用户名: 密码: 验证码:
超声处理对蛋清蛋白结构性质及蛋清液起泡性的影响
详细信息    查看全文 | 推荐本文 |
  • 英文篇名:Effect of Ultrasonic Treatment on Protein Structure and Physicochemical and Foaming Properties of Liquid Egg White
  • 作者:李弓中 ; 赵英 ; 王俊彤 ; 迟玉杰
  • 英文作者:LI Gongzhong;ZHAO Ying;WANG Juntong;CHI Yujie;School of Food Science, Northeast Agricultural University;
  • 关键词:蛋清液 ; 脉冲式超声 ; 起泡性 ; 结构性质 ; 相关性分析
  • 英文关键词:liquid egg white;;pulsed ultrasonic;;foaming properties;;structural properties;;correlation analysis
  • 中文刊名:SPKX
  • 英文刊名:Food Science
  • 机构:东北农业大学食品学院;
  • 出版日期:2018-08-24 10:01
  • 出版单位:食品科学
  • 年:2019
  • 期:v.40;No.598
  • 基金:“十三五”国家重点研发计划重点专项(2018YFD0400304);; 现代农业产业技术体系建设专项(CARS-40-K25)
  • 语种:中文;
  • 页:SPKX201909011
  • 页数:8
  • CN:09
  • ISSN:11-2206/TS
  • 分类号:76-83
摘要
研究脉冲式超声处理对蛋清液拉曼光谱、内源性荧光光谱、静态流变学性质、粒径和理化结构的影响,结合起泡性的变化进行相关性分析。研究发现,超声处理能够改变蛋清蛋白二硫键构象,降低蛋清液黏度,减少总巯基含量,对无规卷曲、β-转角含量和酪氨酸残基峰强比(I_(850)/I_(830))影响较小,蛋清液依旧为假塑性流体。在超声处理15 min内,蛋清蛋白质粒径、表面巯基含量、热变性焓(ΔH)、α-螺旋和β-折叠含量逐渐减少,内源性荧光强度和表面疏水性逐渐增强,色氨酸残基趋向于"暴露的"展开形式;起泡性得到改善,且泡沫体积小,呈均匀紧密的排列,泡沫稳定性小幅降低。随着超声时间的延长,β-折叠含量继续降低,粒径、表面巯基含量、ΔH、α-螺旋含量、色氨酸残基峰强比(I_(1 363)/I_(1 338))、内源性荧光强度和表面疏水性呈现不同的变化趋势,起泡性逐渐降低,但泡沫稳定性有所升高。相关性分析表明,起泡性与I_(1 363)/I_(1 338)、表面疏水性呈正相关,与ΔH、平均粒径、α-螺旋含量和表面巯基含量呈负相关,泡沫稳定性与表面疏水性呈负相关。
        The effect of pulsed ultrasonic treatment on the foaming properties, Raman spectroscopy, endogenous fluorescence spectroscopy, static rheological properties, particle size, physicochemical properties and structural characteristics of liquid egg white(LEW) was investigated. Correlation analysis was also conducted. The results showed that the disulfide bond conformation of egg white protein(EWP) was changed by ultrasonic treatment, and the viscosity and total sulfhydryl group content of LEW were decreased accordingly. LEW was still a pseudoplastic fluid after ultrasonic treatment.The particle size, surface sulfhydryl content, thermal denaturation enthalpy(ΔH) and α-helix and β-sheet contents of EWP gradually decreased with increasing ultrasonic treatment time up to 15 min, whereas the endogenous fluorescence intensity and surface hydrophobicity increased. The tryptophan residues tended to be exposed on the protein surface. Meanwhile,the foaming capacity was gradually improved, and the foam stability was reduced marginally. The micromorphology of the foam was smaller and more evenly and closely arranged after ultrasonic treatment. The content of β-sheet continued to decrease with increasing ultrasonic time, whereas the opposite was observed for particle size, surface sulfhydryl content,ΔH, α-helix content, intensity ratio of tryptophan residues(I_(1 363)/I_(1 338)) ratio, endogenous fluorescence intensity and surface hydrophobicity. Meanwhile, foaming capacity gradually decreased, while foam stability increased. The correlation analysis showed that foam capacity was positively correlated with I_(1 363)/I_(1 338) ratio and surface hydrophobicity, and negatively correlated with surface sulfhydryl content, ΔH, average particle size, and α-helix content. In addition, foam stability was negatively correlated with surface hydrophobicity.
引文
[1]CHEN Chen,CHI Yujie.Antioxidant,ACE inhibitory activities and functional properties of egg white protein hydrolysate[J].Journal of Food Biochemistry,2012,36(4):383-394.DOI:10.1111/j.1745-4514.2011.00555.x.
    [2]LUNOW D,KAISER S,BRüCKNER S,et al.Selective release of ACE-inhibiting tryptophan-containing dipeptides from food proteins by enzymatic hydrolysis[J].European Food Research and Technology,2013,237(1):27-37.DOI:10.1007/s00217-013-2014-x.
    [3]迟玉杰.蛋制品加工技术[M].北京:中国轻工业出版社,2018:100-102.
    [4]王欢,迟玉杰,王晓莹,等.蛋清粉起泡性对戚风蛋糕品质的影响[J].中国家禽,2014,36(20):34-38.
    [5]KATO A,OSAKO Y,MATSUDOMI N,et al.Changes in the emulsifying and foaming properties of proteins during heat denaturation[J].Journal of the Agricultural Chemical Society of Japan,2014,47(1):33-37.DOI:10.1080/00021369.1983.10865579.
    [6]邓涵,祖琴琴,朱杰瑞,等.超声处理对大豆7S蛋白潜在致敏性的影响[J].食品科学,2017,38(5):32-37.DOI:10.7506/spkx1002-6630-201705006.
    [7]MONFORT S,MA?AS P,CONDóN S,et al.Physicochemical and functional properties of liquid whole egg treated by the application of pulsed electric fields followed by heat in the presence of triethyl citrate[J].Food Research International,2012,48(2):484-490.DOI:10.1016/j.foodres.2012.04.015.
    [8]KNE?EVI?-JUGOVI?Z D,STEFANOVI?A B,?U?A M G,et al.Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins[J].Acta Periodica Technologica,2012(43):33-41.DOI:10.2298/apt1243033.
    [9]KENTISH S,ASHOKKUMAR M.The physical and chemical effects of ultrasound[M]//FENG H,BARBOSA-CáNOVAS G V,WEISS J.Ultrasound technologies for food and bioprocessing.New York:Springer,2011:1-12.
    [10]SORIA A C,VILLAMIEL M.Effect of ultrasound on the technological properties and bioactivity of food:a review[J].Trends in Food Science&Technology,2010,21(7):323-331.DOI:10.1016/j.tifs.2010.04.003.
    [11]HU Hao,LI-CHAN E C Y,WAN Li,et al.The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate[J].Food Hydrocolloids,2013,32(2):303-311.DOI:10.1016/j.foodhyd.2013.01.016.
    [12]O’DONNELL C P,TIWARI B K,BOURKE P,et al.Effect of ultrasonic processing on food enzymes of industrial importance[J].Trends in Food Science&Technology,2010,21(7):358-367.DOI:10.1016/j.tifs.2010.04.007.
    [13]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.DOI:10.1016/j.foodhyd.2015.02.009.
    [14]王一博.高起泡性蛋清液制备与应用研究[D].武汉:华中农业大学,2016:26-30.
    [15]JAMBRAK A R,MASON T J,LELAS V,et al.Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions[J].Journal of Food Engineering,2008,86(2):281-287.DOI:10.1016/j.jfoodeng.2007.10.004.
    [16]黄六容,马海乐,穆丽君,等.超声波对木瓜蛋白酶的活性及动力学和热力学参数的影响[J].高校化学工程学报,2012,26(1):89-92.
    [17]CHANG Cuihua,NIU Fuge,SU Yujie,et al.Characteristics and emulsifying properties of acid and acid-heat induced egg white protein[J].Food Hydrocolloids,2016,54:342-350.DOI:10.1016/j.foodhyd.2015.09.026.
    [18]NESTERENKO A,ALRIC I,SILVESTRE F,et al.Influence of soy protein’s structural modifications on their microencapsulation properties:α-tocopherol microparticle preparation[J].Food Research International,2012,48(2):387-396.DOI:10.1016/j.foodres.2012.04.023.
    [19]KUMBáR V,TRNKA J,?áRKA N,et al.On the influence of storage duration on rheological properties of liquid egg products and response of eggs to impact loading:Japanese quail eggs[J].Journal of Food Engineering,2015,166(1):86-94.DOI:10.1016/j.jfoodeng.2015.05.030.
    [20]TANG C H,CHOI S M,MA C Y.Study of thermal properties and heat-induced denaturation and aggregation of soy proteins by modulated differential scanning calorimetry[J].International Journal of Biological Macromolecules,2007,40(2):96-104.DOI:10.1016/j.ijbiomac.2006.06.013.
    [21]MAFORIMBO E,SKURRAY G R,NGUYEN M.Evaluation of L-ascorbic acid oxidation on SH concentration in soy-wheat composite dough during resting period[J].LWT-Food Science and Technology,2007,40(2):338-343.DOI:10.1016/j.lwt.2005.09.008.
    [22]VOUTSINAS L P,CHEUNG E,NAKAI S.Relationships of hydrophobicity to emulsifying properties of heat denatured proteins[J].Journal of Food Science,1983,48(1):26-32.DOI:10.1111/j.1365-2621.1983.tb14781.x.
    [23]YIN Shouwei,TANG Chuanhe,YANG Xiaoquan,et al.Conformational study of red kidney bean(Phaseolus vulgaris L.)protein isolate(KPI)by tryptophan fluorescence and differential scanning calorimetry[J].Journal of Agricultural and Food Chemistry,2010,59(1):241-248.DOI:10.1021/jf1027608.
    [24]CHURCH FC,SWAISGOOD H E,PORTER D H,et al.Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins[J].Journal of Dairy Science,1983,66(6):1219-1227.DOI:10.3168/jds.S0022-0302(83)81926-2.
    [25]J.C.A..Infrared and raman spectroscopy of biological molecules.edited by T.M.Theophanides,D.Reidel,Holland,in co-operation with NATO Scientific Affairs Division,pp.ix+372,price 90 Dfl[J].Journal of Molecular Structure,1978,67:332.DOI:10.1016/0022-2860(80)80386-3.
    [26]WONG H W,CHOI S M,PHILLIPS D L,et al.Raman spectroscopic study of deamidated food proteins[J].Food Chemistry,2009,113(2):363-370.DOI:10.1016/j.foodchem.2008.09.027.
    [27]WANG X S,TANG C H,LI B S,et al.Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates[J].Food Hydrocolloids,2008,22(4):560-567.DOI:10.1016/j.foodhyd.2007.01.027.
    [28]HU H,WU J,LI-CHAN E C Y,et al.Effects of ultrasound on structural and physical properties of soy protein isolate(SPI)dispersions[J].Food Hydrocolloids,2013,30(2):647-655.DOI:10.1016/j.foodhyd.2012.08.001.
    [29]CHANDRAPALA J,OLIVER C,KENTISH S,et al.Ultrasonics in food processing[J].Ultrasonics Sonochemistry,2012,19(5):975-983.DOI:10.1016/j.ultsonch.2012.01.010.
    [30]许以明.拉曼光谱及其在结构生物学中的应用[M].北京:化学工业出版社教材出版中心,2005:11-12.
    [31]TU A T.Raman spectroscopy in biology:principles and applications[M].New York:John Wiley and Sons,1982:165.
    [32]MATEMU A O,KAYAHARA H,MURASAWA H,et al.Improved emulsifying properties of soy proteins by acylation with saturated fatty acids[J].Food Chemistry,2011,124(2):596-602.DOI:10.1016/j.foodchem.2010.06.081.
    [33]STEFANOVIC A,JOVANOVI?J,DOJ?INOVI?M,et al.Impact of high-intensity ultrasound probe on the functionality of egg white proteins[J].Journal of Hygienic Engineering&Design,2014,6:215-224.
    [34]LIU J H,RU Q M,DING Y T.Glycation a promising method for food protein modification:physicochemical properties and structure,a review[J].Food Research International,2012,49(1):170-183.DOI:10.1016/j.foodres.2012.07.034.
    [35]黄群,金永国,马美湖,等.超高压处理对S-卵白蛋白构象与功能特性的影响[J].农业机械学报,2013,44(3):161-166.
    [36]HUANG Q,MA M H,HUANG X,et al.Effect of S-configuration transformation of ovalbumin on its molecular characteristics and emulsifying properties[J].Asian Journal of Chemistry,2012,24(4):1675-1679.
    [37]GüLSEREN I,GüZEY D,BRUCE B D,et al.Structural and functional changes in ultrasonicated bovine serum albumin solutions[J].Ultrasonics Sonochemistry,2007,14(2):173-183.DOI:10.1016/j.ultsonch.2005.07.006.
    [38]CHANDRAPALA J,ZISU B,PALMER M,et al.Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate[J].Ultrasonics Sonochemistry,2011,18(5):951-957.DOI:10.1016/j.ultsonch.2010.12.016.
    [39]ARZENI C,PéREZ O E,PILOSOF A M R.Functionality of egg white proteins as affected by high intensity ultrasound[J].Food Hydrocolloids,2012,29(2):308-316.DOI:10.1016/j.foodhyd.2012.03.009.
    [40]ARZENI C,MARTíNEZ K,ZEMA P,et al.Comparative study of high intensity ultrasound effects on food proteins functionality[J].Journal of Food Engineering,2012,108(3):463-472.DOI:10.1016/j.jfoodeng.2011.08.018.
    [41]MURRAY B S,DURGA K,YUSOFF A,et al.Stabilization of foams and emulsions by mixtures of surface active food-grade particles and proteins[J].Food Hydrocolloids,2011,25(4):627-638.DOI:10.1016/j.foodhyd.2010.07.025.
    [42]?MUDZI?SKI D,PTASZEK P,KRUK J,et al.The role of hydrocolloids in mechanical properties of fresh foams based on egg white proteins[J].Journal of Food Engineering,2014,121(1):128-134.DOI:10.1016/j.jfoodeng.2013.08.020.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700