研究报告

超声对青稞蛋白理化性质和消化特性的影响

  • 陈玉玉 ,
  • 石梦梦 ,
  • 王月琴 ,
  • 周明 ,
  • 张春红 ,
  • 曹洪伟 ,
  • 宋洪东 ,
  • 管骁
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  • 1(上海理工大学 健康科学与工程学院,上海,200093)
    2(西藏喜马拉雅生态科技股份有限公司,西藏 日喀则,857000)
    3(中国人民解放军海军特色医学中心,上海,200052)
    4(国家粮食产业(城市粮油保障)技术创新中心,上海,200093)
第一作者:硕士研究生(曹洪伟讲师为通信作者,E-mail:chwei@usst.edu.cn)

收稿日期: 2023-02-11

  修回日期: 2023-03-22

  网络出版日期: 2024-06-11

基金资助

上海市科学技术委员会国内合作项目(21015801100);中国科学技术协会青年人才托举工程(2021QNRC001)

Effect of ultrasound on physicochemical properties and digestive characteristics of barley protein

  • CHEN Yuyu ,
  • SHI Mengmeng ,
  • WANG Yueqin ,
  • ZHOU Ming ,
  • ZHANG Chunhong ,
  • CAO Hongwei ,
  • SONG Hongdong ,
  • GUAN Xiao
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  • 1(School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China)
    2(Tibet Himalayan Ecological Technology Co.Ltd., Shigatse 857000, China)
    3(Chinese People's Liberation Army Naval Characteristic Medical Center, Shanghai 200052, China)
    4(National Grain Industry (Urban Grain and Oil Security) Technology Innovation Center, Shanghai 200093, China)

Received date: 2023-02-11

  Revised date: 2023-03-22

  Online published: 2024-06-11

摘要

为改善青稞蛋白的理化性质和消化特性,研究了超声波作用下青稞蛋白的理化性质、体外消化特性及其内部微观结构的变化,用600 W超声对青稞蛋白进行不同时间的超声改性处理。结果表明,超声20 min时青稞蛋白的溶解度、起泡性和乳化性分别提高了23.82%、21.54%、6.95 m2/g;短时间(10、20 min)的超声处理有利于蛋白质分子结构的展开解离,减小平均粒径和表观黏度;而长时间的超声作用又会诱导蛋白质重聚集,增大青稞蛋白的平均粒径和表观黏度。由青稞蛋白微观结构的观察实验以及紫外和荧光分析结果可知,超声20 min时青稞蛋白的结构更加疏松多孔且蛋白颗粒较小,促使蛋白质分子三级结构的伸展及其内部极性区域的展开,紫外吸光度和荧光强度增大,有利于改善青稞蛋白的理化性质。此外,超声波的空化作用促使青稞蛋白暴露更多接触位点,显著提高了青稞蛋白的体外消化率,从原来的68.47%提高到79.3%。综上所述,600 W超声处理20 min可明显改善青稞蛋白的理化性质,促进青稞蛋白的体外消化吸收,对增强青稞蛋白产品的品质特性具有重要意义。

本文引用格式

陈玉玉 , 石梦梦 , 王月琴 , 周明 , 张春红 , 曹洪伟 , 宋洪东 , 管骁 . 超声对青稞蛋白理化性质和消化特性的影响[J]. 食品与发酵工业, 2024 , 50(8) : 68 -75 . DOI: 10.13995/j.cnki.11-1802/ts.035101

Abstract

To improve the physicochemical properties and the digestive characteristics of barley protein, the changes of physicochemical properties, in vitro digestive characteristics and internal microstructure of barley protein under the action of the ultrasonic wave were studied, using 600 W ultrasound to modify barley protein at different times.Results showed that the solubility, foaming, and emulsification of barley protein increased by 23.82%, 21.54%, and 6.95 m2/g, respectively when the ultrasonic time was 20 min.Then, short time (10, 20 min) ultrasonic treatment was conducive to the development of protein molecular structure and dissociation into small particles, reducing the average particle size and apparent viscosity.However, further extension of ultrasonic time induced protein reaggregation, increasing the average particle size and apparent viscosity of barley protein.It could be seen from the observation experiment of the microstructure of barley protein and the results of ultraviolet or fluorescence analysis that after 20 minutes of ultrasound, the structure of barley protein was more porous and smaller, promoting the tertiary structure of the protein molecule to extend and the polar regions within it to unfold, significantly improving the physical and chemical properties of barley protein.In addition, ultrasonic cavitation promoted the barley protein to expose more contact sites, which dramatically improved the in vitro digestibility of barley protein from the original 68.47% to 79.3%.In summary, the 600 W ultrasonic treatment for 20 min can obviously improve the physicochemical properties, and promote the digestion and absorption of barley protein in vitro, which is of great significance to enhance the quality characteristics of barley protein products.

参考文献

[1] 杨希娟, 党斌, 吴昆仑, 等.青稞蛋白的超声波辅助提取工艺及其功能特性研究[J].中国食品学报, 2013, 13(6):48-56.
YANG X J, DANG B, WU K L, et al.Study on functional properties and hulless barley protein by ulrasonic-assisted extraction[J].Journal of Chinese Institute of Food Science and Technology, 2013, 13(6):48-56.
[2] 刘远方, 李萌萌, 刘远晓, 等.功率超声波及其在食品工业中的降解应用研究进展[J].食品与发酵工业, 2018, 44(10):283-289.
LIU Y F, LI M M, LIU Y X, et al.Progress in power ultrasound method and its application in degradation process in food industry[J].Food and Fermentation Industries, 2018, 44(10):283-289.
[3] DU Y, LIANG F, CHEN Z X, et al.Effects of decolorization on aggregation behavior of highland barley proteins:Comparison with wheat proteins[J].Food Research International, 2022, 160:111712.
[4] JIN J, OKAGU O D, YAGOUB A E A, et al.Effects of sonication on the in vitro digestibility and structural properties of buckwheat protein isolates[J].Ultrasonics Sonochemistry, 2021, 70:105348.
[5] HU H, WU J H, LI-CHAN E C Y, et al.Effects of ultrasound on structural and physical properties of soy protein isolate dispersions[J].Food Hydrocolloids, 2013, 30(2):647-655.
[6] MARTINI S, POTTER R, WALSH M K.Optimizing the use of power ultrasound to decrease turbidity in whey protein suspensions[J].Food Research International, 2010, 43(10):2444-2451.
[7] DABBOUR M, HE R, MINTAH B, et al.Changes in functionalities, conformational characteristics and antioxidative capacities of sunflower protein by controlled enzymolysis and ultrasonication action[J].Ultrasonics Sonochemistry, 2019, 58:104625.
[8] GAO K, ZHA F C, YANG Z Y, et al.Structure characteristics and functionality of water-soluble fraction from high-intensity ultrasound treated pea protein isolate[J].Food Hydrocolloids, 2022, 125:107409.
[9] ZHANG T H, ZHAO Y L, TIAN X, et al.Effect of ultrasound pretreatment on structural, physicochemical, rheological and gelation properties of transglutaminase cross-linked whey protein soluble aggregates[J].Ultrasonics Sonochemistry, 2021, 74:105553.
[10] FLORES-JIMÉNEZ N T, ULLOA J A, URÍAS-SILVAS J E, et al.Influence of high-intensity ultrasound on physicochemical and functional properties of a guamuchil Pithecellobium dulce (Roxb.) seed protein isolate[J].Ultrasonics Sonochemistry, 2022, 84:105976.
[11] WANG Y, ZHOU Y, LI P J, et al.Combined effect of CaCl2 and high pressure processing on the solubility of chicken breast myofibrillar proteins under sodium-reduced conditions[J].Food Chemistry, 2018, 269:236-243.
[12] HUANG L R, DING X N, Li Y L, et al.The aggregation, structures and emulsifying properties of soybean protein isolate induced by ultrasound and acid[J].Food Chemistry, 2019, 279:114-119.
[13] WANG X, LIN Q Q, YE A Q, et al.Flocculation of oil-in-water emulsions stabilised by milk protein ingredients under gastric conditions:Impact on in vitro intestinal lipid digestion[J].Food Hydrocolloids, 2019, 88:272-282.
[14] JIANG S, ZHANG M, LIU H, et al.Ultrasound treatment can increase digestibility of myofibrillar protein of pork with modified atmosphere packaging[J].Food Chemistry, 2022, 377:131811.
[15] RAHMAN M M, BYANJU B, GREWELL D, et al.High-power sonication of soy proteins:Hydroxyl radicals and their effects on protein structure[J].Ultrasonics Sonochemistry, 2020, 64:105019.
[16] YAN S Z, XU J W, ZHANG S, et al.Effects of flexibility and surface hydrophobicity on emulsifying properties:Ultrasound-treated soybean protein isolate[J].LWT, 2021, 142:110881.
[17] GUPTA A, SHARMA S, SURASANI V K R, et al.Quinoa protein isolate supplemented pasta:Nutritional, physical, textural and morphological characterization[J].LWT, 2021, 135:110045.
[18] CUI Q, ZHANG A Q, LI R, et al.Ultrasonic treatment affects emulsifying properties and molecular flexibility of soybean protein isolate-glucose conjugates[J].Food Bioscience, 2020, 38:100747.
[19] FIGUEROA-GONZÁLEZ J J, LOBATO-CALLEROS C, VERNON-CARTER E J, et al.Modifying the structure, physicochemical properties, and foaming ability of amaranth protein by dual pH-shifting and ultrasound treatments[J].LWT-Food Science Technology, 2022, 153:112561.
[20] WANG Y T, WANG S S, LI R, et al.Effects of combined treatment with ultrasound and pH shifting on foaming properties of chickpea protein isolate[J].Food Hydrocolloids, 2022, 124:107351.
[21] SHOKRI S, JAVANMARDI F, MOHAMMADI M, et al.Effects of ultrasound on the techno-functional properties of milk proteins:A systematic review[J].Ultrasonics Sonochemistry, 2022, 83:105938.
[22] HU A N, LI L.Effect mechanism of ultrasound pretreatment on fibrillation kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils[J].Ultrasonics Sonochemistry, 2021, 78:105741
[23] O'SULLIVAN J, MURRAY B, FLYNN C, et al.The effect of ultrasound treatment on the structural, physical and emulsifying properties of animal and vegetable proteins[J].Food Hydrocolloids, 2016, 53:141-154.
[24] ZHAO X Q, FAN X X, SHAO X Q, et al.Modifying the physicochemical properties, solubility and foaming capacity of milk proteins by ultrasound-assisted alkaline pH-shifting treatment[J].Ultrasonics Sonochemistry, 2022, 88:106089.
[25] MALIK M A, SAINI C S.Rheological and structural properties of protein isolates extracted from dephenolized sunflower meal:Effect of high intensity ultrasound[J].Food Hydrocolloids, 2018, 81:229-241.
[26] AMADEO B B, POLLET J, CHEN W H, et al.A method to probe protein structure from UV absorbance spectra[J].Analytical Biochemistry, 2019, 587:1-8.
[27] YANG X, LI Y L, LI S Y, et al.Effects of multi-frequency ultrasound pretreatment under low power density on the enzymolysis and the structure characterization of defatted wheat germ protein[J].Ultrasonics Sonochemistry, 2017, 38:410-420.
[28] SHEN L, TANG C H.Microfluidization as a potential technique to modify surface properties of soy protein isolate[J].Food Research International, 2012, 48(1):108-118.
[29] DONG Z Y, LI M Y, TIAN G, et al.Effects of ultrasonic pretreatment on the structure and functionality of chicken bone protein prepared by enzymatic method[J].Food Chemistry, 2019, 299:125103.
[30] QU W J, MA H L, LIU B, et al.Enzymolysis reaction kinetics and thermodynamics of defatted wheat germ protein with ultrasonic pretreatment[J].Ultrasonics Sonochemistry, 2013, 20(6):1408-1413.
[31] KHATKAR A B, KAUR A, KHATKAR S K.Restructuring of soy protein employing ultrasound:Effect on hydration, gelation, thermal, in vitro protein digestibility and structural attributes[J].LWT, 2020, 132:109781.
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