of free sulfhydryl groups increased and intrinsic fluorescence spectra suggested the SOVA became more unfolded and flexible as the degree of succinylation enhanced. Furthermore, succinylation effectively enhanced the solubility and decreased the interface tension (oil-water and air-water interface) of OVA. Compared to NOVA, the emulsifying activity and stability of SOVA were increased by 1.6 times and 1.2 times, respectively, and foaming capacity and stability were enhanced by 2.7 times and 1.5 times, respectively.
引用
收藏
页数：13
相关论文
共 44 条
  • [1] Chemical modifications and their effects on gluten protein: An extensive review
    Abedi, E.
    Pourmohammadi, K.
    [J]. FOOD CHEMISTRY, 2021, 343
  • [2] [Anonymous], 2011, FOOD ADDITIVES DATA, DOI DOI 10.1002/9781444323351
  • [3] Infrared Microspectroscopy Applications - Review
    Bunaciu, Andrei A.
    Fleschin, Serban
    Aboul-Enein, Hassan Y.
    [J]. CURRENT ANALYTICAL CHEMISTRY, 2014, 10 (01) : 132 - 139
  • [4] Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation
    Charoensuk, Danai
    Brannan, Robert G.
    Chanasattru, Wanlop
    Chaiyasit, Wilailuk
    [J]. INTERNATIONAL JOURNAL OF FOOD PROPERTIES, 2018, 21 (01) : 1633 - 1645
  • [5] A natural-based polymeric hydrogel based on functionalized soy protein
    Cuadri, A. A.
    Bengoechea, C.
    Romero, A.
    Guerrero, A.
    [J]. EUROPEAN POLYMER JOURNAL, 2016, 85 : 164 - 174
  • [6] Investigating the effect of temperature on the formation and stabilization of ovalbumin foams
    Delahaije, Roy J. B. M.
    Lech, Frederik J.
    Wierenga, Peter A.
    [J]. FOOD HYDROCOLLOIDS, 2019, 91 : 263 - 274
  • [7] HIGH-PRESSURE EFFECTS ON BETA-LACTOGLOBULIN INTERACTIONS WITH LIGANDS STUDIED BY FLUORESCENCE
    DUFOUR, E
    HOA, GHB
    HAERTLE, T
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1994, 1206 (02): : 166 - 172
  • [8] A COLORIMETRIC METHOD FOR DETERMINING LOW CONCENTRATIONS OF MERCAPTANS
    ELLMAN, GL
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1958, 74 (02) : 443 - 450
  • [9] Improved oxidative stability of fish oil emulsion by grafted ovalbumin-catechin conjugates
    Feng, Jin
    Cai, He
    Wang, Hua
    Li, Chunyang
    Liu, Songbai
    [J]. FOOD CHEMISTRY, 2018, 241 : 60 - 69
  • [10] Gliadin nanoparticles stabilized by a combination of thermally denatured ovalbumin with gemini dodecyl O-glucoside: The modulating effect of cosurfactant
    Feng, Jin
    Wu, Shanshan
    Wang, Hua
    Liu, Songbai
    [J]. COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, 2017, 516 : 94 - 105
12345