Effect of phlorotannins modification on the physicochemical, structural and functional properties of soybean protein isolate and controlled hydrolysates: Covalent and non-covalent interactions

被引:31
作者
Cheng, Lin [1 ]
Lian, Ziteng [1 ]
Liu, Xiuying [1 ]
Dai, Shicheng [1 ]
Li, Lanxin [1 ]
Wang, Mengmeng [1 ]
Li, Ka [1 ]
Ren, Kunyu [1 ]
Tong, Xiaohong [2 ]
Wang, Huan [1 ]
Jiang, Lianzhou [1 ]
机构
[1] Northeast Agr Univ, Coll Food Sci, Harbin 150030, Peoples R China
[2] Northeast Agr Univ, Coll Agr, Harbin 150030, Peoples R China
关键词
Soybean protein isolate; Phlorotannins; Controlled enzymatic hydrolysis; Non-covalent interaction; Covalent interaction; WHEY-PROTEIN; ANTIOXIDANT PROPERTIES; ENZYMATIC-HYDROLYSIS; INHIBITORY-ACTIVITY; FOAMING PROPERTIES; ACID; POLYPHENOLS; ANTHOCYANINS; COMPLEXATION; EXTRACTION;
D O I
10.1016/j.foodhyd.2023.109591
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
In this research, the physicochemical, structural and functional properties of soybean protein isolate (SPI) as well as controlled hydrolysates (HSPI) were investigated by treatment with different concentrations of phlorotannins (PT) (0, 0.2, 0.5, 1.0, 2.0, mg/mL) through covalent and non-covalent interactions. Native/SDS-PAGE confirmed the formation of covalent and non-covalent complexes between PT and SPI/HSPI, and the presence of covalent bonds other than disulfide bonds in the covalent complexes (C-N, C-S bonds). After binding to PT, the secondary and tertiary structures of SPI/HSPI were changed. The secondary structure of complexes was transformed from beta-sheet and beta-turn to alpha-helix and random coil, and higher rates of transformation for covalent complexes. With the increase of PT concentration, the fluorescence and UV intensity of covalent/non-covalent complexes grad-ually reduced and rose, respectively; covalent complexes had lower fluorescence and higher UV intensity at equal concentrations. The particle size and zeta-potential of covalent/non-covalent complexes rose with PT concentration, and the PDI decreased and then rose, reaching a minimum value of 0.21 (HSPI-PT covalent) at PT of 0.5 mg/mL. TEM showed PT addition induced the aggregation of the complexes to increase. Meanwhile, surface hydro-phobicity reduced while the antioxidant activity rose. Solubility, foaming activity and emulsifying activity of HSPI-PT covalent complexes first rose and then declined, and were optimal at PT of 0.5 mg/mL, with 78%, 250% and 97 m2/g, respectively. These will provide references for the improvement of soy protein properties and the application of complexes in formulated foods.
引用
收藏
页数:15
相关论文
共 71 条
[1]   Adding functionality to milk-based protein: Preparation, and physicochemical characterization of β-lactoglobulin-phenolic conjugates [J].
Abd El-Maksoud, Ahmed A. ;
Abd El-Ghany, Ismail H. ;
El-Beltagi, Hossam S. ;
Anankanbil, Sampson ;
Banerjee, Chiranjib ;
Petersen, Steen V. ;
Perez, Bianca ;
Guo, Zheng .
FOOD CHEMISTRY, 2018, 241 :281-289
[2]   Combined spectroscopic and molecular docking study on the pH dependence of molecular interactions between β-lactoglobulin and ferulic acid [J].
Abdollahi, Kourosh ;
Ince, Cameron ;
Condict, Lloyd ;
Hung, Andrew ;
Kasapis, Stefan .
FOOD HYDROCOLLOIDS, 2020, 101
[3]   Functional properties of gelatin from cuttlefish (Sepia pharaonis) skin as affected by bleaching using hydrogen peroxide [J].
Aewsiri, Tanong ;
Benjakul, Soottawat ;
Visessanguan, Wonnop .
FOOD CHEMISTRY, 2009, 115 (01) :243-249
[4]   Applications of soy protein hydrolysates in the emerging functional foods: a review [J].
Ashaolu, Tolulope Joshua .
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 2020, 55 (02) :421-428
[5]   In vitro antioxidant properties of crude extracts and compounds from brown algae [J].
Balboa, Elena M. ;
Conde, Enma ;
Moure, Andres ;
Falque, Elena ;
Dominguez, Herminia .
FOOD CHEMISTRY, 2013, 138 (2-3) :1764-1785
[6]   Effects of (-)-epigallocatechin-3-gallate incorporation on the physicochemical and oxidative stability of myofibrillar protein-soybean oil emulsions [J].
Cao, Yungang ;
Ai, Nasi ;
True, Alma D. ;
Xiong, Youling L. .
FOOD CHEMISTRY, 2018, 245 :439-445
[7]   Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study [J].
Carbonaro, M. ;
Maselli, P. ;
Nucara, A. .
AMINO ACIDS, 2012, 43 (02) :911-921
[8]   Gastrointestinal modifications and bioavailability of brown seaweed phlorotannins and effects on inflammatory markers [J].
Corona, Giulia ;
Ji, Yang ;
Anegboonlap, Prapaporn ;
Hotchkiss, Sarah ;
Gill, Chris ;
Yaqoob, Parveen ;
Spencer, Jeremy P. E. ;
Rowland, Ian .
BRITISH JOURNAL OF NUTRITION, 2016, 115 (07) :1240-1253
[9]   Peptide-peptide and protein-peptide interactions in mixtures of whey protein isolate and whey protein isolate hydrolysates [J].
Creusot, Nathalie ;
Gruppen, Harry ;
van Koningsveld, Gerrit A. ;
de Kruif, Cornelis G. ;
Voragen, Alphons G. J. .
INTERNATIONAL DAIRY JOURNAL, 2006, 16 (08) :840-849
[10]   Changes in functionalities, conformational characteristics and antioxidative capacities of sunflower protein by controlled enzymolysis and ultrasonication action [J].
Dabbour, Mokhtar ;
He, Ronghai ;
Mintah, Benjamin ;
Xiang, Jiahui ;
Ma, Haile .
ULTRASONICS SONOCHEMISTRY, 2019, 58