研究报告

脂质自由基诱导氧化对花生蛋白功能特性的影响

  • 杨曦 ,
  • 程群 ,
  • 刘江 ,
  • 陈琼 ,
  • 王振兴 ,
  • 张雪春 ,
  • 孙健
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  • 1(西南林业大学 生命科学学院,云南 昆明,650224)
    2(广西农业科学院 农产品加工研究所,广西 南宁,530007)
硕士研究生(张雪春副教授为通讯作者,E-mail:xuechun_zhang@163.com)

收稿日期: 2020-02-12

  网络出版日期: 2020-06-17

基金资助

国家自然科学基金(31760440);云南省农业基础研究联合专项面上项目(2017FG001(-020));西南林业大学科研启动基金项目(111303);广西壮族自治区农业科学院博士后启动基金(桂农科博2018033)

Effect of lipid free radical-mediated oxidation on the functional properties of peanut proteins

  • YANG Xi ,
  • CHENG Qun ,
  • LIU Jiang ,
  • CHEN Qiong ,
  • WANG Zhenxing ,
  • ZHANG Xuechun ,
  • SUN Jian
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  • 1(College of Life Sciences, Southwest Forestry University, Kunming 650224, China)
    2(Agro-food Science and Technology Research Institute, Guangxi Academy of Agricultural Sciences, Nanning 530007, China)

Received date: 2020-02-12

  Online published: 2020-06-17

摘要

为探究脂质自由基处理对花生蛋白在食品生产过程中功能特性的影响,该文建立铁/过氧化氢/抗环血酸(Fe/H2O2/Asc)和2,2'-盐酸脒基丙烷(2,2'-azobis (2-amidinopropane) dihydrochloride,AAPH)体系,代表脂质氧化中产生的羟自由基和过氧自由基对花生蛋白进行氧化修饰,研究氧化对花生蛋白羰基、溶解度、乳化性能和起泡性能等功能特性的影响。结果表明,随着两个体系中自由基浓度的增加,花生蛋白的羰基含量分别增加1.42倍和1.66倍,溶解度分别下降43.06%和49.62%,内源荧光最大吸收波长蓝移,荧光强度分别下降33.01%和28.02%,乳化性分别下降63.91%和28.91%,乳化稳定性分别下降46.79%和33.08%,起泡性及起泡稳定性呈先上升后下降的趋势,起泡稳定性分别在5 mmol/L和0.5 mmol/L时最高。研究结果表明羟自由基和过氧自由基氧化对花生蛋白的功能特性有较大影响,可通过适度氧化对其性质进行调控。

本文引用格式

杨曦 , 程群 , 刘江 , 陈琼 , 王振兴 , 张雪春 , 孙健 . 脂质自由基诱导氧化对花生蛋白功能特性的影响[J]. 食品与发酵工业, 2020 , 46(10) : 87 -91 . DOI: 10.13995/j.cnki.11-1802/ts.023609

Abstract

To explore the effect of the treatment with the lipid free radical on the functional properties of peanut proteins during food production, the hydroxyl radicals generating system (Fe/H2O2/Ascorbate) and peroxy radicals generating system (2,2'-azobis (2-amidinopropane) dihydrochloride, AAPH) were established to oxidize the peanut proteins, respectively. The functional properties (carbonyl content, solubility, emulsifying and foaming properties) of oxidized peanut proteins were further studied. The results showed that increase of radical concentration in 2 systems raised the carbonyl derivatives of peanut protein 1.42 times and 1.66 times, and the solubility decreased by 43.06% and 49.62%, respectively. Fluorescence analysis revealed a blue shift of maximum absorption wavelength, and the fluorescence intensity decreased by 33.01% and 28.02%, respectively. In addition, the emulsifying ability decreased by 63.91% and 28.91%, respectively, while emulsifying stability decreased by 46.79% and 33.08%, respectively. With the increase of free radical concentration, foamability and foaming stability first increased and then decreased. The highest foaming stability was obtained at hydroxyl radical concentration of 5 mmol/L and peroxy radical concentration of 0.5 mmol/L, respectively. In conclusion, these results imply that the functional properties of peanut proteins are greatly affected by the lipid free radicals, and could be regulated by appropriate oxidation.

参考文献

[1] ZHAO J, ZHOU T, ZHANG Y, et al. Optimization of arachin extraction from defatted peanut (Arachis hypogaea) cakes and effects of ultra-high pressure (UHP) treatment on physiochemical properties of arachin[J]. Food and Bioproducts Processing, 2015,95:38-46.
[2] ZHAO H, ZHOU F, PENG W, et al. The effects of carrageenan on stability of arachin and the interactions between them[J]. Food Hydrocolloids, 2015,43:763-768.
[3] GHATAK S K, SEN K. Peanut proteins: Applications, ailments and possible remediation[J]. Journal of Industrial and Engineering Chemistry, 2013,19(2):369-374.
[4] HELLWIG M. The chemistry of protein oxidation in food[J]. Angewandte Chemie, 2019,58(47):16 742-16 763.
[5] STADTMAN E R, LEVINE R L. Protein oxidation[J]. Annals of the New York Academy of Sciences, 2010,899(1):191-208.
[6] SKIBSTED L H, RISBO J, ANDERSEN M L. Chemical Deterioration and Physical Instability of Food and Beverages[M]. Cambrigde: Woodhead Publishing, 2010:33-69.
[7] 李艳青. 蛋白质氧化对鲤鱼蛋白结构和功能性的影响及其控制技术[D]. 哈尔滨:东北农业大学, 2013.
[8] 周非白. 氧化修饰对猪肉肌原纤维蛋白结构与功能特性的调控研究[D]. 广州:华南理工大学, 2016.
[9] SALIM A P A D, SUMAN S P, CANTO A C V D, et al. Influence of muscle source on proximate composition, texture profile and protein oxidation of beef from grain-finished bos indicus cattle[J]. Ciência Rural, 2019,49(4):1-6.
[10] 尤翔宇. 过氧自由基和丙二醛氧化对米糠蛋白结构.功能性质和消化性质的影响[D]. 长沙:中南林业科技大学, 2019.
[11] PARK D, XIONG Y L, ALDERTON A L. Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein[J]. Food Chemistry, 2007,101(3):1 239-1 246.
[12] WU W, ZHANG C, KONG X, et al. Oxidative modification of soy protein by peroxyl radicals[J]. Food Chemistry, 2009,116(1):295-301.
[13] LEVINE R L, WILLIAMS J A, STADTMAN E P, et al. Carbonyl assays for determination of oxidatively modified proteins[J].Methods Enzymol, 1994,233:346-357.
[14] PEYRANO F, SPERONI F, AVANZA M V. Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure[J]. Innovative Food Science & Emerging Technologies, 2016,33:38-46.
[15] RAMÍREZ SUÁREZ J C, XIONG Y L. Rheological properties of mixed muscle/nonmuscle protein emulsions treated with transglutaminase at two ionic strengths[J]. International Journal of Food Science & Technology, 2003,38(7):777-785.
[16] AUGUSTYNIAK E, ADAM A, WOJDYLA K, et al. Validation of protein carbonyl measurement: A multi-centre study[J]. Redox Biol, 2015,4:149-157.
[17] SOLADOYE O P, JUAREZ M L, AALHUS J L, et al. Protein oxidation in processed meat: Mechanisms and potential implications on human health[J]. Comprhenensive Reviews in Food Science and Food Satety,2015,14(2):106-122.
[18] CANO-MEDINA A, JIMÉNEZ-ISLAS H, DENDOOVEN L, et al. Emulsifying and foaming capacity and emulsion and foam stability of sesame protein concentrates[J]. Food Research International, 2011,44(3):684-692.
[19] FERREYRA J C, KUSKOSKI E M, LUIZ M T B, et al. Emulsifying and foaming properties of peanut (Arachis hypogaea Lineau) flour[J]. Grasas Y Aceites, 2007,58(58):264-269.
[20] CHEN N, ZHAO M, SUN W, et al. Effect of oxidation on the emulsifying properties of soy protein isolate[J]. Food Research International, 2013,52(1):26-32.
[21] VIVIAN J T, CALLIS P R. Mechanisms of tryptophan fluorescence shifts in proteins[J]. Biophysical Journal, 2001,80(5):2 093-2 109.
[22] SIMAT T J, STEINHART H. Oxidation of free tryptophan and tryptophan residues in peptides and proteins[J]. Journal of Agricultural and Food Chemistry, 1998,46(2):490-498.
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