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To improve the solubility, stability and bioactivity of rice bran protein (RBP) and its hydrolysates and to enhance their utilization as biological carriers, this study prepared binary nanoparticles composed of rice bran protein hydrolysates and gum arabic (GA) by taking advantage of the interaction between proteins and polysaccharides. Trypsin hydrolysate (R-t) and alkaline protease hydrolysate (R-a) of RBP were prepared and their physicochemical and structural properties were determined. Subsequently, each hydrolysate was combined with GA to prepare binary nanoparticles, which were characterized using intermolecular interaction analysis, transmission electron microscopy (TEM), X-ray diffraction (XRD), and Fourier transform infrared (FTIR) spectroscopy. The results showed that the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity of R-t and R-a were (72.82 ± 1.95)% and (66.83 ± 2.34)%, respectively, which were significantly higher than that of RBP. R-t-G nanoparticles with good stability were obtained at pH 1.4, R-t/GA ratio of 1:1 (m/m), and total polymer concentration of 4 mg/mL. R-a-G nanoparticles with good stability were obtained at pH 1.4, R-a/GA ratio of 1:2.5 (m/m), and total polymer concentration of 4 mg/mL. Electrostatic interaction played a significant role in the binding of R-t and R-a to GA, thereby stabilizing the structure of nanoparticles, and R-t-G exhibited a more stable system compared with R-a-G, with superior dispersion, thermal stability and a stronger crystal structure.
WANG B, WANG L J, LI D, et al. Effect of gum arabic on stability of oil-in-water emulsion stabilized by flaxseed and soybean protein[J]. Carbohydrate Polymers, 2011, 86(1): 343-351. DOI:10.1016/j.carbpol.2011.04.059.
WEINBRECK F, TROMP R H, DE KRUIF C G. Composition and structure of whey protein/gum arabic coacervates[J]. Biomacromolecules, 2004, 5(4): 1437-1445. DOI:10.1021/bm049970v.
GUO X N, XIONG Y L. Characteristics and functional properties of buckwheat protein-sugar Schiff base complexes[J]. LWT-Food Science and Technology, 2013, 51(2): 397-404. DOI:10.1016/j.lwt.2012.12.003.
GONG F, QIAN J Q, CHEN Y, et al. Preparation and properties of gum arabic cross-link binding nisin microparticles[J]. Carbohydrate Polymers, 2018, 197: 608-613. DOI:10.1016/j.carbpol.2018.05.080.
ZHANG L T, PAN Z, SHEN K Q, et al. Influence of ultrasoundassisted alkali treatment on the structural properties and functionalities of rice protein[J]. Journal of Cereal Science, 2018, 79: 204-209. DOI:10.1016/j.jcs.2017.10.013.
BANDYOPADHYAY K, MISRA G, GHOSH S. Preparation and characterisation of protein hydrolysates from Indian defatted rice bran meal[J]. Journal of Oleo Science, 2008, 57(1): 47-52. DOI:10.5650/jos.57.47.
RODSAMRAN P, SOTHORNVIT R. Physicochemical and functional properties of protein concentrate from by-product of coconut processing[J]. Food Chemistry, 2018, 241: 364-371. DOI:10.1016/j.foodchem.2017.08.116.
YANG J Q, ZAMANI S, LIANG L, et al. Extraction methods significantly impact pea protein composition, structure and gelling properties[J]. Food Hydrocolloids, 2021, 117: 106678. DOI:10.1016/j.foodhyd.2021.106678.
CHEN Q, CHEN X, LI S H, et al. Preparation, characterization, and in vitro antioxidant activities of natural selenium-enriched peanut protein fractions[J]. Food Bioscience, 2022, 49: 101923. DOI:10.1016/j.fbio.2022.101923.
CHEN P, WANG R M, XU B C, et al. Food emulsifier based on the interaction of casein and butyrylated dextrin for improving stability and emulsifying properties[J]. Journal of Dairy Science, 2023, 106(3): 1576-1585. DOI:10.3168/jds.2022-22532.
YEOM H J, LEE E H, HA M S, et al. Production and physicochemical properties of rice bran protein isolates prepared with autoclaving and enzymatic hydrolysis[J]. Journal of the Korean Society for Applied Biological Chemistry, 2010, 53(1): 62-70. DOI:10.3839/jksabc.2010.011.
ZHENG X Q, WANG J T, LIU X L, et al. Effect of hydrolysis time on the physicochemical and functional properties of corn glutelin by Protamex hydrolysis[J]. Food Chemistry, 2015, 172: 407-415. DOI:10.1016/j.foodchem.2014.09.080.
NAKAI S, MODLER W H. Food proteins: properties and characterization[M]. Chichester: John Wiley & Sons, 1996.
MUTILANGI W A M, PANYAM D, KILARA A. Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate[J]. Journal of Food Science, 1996, 61(2): 270-275. DOI:10.1111/j.1365-2621.1996.tb14174.x.
MUNE M A. Influence of degree of hydrolysis on the functional properties of cowpea protein hydrolysates[J]. Journal of Food Processing and Preservation, 2015, 39(6): 2386-2392. DOI:10.1111/jfpp.12488.
JIN F, WANG Y P, TANG H K, et al. Limited hydrolysis of dehulled walnut (Juglans regia L.) proteins using trypsin: functional properties and structural characteristics[J]. LWT-Food Science and Technology, 2020, 133: 110035. DOI:10.1016/j.lwt.2020.110035.
WU Z, HUANG J C, HUANG J N, et al. Lys-C/Arg-C, a more specific and efficient digestion approach for proteomics studies[J]. Analytical Chemistry, 2018, 90(16): 9700-9707. DOI:10.1021/acs.analchem.8b02448.
TAVANO O L. Protein hydrolysis using proteases: an important tool for food biotechnology[J]. Journal of Molecular Catalysis B: Enzymatic, 2013, 90: 1-11. DOI:10.1016/j.molcatb.2013.01.011.
DOUCET D, OTTER D E, GAUTHIER S F, et al. Enzyme-induced gelation of extensively hydrolyzed whey proteins by alcalase: peptide identification and determination of enzyme specificity[J]. Journal of Agricultural and Food Chemistry, 2003, 51(21): 6300-6308. DOI:10.1021/jf026242v.
ZANG X D, YUE C H, WANG Y X, et al. Effect of limited enzymatic hydrolysis on the structure and emulsifying properties of rice bran protein[J]. Journal of Cereal Science, 2019, 85: 168-174. DOI:10.1016/j.jcs.2018.09.001.
GUAN X, YAO H Y, CHEN Z X, et al. Some functional properties of oat bran protein concentrate modified by trypsin[J]. Food Chemistry, 2007, 101(1): 163-170. DOI:10.1016/j.foodchem.2006.01.011.
LEE H, YILDIZ G, DOS SANTOS L C, et al. Soy protein nanoaggregates with improved functional properties prepared by sequential pH treatment and ultrasonication[J]. Food Hydrocolloids, 2016, 55: 200-209. DOI:10.1016/j.foodhyd.2015.11.022.
YAO X L, XU K, SHU M, et al. Fabrication of iron loaded whey protein isolate/gum arabic nanoparticles and its adsorption activity on oil-water interface[J]. Food Hydrocolloids, 2021, 115: 106610. DOI:10.1016/j.foodhyd.2021.106610.
SAVADKOOHI S, BANNIKOVA A, MANTRI N, et al. Structural properties of condensed ovalbumin systems following application of high pressure[J]. Food Hydrocolloids, 2016, 53: 104-114. DOI:10.1016/j.foodhyd.2014.09.021.
CHANG C, WANG T R, HU Q B, et al. Caseinate-zein-polysaccharide complex nanoparticles as potential oral delivery vehicles for curcumin: effect of polysaccharide type and chemical crosslinking[J]. Food Hydrocolloids, 2017, 72: 254-262. DOI:10.1016/j.foodhyd.2017.05.039.
TANG Y, GAO C C, ZHANG Y, et al. Structure and functionality of cinnamaldehyde/chitosan/gum arabic complex particles[J]. Food Hydrocolloids, 2024, 146: 109220. DOI:10.1016/j.foodhyd.2023.109220.
HUANG G Q, SUN Y T, XIAO J X, et al. Complex coacervation of soybean protein isolate and chitosan[J]. Food Chemistry, 2012, 135(2): 534-539. DOI:10.1016/j.foodchem.2012.04.140.
CHEN S, LI Q K, MCCLEMENTS D J, et al. Co-delivery of curcumin and piperine in zein-carrageenan core-shell nanoparticles: formation, structure, stability and in vitro gastrointestinal digestion[J]. Food Hydrocolloids, 2020, 99: 105334. DOI:10.1016/j.foodhyd.2019.105334.
GUO Q, SU J Q, XIE W F, et al. Curcumin-loaded pea protein isolate-high methoxyl pectin complexes induced by calcium ions: characterization, stability and in vitro digestibility[J]. Food Hydrocolloids, 2020, 98: 105284. DOI:10.1016/j.foodhyd.2019.105284.
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