制油工艺对棉籽粕中蛋白结构与功能特性的影响
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摘要
以亚临界流体萃取法、热榨浸出法、冷榨浸出法所得棉籽饼粕为实验材料,采用超声波辅助碱法提取棉籽蛋白,对其蛋白结构与功能特性进行分析。结果表明:棉籽蛋白的主要亚基分子质量为50、45 kDa且只有一个吸热峰,起始温度、变性温度和焓变范围分别为85.6～87.8、94.3～97.7℃和5.6～7.9 J/g,热榨浸出粕蛋白二硫键的含量最低并且含有许多低分子质量亚基;亚临界流体萃取粕蛋白和冷榨浸出棉籽粕蛋白的二级结构中有较低的β-折叠含量、较高的α-螺旋和β-转角含量;热榨浸出粕蛋白的变性温度最高。亚临界流体萃取粕蛋白具有较高的吸水性、吸油性、乳化稳定性、起泡性、表面疏水性和荧光强度。冷榨浸出粕蛋白的吸水性、吸油性、表面疏水性和荧光强度高于热榨浸出粕蛋白。亚临界流体萃取法所得棉籽粕的蛋白变性程度最小,更多地保留了棉籽蛋白的天然结构和功能特性。
This study was conducted to analyze the functional properties and structural characteristics of proteins extracted from hot-pressed solvent extracted cottonseed meal(HCM), cold-pressed solvent extracted cottonseed meal(CCM) and subcritical ?uid extracted cottonseed meal(SCM) by ultrasonic-assisted alkaline hydrolysis. The results indicated that each of the four proteins contained two major subunits(about 50 and 45 kDa) and showed one endothermic peak. The initial temperature, denaturation temperature and enthalpy change were 85.6–87.8, 94.3–97.7 ℃ and 5.6–7.9 J/g, respectively. The protein isolated from HCM(HCMPI) had the lowest disul?de bond level along with many low-molecular mass subunits.The secondary structures of the proteins isolated from SCM(SCMPI) and CCM(CCMPI) showed less β-sheet and moreα-helix and β-turn. HCMPI showed the highest denaturalization temperature. SCMPI had high water-absorbing capacity,oil-absorbing capacity, emulsion stability, foaming characteristics, surface hydrophobicity, and fluorescence intensity.CCMPI had higher water-absorbing capacity, oil-absorbing capacity, surface hydrophobicity, and ?uorescence intensity than HCMPI. The denaturation level of SCMPI was lowest, suggesting better retention of the natural structural properties and functional properties.
This study was conducted to analyze the functional properties and structural characteristics of proteins extracted from hot-pressed solvent extracted cottonseed meal(HCM), cold-pressed solvent extracted cottonseed meal(CCM) and subcritical ?uid extracted cottonseed meal(SCM) by ultrasonic-assisted alkaline hydrolysis. The results indicated that each of the four proteins contained two major subunits(about 50 and 45 kDa) and showed one endothermic peak. The initial temperature, denaturation temperature and enthalpy change were 85.6–87.8, 94.3–97.7 ℃ and 5.6–7.9 J/g, respectively. The protein isolated from HCM(HCMPI) had the lowest disul?de bond level along with many low-molecular mass subunits.The secondary structures of the proteins isolated from SCM(SCMPI) and CCM(CCMPI) showed less β-sheet and moreα-helix and β-turn. HCMPI showed the highest denaturalization temperature. SCMPI had high water-absorbing capacity,oil-absorbing capacity, emulsion stability, foaming characteristics, surface hydrophobicity, and fluorescence intensity.CCMPI had higher water-absorbing capacity, oil-absorbing capacity, surface hydrophobicity, and ?uorescence intensity than HCMPI. The denaturation level of SCMPI was lowest, suggesting better retention of the natural structural properties and functional properties.
引文
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[28]赵小龙,刘大川.棉籽分离蛋白的功能特性研究[J].中国油脂,2015,40(1):27-30.
[29]MCCLEMENTS D J.Critical review of techniques and methodologies for characterization of emulsion stability[J].Critical Reviews in Food Science and Nutrition,2007,47(7):611-649.DOI:101080/10408390701289292.
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[31]GONG Kukie,SHI Aimin,LIU Hongzhi,et al.Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate[J].Journal of Food Engineering,2016,170:33-40.DOI:101016/jjfoodeng201509011.
[32]WONG B T,ZHAI J L,HOFFMANN S V,et al.Conformational changes to deamidated wheat gliadins andβ-casein upon adsorption to oil-water emulsion interfaces[J].Food Hydrocolloids,2012,27(1):91-101.DOI:10.1016/j.foodhyd.2011.08.012.
[33]高海燕,赵镭,尹京苑,等.棉籽分离蛋白功能性质的研究[J].食品科学,2008,29(11):72-76.DOI:103321/j.issn:1002-6630.2008.11.009.
[2]CAN A,HUMMEL J,DENEK N,et al.Effects of non-enzymatic browning reaction intensity on in vitro ruminal protein degradation and intestinal protein digestion of soybean and cottonseed meals[J].Animal Feed Science and Technology,2011,163(2/3/4):255-259.DOI:101016/janifeedsci201011003.
[3]CATER C M,MATTIL K F,MEINKE W W,et al.Cottonseed protein food products[J].Journal of the American Oil Chemists’Society,1977,54(2):90A-93A.DOI:101007/BF02912380.
[4]TSALIKI E,KECHAGIA U,DOXASTAKIS G.Evaluation of the foaming properties of cottonseed protein isolates[J].Food Hydrocolloids,2002,16(6):645-652.DOI:101016/S0268-005X(02)00030-9.
[5]刘琳.食品中蛋白质的功能(七)食品蛋白质功能特性的影响因素[J].肉类研究,2009,23(10):61-66.
[6]JOSHI M,ADHIKARI B,ALDRED P,et al.Interfacial and emulsifying properties of lentil protein isolate[J].Food Chemistry,2012,134(3):1343-1353.DOI:101016/jfoodchem201203029.
[7]刘大川,齐玉堂,张宏强,等.大豆脱皮、浸出粕低温脱溶工艺研究及大豆蛋白产品的开发[J].中国油脂,1993,18(4):3-9.
[8]REDDY M I,RAO S N M.Physicochemical properties of gossypin(11S protein)and congossypin(7S protein)of glanded cottonseed[J].Journal of Agricultural and Food Chemistry,1988,36(2):241-245.DOI:10.1021/jf00080a002.
[9]TSALIKI E,PEGIADOU S,DOXASTAKIS G.Evaluation of the emulsifying properties of cottonseed protein isolates[J].F o o d H y d r o c o l l o i d s,2 0 0 4,1 8(4):6 3 1-6 3 7.D O I:1 0 1 0 1 6/jfoodhyd200311001.
[10]邢要非,王延琴,方丹,等.亚临界丁烷萃取棉籽油工艺及产物品质研究[J].中国油脂,2014,39(9):5-9.
[11]栾姝,孟磊,孙莲,等.高效液相色谱法测定棉籽仁中棉酚的质量分数[J].食品科学,2010,31(4):198-200.
[12]马梦婷,王艺静,王青林,等.超声波辅助碱法提取棉籽蛋白工艺条件的优化[J].食品工业,2017,38(8):66-71.
[13]AROGUNDADE L A,TAIHUA M U,FAKINHANMI T.Structural,physicochemical and interfacial stabilisation properties of ultrafiltered african yam bean(Sphenostylis stenocarpa)protein isolate compared with those of isoelectric protein isolate[J].LWT-Food Science and Technology,2016,69:400-408.DOI:101016/jlwt201601049.
[14]KATO A,NAKAI S.Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins[J].Biochimica et Biophysica Acta(BBA)-Protein Structure,1980,624(1):13-20.DOI:101016/0005-2795(80)90220-2.
[15]WU Haiwen,WANG Qiang,MA Tiezheng,et al.Comparative studies on the functional properties of various protein concentrate preparations of peanut protein[J].Food Research International,2009,42(3):343-348.DOI:101016/jfoodres200812006.
[16]王林林,祁鲲,朱新亮,等.亚临界流体萃取牡丹籽油工艺研究[J].粮食与油脂,2015,28(11):34-37.
[17]ZHANG Y P,YANG R J,ZHAO W,et al.Physicochemical and emulsifying properties of protein extracted from soybean meal assisted by steam flash-explosion[J].Innovative Food Science and Emerging Technologies,2014,23(3):131-137.DOI:101016/jifset201403009.
[18]SHEVKANI K,SINGH N,KAUR A,et al.Structural and functional characterization of kidney bean and field pea protein isolates:a comparative study[J].Food Hydrocolloids,2015,43:679-689.DOI:101016/jfoodhyd201407024.
[19]KONG J L,YU S N.Fourier transform infrared spectroscopic analysis of protein secondary structures[J].Acta Biochimica et Biophysica Sinica,2007,39(8):549-559.DOI:101111/j1745-7270200700320x.
[20]T I M I L S E N A Y P,A D H I K A R I R,B A R R O W C J,e t a l.Physicochemical and functional properties of protein isolate produced from australian chia seeds[J].Food Chemistry,2016,212:648-656.DOI:101016/jfoodchem201606017.
[21]DINIZ R S,DOS REIS COIMBRA J S,DE CARVALHO TEIXEIRAáV N,et al.Production,characterization and foamability ofα-lactalbumin/glycomacropeptide supramolecular structures[J].Food Research International,2014,64:157-165.DOI:10.1016/j.foodres.2014.05.079.
[22]TANG C H,SUN X.A comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes:implications for the structure-function relationship[J].F o o d H y d r o c o l l o i d s,2 0 1 1,2 5(3):3 1 5-3 2 4.D O I:1 0 1 0 1 6/jfoodhyd201006009.
[23]ADEBOWALE Y A,ADEYEMI I A,OSHODI A A.Functional and physicochemical properties of flours of six Mucuna species[J].African Journal of Biotechnology,2005,4(12):1461-1468.
[24]ANTONOV Y A,ZHURAVLEVA I L,CARDINAELS R,et al.Structural studies on the interaction of lysozyme with dextran sulfate[J].Food Hydrocolloids,2015,44:71-80.DOI:101016/jfoodhyd201409006.
[25]AJIBOLA C F,MALOMO S A,FAGBEMI T N,et al.Polypeptide composition and functional properties of african yam bean seed(Sphenostylis stenocarpa)albumin,globulin and protein concentrate[J].Food Hydrocolloids,2016,56:189-200.DOI:101016/jfoodhyd201512013.
[26]ZHAO Q,XIONG H,SELOMULYA C,et al.Effects of spray drying and freeze drying on the properties of protein isolate from rice dreg protein[J].Food and Bioprocess Technology,2013,6(7):1759-1769.DOI:101007/s11947-012-0844-3.
[27]李园,汪学德,刘日斌.不同制油工艺提取芝麻蛋白的功能特性研究[J].粮油食品科技,2013,21(3):32-34.DOI:10.16210/j.cnki.1007-7561.2013.03.012.
[28]赵小龙,刘大川.棉籽分离蛋白的功能特性研究[J].中国油脂,2015,40(1):27-30.
[29]MCCLEMENTS D J.Critical review of techniques and methodologies for characterization of emulsion stability[J].Critical Reviews in Food Science and Nutrition,2007,47(7):611-649.DOI:101080/10408390701289292.
[30]PANYAM D.Enhancing the functionality of food proteins by enzymatic modification[J].Trends in Food Science&Technology,1996,7(4):120-125.DOI:101016/0924-2244(96)10012-1.
[31]GONG Kukie,SHI Aimin,LIU Hongzhi,et al.Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate[J].Journal of Food Engineering,2016,170:33-40.DOI:101016/jjfoodeng201509011.
[32]WONG B T,ZHAI J L,HOFFMANN S V,et al.Conformational changes to deamidated wheat gliadins andβ-casein upon adsorption to oil-water emulsion interfaces[J].Food Hydrocolloids,2012,27(1):91-101.DOI:10.1016/j.foodhyd.2011.08.012.
[33]高海燕,赵镭,尹京苑,等.棉籽分离蛋白功能性质的研究[J].食品科学,2008,29(11):72-76.DOI:103321/j.issn:1002-6630.2008.11.009.