超高压对酱卤羊肚感官品质、微观结构及其肌浆蛋白特性的影响
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摘要
以真空包装酱卤羊肚为研究对象,通过单因素试验探讨超高压(ultra high pressure,UHP)处理对酱卤羊肚感官品质的影响;采用压力水平100、250、400 MPa,保压时间5、10、15、20、25 min,保压温度25℃的条件进行UHP处理,通过双缩脲法、圆二色光谱、扫描电子显微镜观察及肌浆蛋白的物化指标分析,研究UHP对酱卤羊肚微观结构及肌浆蛋白特性的影响。结果表明:不同条件的UHP处理导致酱卤羊肚的感官品质差异明显,UHP处理使酱卤羊肚肌浆蛋白的内部基团暴露于分子表面,导致蛋白质的二级结构发生改变,较稳定的α-螺旋含量增加,β-折叠含量降低,而不规则的β-转角和无规卷曲含量无明显变化;羰基含量、表面疏水性和浊度增加,总巯基含量、游离氨基比例、溶解性减小,400 MPa、25℃UHP处理20 min可使肌浆蛋白发生适度的氧化变性,导致酱卤羊肚的微观结构发生改变,最终使产品的感官品质得到改善。
In this paper, vacuum packaged sauced sheep stomach was used to evaluate its sensory quality as affected by ultra high pressure(UHP) treatment. UHP treatments were carried out under varying conditions of pressure(100, 250 and 400 MPa) and holding time(5, 10, 15, 20 and 25 min) and at a constant temperature of 25 ℃. The physicochemical and functional properties and sarcoplasmic protein characteristics were studied by the biuret method, circular dichroism spectroscopy and scanning electron microscopy in order to investigate the effect of UHP on the microstructure and sarcoplasmic protein characteristics of sauced sheep stomach. The results showed that sensory quality significantly differentiated between UHP-treated and untreated samples. UHP treatment led to exposure of internal groups on the protein surface and alterations in the protein secondary structure. After the treatment, the contents of the stable secondary structures α-helix and β-sheet increased and decreased respectively, while the contents of irregular β-turn and random coil did not significantly change. In addition, UHP treatment caused an increase in carbonyl content, surface hydrophobicity and turbidity, and a decrease in total sulfhydryl content, free ammonia content and solubility. UHP treatment under 400 MPa and25 ℃ for 20 min could cause moderate oxidative denaturation of sarcoplasmic protein, changes in the microstructure, and eventually improve the sensory quality of sauced sheep stomach.
In this paper, vacuum packaged sauced sheep stomach was used to evaluate its sensory quality as affected by ultra high pressure(UHP) treatment. UHP treatments were carried out under varying conditions of pressure(100, 250 and 400 MPa) and holding time(5, 10, 15, 20 and 25 min) and at a constant temperature of 25 ℃. The physicochemical and functional properties and sarcoplasmic protein characteristics were studied by the biuret method, circular dichroism spectroscopy and scanning electron microscopy in order to investigate the effect of UHP on the microstructure and sarcoplasmic protein characteristics of sauced sheep stomach. The results showed that sensory quality significantly differentiated between UHP-treated and untreated samples. UHP treatment led to exposure of internal groups on the protein surface and alterations in the protein secondary structure. After the treatment, the contents of the stable secondary structures α-helix and β-sheet increased and decreased respectively, while the contents of irregular β-turn and random coil did not significantly change. In addition, UHP treatment caused an increase in carbonyl content, surface hydrophobicity and turbidity, and a decrease in total sulfhydryl content, free ammonia content and solubility. UHP treatment under 400 MPa and25 ℃ for 20 min could cause moderate oxidative denaturation of sarcoplasmic protein, changes in the microstructure, and eventually improve the sensory quality of sauced sheep stomach.
引文
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[24]田童童,巩子路,朱新荣,等.蛋白质氧化对乳清蛋白理化性质变化的影响[J].江苏农业科学,2013,41(11):301-303.DOI:10.3969/j.issn.1002-1302.2013.11.117.
[25]BOURAOUI M,NAKAII S,LI-CHAN E.In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy[J].Food Research International,1997,30(1):65-72.
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[27]MORZEL M,GATELLIER P,SAYD T,et al.Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins[J].Meat Science,2006,73(3):536-543.DOI:10.1016/j.meatsci.2006.02.005.
[2]王俊,庄天慧,陈雪.新疆居民畜产品消费分析[J].四川农业大学学报,2017,35(2):280-288.DOI:10.16036/j.issn.1000-2650.2017.02.022.
[3]ARVANITOYANNIS I S,LADAS D.Meat waste treatment methods and potential uses[J].International Journal of Food Science and Technology,2008,43(3):543-559.DOI:10.1111/j.1365-2621.2006.01492.x.
[4]王琳琳,余群力,曹晖,等.我国肉牛副产品加工利用现状及技术研究[J].农产品加工业,2015(17):36-41.
[5]董鹏,张良,陈芳,等.食品超高压技术研究进展与应用现状[J].农产品加工,2013(6):28-29.DOI:10.3969/j.issn.1671-9646.2013.06.014.
[6]TORRES J A,VELAZQUEZ G.Commercial opportunities and research challenges in the high pressure processing of foods[J].Journal of Food Engineering,2005,67(1/2):95-112.DOI:10.1016/j.jfoodeng.2004.05.066.
[7]BUCKOW R,SIKES A,TUME R.Effect of high pressure on physicochemical properties of meat[J].Critical Reviews in Food Science and Nutrition,2013,53(7):770-786.DOI:10.1080/10408398.2011.560296.
[8]HEINZ V,BUCKOW R.Food preservation by high pressure[J].Journal for Consumer Protection and Food Safety,2010,5(1):73-81.DOI:10.1007/s00003-009-0311-x.
[9]王甜甜,曹晓虹,马岩涛.肌浆蛋白的研究进展[J].食品研究与开发,2015,36(6):109-112.DOI:10.3969/j.issn.1005-6521.2015.06.031.
[10]KRUK Z A,YUN H,RUTLEY D L,et al.The effect of high pressure on microbial population,meat quality and sensory characteristics of chicken breast fillet[J].Food Control,2011,22(1):6-12.
[11]冷雪娇.超高压处理对鸡胸肉腌制效果的研究[D].南京:南京农业大学,2013:3.DOI:10.7666/d.Y2528170.
[12]斯琴其木格,苏和,李金桩,等.超高压处理对骨骼肌肌肉蛋白质的影响[J].食品科技,2014,39(1):156-161.DOI:10.13684/j.cnki.spkj.2014.01.034.
[13]刘贝贝.冷冻牛肚超高压改性与卤制技术研究[D].合肥:合肥工业大学,2017:54.
[14]张大力,蔡丹,盛悦,等.超高压处理对牛肚杀菌效果影响[J].肉类研究,2016,30(1):21-24.DOI:10.15922/j.cnki.rlyj.2016.01.005.
[15]SALLAM K I.Chemical,sensory and shelf life evaluation of sliced salmon treated with salts of organic acids[J].Food Chemistry,2007,101(2):592-600.
[16]赵伟,杨瑞金,张文斌,等.超高压处理对牡蛎超微结构、组分及蛋白质变性的影响[J].食品与发酵工业,2011,37(5):7-11.DOI:10.13995/j.cnki.11-1802/ts.2011.05.040.
[17]HASHIMOTO K,WATABE S,KONO M,et al.Muscle protein composition of sardine and mackerel[J].Bulletin of the Japanese Society of Scientific Fisheries,1979,45(11):1435-1441.
[18]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,2013:11.DOI:10.7666/d.Y2295487.
[19]YONGSAWATDIGUL J,PARK J W.Thermal denaturation and aggregation of threadfin bream actomyosin[J].Food Chemistry,2003,83(3):409-416.
[20]BRANDS C M,VAN BOEKEL M A.Kinetic modeling of reactions in heated monosaccharide-casein systems[J].Journal of Agricultural and Food Chemistry,2002,50(23):6725-6739.DOI:10.1021/jf011164h.
[21]XIONG Youling L.,BLANCHARDD S P.Myofibrillar protein gelation:viscoelastic changes related to heating procedures[J].Journal of Food Science,1994,59(4):734-738.
[22]XIONG Youling L..Protein oxidation and implications for muscle food quality[J].Antioxidants in Muscle Foods:Nutritional Strategies to Improve Quality,2000,2000:85-111.
[23]OHMORI T,SHIGEHISA T,TAJI S,et al.Effect of high pressure on the protease activities in meat[J].Agricultural and Biological Chemistry,1991,55(2):357-361.
[24]田童童,巩子路,朱新荣,等.蛋白质氧化对乳清蛋白理化性质变化的影响[J].江苏农业科学,2013,41(11):301-303.DOI:10.3969/j.issn.1002-1302.2013.11.117.
[25]BOURAOUI M,NAKAII S,LI-CHAN E.In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy[J].Food Research International,1997,30(1):65-72.
[26]KOLCZAK T,WEBERER M.Water extractable proteins of porcine muscle[J].Journal of Food Science,1969,34(6):547-550.DOI:10.1111/j.1365-2621.1969.tb12085.x.
[27]MORZEL M,GATELLIER P,SAYD T,et al.Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins[J].Meat Science,2006,73(3):536-543.DOI:10.1016/j.meatsci.2006.02.005.