Preparation and characterization of oat digestive resistant peptide nanocarrier and its embedding effect on caffeic acid phenethyl ester
JIN Zulong1, FENG Siyi1, HU Yawen1, SONG Hongdong1, GUAN Xiao1*, SUN Zhu2, DAI Zhihua3
1(School of Health Science and Engineering/National Grain Industry (Urban Grain and Oil Security)Technology Innovation Center, University of Shanghai for Science and Technology, Shanghai 200093, China) 2(Inner Mongolia Yangufang Ecological Agriculture Technology (Group) Co. Ltd., Hohhot 011700, China) 3(MDO Smarter Grain Technology Co. Ltd., Shanghai 200241, China)
Abstract: In order to improve the water solubility of oat protein and its application value in the field of nano materials, oat digestion resistant peptide nanoparticles were prepared by enzymatic hydrolysis, and their ability to encapsulate hydrophobic active substances and digestion resistance were evaluated. Oat protein was digested by pepsin and trypsin to prepare oat peptide nanoparticles, which were spherical micelles with a size of 50 nm. The degree of hydrolysis of oat protein was 3.1% by pepsin digestion and 10.7% by trypsin digestion. Internal interaction analysis showed that the self-assembly of oat peptide nanoparticles was mainly driven by hydrophobic interaction, and hydrogen bond and disulfide bond played a certain role in maintaining structural stability. The study of surface activity showed that the surface of oat peptide had certain hydrophobicity and lipophilicity, and hydrolysis modification greatly enhanced the water solubility of nanoparticles. Caffeic acid phenethyl ester was used as a model drug to evaluate the drug loading performance of oat peptide nanoparticles. The results showed that entrapment efficiency was 71%, the drug loading was 3.5%, and the concentration of caffeic acid phenethyl ester in water was increased from 1.8 μg/mL to 140 μg/mL. The results of simulated digestion of drug loaded nanoparticles in vitro showed that digestive resistant peptide nanoparticles had strong digestive resistance. Steady state fluorescence spectra showed that hydrophobic interaction was the main binding force between caffeic acid phenethyl ester and peptide molecules. Oat peptide nanoparticles are good carriers to increase the solubility of hydrophobic substances.
TANG C H.Strategies to utilize naturally occurring protein architectures as nanovehicles for hydrophobic nutraceuticals[J].Food Hydrocolloids, 2021, 112:106344.
[2]
王妙玲, 张彩猛, 李兴飞, 等.水媒法燕麦分离蛋白的制备[J].食品与发酵工业, 2021, 47(23):164-168.WANG M L, ZHANG C M, LI X F, et al.Preparation of oat protein isolate by aqueous extraction method[J].Food and Fermentation Industries, 2021, 47(23):164-168.
[3]
CORSARO C, MALLAMACE D, NERI G, et al.Hydrophilicity and hydrophobicity:Key aspects for biomedical and technological purposes[J].Physica A:Statistical Mechanics and Its Applications, 2021, 580:126189.
[4]
李佳釔, 方佳兴, 李亚隆, 等.酶解大豆蛋白复合凝聚微胶囊的制备及其性质表征[J].食品与发酵工业, 2021, 47(10):1-7.LI J Y, FANG J X, LI Y L, et al.Preparation and characterization of hydrolyzed soy protein isolate microcapsules by complex coacervation[J].Food and Fermentation Industries, 2021, 47(10):1-7.
[5]
张汆, 刘洋, 陈志宏, 等.双指标评价核桃蛋白酶法增溶改性[J].中国粮油学报, 2019, 34(12):27-33;40.ZHANG C, LIU Y, CHEN Z H, et al.Enzymatic solubilization modification of walnut protein evaluated with double indices[J].Journal of the Chinese Cereals and Oils Association, 2019, 34(12):27-33;40.
[6]
郝梦真, 李欣芮, 牟瑶, 等.基于耐消化肽的核桃主要过敏原Jug r 2的线性表位筛选[J].中国食品学报, 2022, 22(2):1-10.HAO M Z, LI X R, MU Y, et al.Linear epitopes screening study of major walnut allergen Jug r 2 based on anti-digestion peptides[J].Journal of Chinese Institute of Food Science and Technology, 2022, 22(2):1-10.
[7]
魏雪林, 钟艳, 刘雪, 等.疏水性功能性因子纳米包埋体系研究进展[J].食品与发酵工业, 2021, 47(14):300-306.WEI X L, ZHONG Y, LIU X, et al.Review of hydrophobic functional factor nano-embedding system[J].Food and Fermentation Industries, 2021, 47(14):300-306.
[8]
QIN J J, YANG M, WANG Y C, et al.Interaction between caffeic acid/caffeic acid phenethyl ester and micellar casein[J].Food Chemistry, 2021, 349:129154.
[9]
MAT D J L, CATTENOZ T, SOUCHON I, et al.Monitoring protein hydrolysis by pepsin using pH-stat:In vitro gastric digestions in static and dynamic pH conditions[J].Food Chemistry, 2018, 239:268-275.
[10]
MAT D J L, LE FEUNTEUN S, MICHON C, et al.In vitro digestion of foods using pH-stat and the INFOGEST protocol:Impact of matrix structure on digestion kinetics of macronutrients, proteins and lipids[J].Food Research International, 2016, 88:226-233.
[11]
SHEN P H, ZHOU F B, ZHANG Y H, et al.Formation and characterization of soy protein nanoparticles by controlled partial enzymatic hydrolysis[J].Food Hydrocolloids, 2020, 105:105844.
[12]
ZHANG Y H, ZHAO M M, NING Z X, et al.Development of a sono-assembled, bifunctional soy peptide nanoparticle for cellular delivery of hydrophobic active cargoes[J].Journal of Agricultural and Food Chemistry, 2018, 66(16):4 208-4 218.
[13]
TIAN R, FENG J R, HUANG G, et al.Ultrasound driven conformational and physicochemical changes of soy protein hydrolysates[J].Ultrasonics Sonochemistry, 2020, 68:105202.
[14]
DONG Y B, LAN T, HUANG G, et al.Development and characterization of nanoparticles formed by soy peptide aggregate and epigallocatechin-3-gallate as an emulsion stabilizer[J].LWT, 2021, 152:112385.
[15]
JIANG P, HUANG J, BAO C, et al.Enzymatically partially hydrolyzed α-lactalbumin peptides for self-assembled micelle formation and their application for coencapsulation of multiple antioxidants[J].Journal of Agricultural and Food Chemistry, 2018, 66(49):12 921-12 930.
[16]
CHITHRANI B D, GHAZANI A A, CHAN W C W.Determining the size and shape dependence of gold nanoparticle uptake into mammalian cells[J].Nano Letters, 2006, 6(4):662-668.
[17]
LI T, LU X M, ZHANG M R, et al.Peptide-based nanomaterials:Self-assembly, properties and applications[J].Bioactive Materials, 2022, 11:268-282.
[18]
ZANGI R, ZHOU R H, BERNE B J.Urea’s action on hydrophobic interactions[J].Journal of the American Chemical Society, 2009, 131(4):1 535-1 541.
[19]
LIU K, ZHA X Q, LI Q M, et al.Hydrophobic interaction and hydrogen bonding driving the self-assembling of quinoa protein and flavonoids[J].Food Hydrocolloids, 2021, 118:106807.
[20]
CHANDLER D.Interfaces and the driving force of hydrophobic assembly[J].Nature, 2005, 437(7 059):640-647.
[21]
孔金龙, 张瑜, 朱亚萍, 等.纳米微球表面特性对载药性能影响的研究进展[J].橡塑技术与装备, 2022, 48(2):15-19.KONG J L, ZHANG Y, ZHU Y P, et al.Research progress on the effect of nanosphere surface characteristics on drug loading performance[J].China Rubber/Plastics Technology and Equipment, 2022, 48(2):15-19.
[22]
YANO Y F.Kinetics of protein unfolding at interfaces[J].Journal of Physics.Condensed Matter:An Institute of Physics Journal, 2012, 24(50):503101.
[23]
XIAO H S, HUANG L Y, ZHANG W, et al.Damage of proteins at the air/water interface:Surface tension characterizes globulin interface stability[J].International Journal of Pharmaceutics, 2020, 584:119445.
[24]
STANIMIROVA R D, MARINOVA K G, DANOV K D, et al.Competitive adsorption of the protein hydrophobin and an ionic surfactant:Parallel vs sequential adsorption and dilatational rheology[J].Colloids and Surfaces A:Physicochemical and Engineering Aspects, 2014, 457:307-317.
[25]
WEN L L, LYU M, XIAO H S, et al.Protein aggregation and performance optimization based on microconformational changes of aromatic hydrophobic regions[J].Molecular Pharmaceutics, 2018, 15(6):2 257-2 267.
[26]
邢永娜, 冯进, 李春阳.姜黄素与白首乌蛋白以及大豆分离蛋白相互作用的比较[J].食品科学, 2020, 41(10):53-60.XING Y N, FENG J, LI C Y.Comparative interactions of curcumin with Cynanchum auriculatum royle ex wight protein and soy protein isolate[J].Food Science, 2020, 41(10):53-60.
2022, Vol. 48 
