研究报告

冻融对肌原纤维蛋白溶出猪肉糜体系蛋白质变性及品质的影响

  • 吴兴阁 ,
  • 曾茂茂 ,
  • 何志勇 ,
  • 王召君 ,
  • 秦昉 ,
  • 张志刚 ,
  • 陈洁
展开
  • 1(食品科学与技术国家重点实验室(江南大学),江苏 无锡,214122)
    2(厦门银祥集团有限公司 肉食品安全生产技术国家重点实验室,福建 厦门,361100)
硕士研究生(陈洁教授为通讯作者,E-mail:chenjie@jiangnan.edu.cn)

收稿日期: 2021-01-10

  修回日期: 2021-03-04

  网络出版日期: 2021-11-04

基金资助

天津合成生物学创新能力提升计划项目(TSBICIP-KJGG-004)

Effect of freeze-thaw cycles on myofibril dissolution system protein denaturation and quality of minced pork

  • WU Xingge ,
  • ZENG Maomao ,
  • HE Zhiyong ,
  • WANG Zhaojun ,
  • QIN Fang ,
  • ZHANG Zhigang ,
  • CHEN Jie
Expand
  • 1(State Key Laboratory of Food Science and Technology,Jiangnan University,Wuxi 214122,China)
    2(State Key Laboratory of Food Safety Technology for Meat Products,Yinxiang Group,Xiamen 361100,China)

Received date: 2021-01-10

  Revised date: 2021-03-04

  Online published: 2021-11-04

摘要

为探究肌原纤维蛋白溶出的猪肉糜体系在冻藏过程中品质下降的主要因素,通过冻融循环(0~7次)处理,测定肌原纤维蛋白的羰基、自由氨基、巯基、二硫键以及变性焓,肌红蛋白含量和价态变化,并分析蛋白质变性对冻藏猪肉糜质构以及色泽的影响。结果表明,随冻融次数的增加,蛋白质变性和品质下降程度均逐渐加强。冻融7次时,肉糜蒸煮损失增加了30.28%(P<0.05),羰基从2.51 nmol/mg上升至5.14 nmol/mg,巯基减少了40.3%,二硫键从1.42 μmol/g上升至9.03 μmol/g,变性焓下降了34.21%(P<0.05);肌红蛋白含量显著下降(P<0.05),氧合肌红蛋白比例呈现先升高后降低的趋势,高铁肌红蛋白则具有相反的趋势。质构和颜色方面,冻融7次时猪肉糜的硬度、弹性、内聚性均降至最低,咀嚼性下降21.01%(P<0.05);红绿值(a*值)和感官评价得分降低。相关性分析显示,肉糜质构及感官与蛋白质变性指标(羰基、巯基、二硫键)有强相关性(P<0.05),表明猪肉糜在冻融过程中发生蛋白质氧化及冷冻变性使猪肉糜的凝胶网络结构及色泽劣化,且质构劣化,口感下降。主成分分析显示,在冻融4次后,猪肉糜发生显著劣变(P<0.05)。该研究可为肉糜冷冻储藏过程品质劣变的控制提供一定的理论和实验依据。

本文引用格式

吴兴阁 , 曾茂茂 , 何志勇 , 王召君 , 秦昉 , 张志刚 , 陈洁 . 冻融对肌原纤维蛋白溶出猪肉糜体系蛋白质变性及品质的影响[J]. 食品与发酵工业, 2021 , 47(19) : 101 -110 . DOI: 10.13995/j.cnki.11-1802/ts.026709

Abstract

To investigate the main factors of quality degradation of myofibrillar protein in minced pork system during frozen storage, the content of carbonyl, free amino, sulfhydryl, disulfide bonds and denaturation enthalpy of myofibrillar protein, as well as myoglobin (Mb) content and valence changes were determined during freeze -thaw cycles (0~7 times). The effects of protein denaturation on the texture and color of frozen pork mince were analyzed. The results showed that with the increase of freeze-thaw cycles, protein denaturation and quality decline gradually increased. The cooking loss of pork mince increased by 30.28% (P<0.05), and the carbonyl content increased from 2.51 nmol/mg to 5.14 nmol/mg. The sulfhydryl group decreased by 40.3%, the disulfide bond increased from 1.42 μmol/g to 9.03 μmol/g, and the denaturation enthalpy decreased by 34.21% (P<0.05) after 7 times of freeze-thawing. The Mb content decreased significantly (P<0.05), and the ratio of oxymyoglobin (OMb) showed a tendency to increase first and then decrease, while metmyoglobin (MMb) showed the opposite trend. In terms of texture and color, the hardness, elasticity and cohesiveness of minced pork were reduced to a minimum after 7 cycles of freezing-thawing, and the chewiness decreased by 21.01% (P<0.05). Meanwhile, the a* value and the sensory evaluation score decreased. Correlation analysis showed a strong correlation (P<0.05) between texture, sensory and protein denaturation indexes (carbonyl, sulfhydryl, disulfide bonds), which indicating that protein oxidation and freezing denaturation that occurs during freeze-thaw cycles of minced pork, and which further deteriorated the gel network structure and color of minced pork, and degraded the texture and taste. Principal component analysis (PCA) showed that after four freeze-thaw cycles, the quality of minced pork changed significantly(P<0.05). This study is expected to provide a theoretical basis for the quality deterioration of minced pork during frozen storage.

参考文献

[1] 陈茜茜, 黄明,邹玉峰,等.辐照和反复冻融对牛肉蛋白质氧化及食用品质的影响[J].食品科学,2014,35(19):1-5.
CHEN Q Q,HUANG M,ZOU Y F,et al.Influence of irradiation and freeze-thawing cycles on myofibrillar protein oxidation and eating quality of beef[J].Food Science,2014,35(19):1-5.
[2] 戚军. 反复冻融对羊肉品质的影响研究[D].南京:南京农业大学,2009.
QI J.Effect of repeated freeze-thaw cycles on goat meat quality[D].Nanjing:Nanjing Agricultural University,2009.
[3] QI J,LI C B,CHEN Y J,et al.Changes in meat quality of ovine longissimus dorsi muscle in response to repeated freeze and thaw[J].Meat Science,2012,92(4):619-626.
[4] ALI S,ZHANG W G,RAJPUT N,et al.Effect of multiple freeze-thaw cycles on the quality of chicken breast meat[J].Food Chemistry,2015,173:808-814.
[5] PAN N,DONG C H,DU X,et al.Effect of freeze-thaw cycles on the quality of quick-frozen pork patty with different fat content by consumer assessment and instrument-based detection[J].Meat Science,2021,172:108313.
[6] ZHANG M C,LI F F,DIAO X P,et al.Moisture migration,microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freeze-thaw cycles[J].Meat Science,2017,133:10-18.
[7] HENRIOTT M L,HERRERA N J,RIBEIRO F A,et al.Impact of myoglobin oxygenation state prior to frozen storage on color stability of thawed beef steaks through retail display[J].Meat Science,2020,170:108232.
[8] LEELAPONGWATTANA K,BENJAKUL S,VISESSANGUAN W,et al.Physicochemical and biochemical changes during frozen storage of minced flesh of lizardfish (Saurida micropectoralis)[J].Food Chemistry,2005,90(1-2):141-150.
[9] SAEED S,HOWELL N K.Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus)[J].Journal of the Science of Food and Agriculture,2002,82(5):579-586.
[10] 余小领, 李学斌,赵良,等.常规冷冻冻藏对猪肉保水性和组织结构的影响[J].农业工程学报,2008,24(12):264-268.
YU X L,LI X B,ZHAO L,et al.Effects of conventional freezing processing and frozen storage on pork water-holding capacity and structure[J].Transactions of the Chinese Society of Agricultural Engineering,2008,24(12):264-268.
[11] LIU Z L,XIONG Y L,CHEN J.Protein oxidation enhances hydration but suppresses water-holding capacity in porcine longissimus muscle[J].Journal of Agricultural and Food Chemistry,2010,58(19):10 697-10 704.
[12] MIGNINO L A,CRUPKIN M,PAREDI M E.Surface hydrophobicity and functional properties of myofibrillar proteins of mantle from frozen-stored squid (Illex argentinus) caught either jigging machine or trawling[J].LWT-Food Science and Technology,2008,41(4):678-685.
[13] 邓思杨,王博,李海静,等.冻融次数对镜鲤鱼肌原纤维蛋白功能和结构特性变化的影响[J].食品科学,2019,40(11):95-101.
DENG S Y,WANG B,LI H J,et al.Effect of freeze-thaw cycles on changes in functional and structural properties of myofibrillar protein from mirror carp(Cyprinus carpio var.specularis)[J].Food Science,2019,40(11):95-101.
[14] ZHANG Y M,PUOLANNE E,ERTBJERG P.Mimicking myofibrillar protein denaturation in frozen-thawed meat:Effect of pH at high ionic strength[J].Food Chemistry,2021,338:128017.
[15] ARSLAN S.Effects of salt and phosphate levels on the emulsion properties of fresh and frozen hen meats[J].African Journal of Biotechnology,2006,5(10):1 006-1 012.
[16] XIA X F,KONG B H,XIONG Y L,et al.Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation[J].Meat Science,2010,85(3):481-486.
[17] 霍晓娜,李兴民,刘毅,等.光源和光照度对猪肉脂肪氧化程度和色泽变化的影响[J].中国农业大学学报,2006,11(4):47-50.
HUO X N,LI X M,LIU Y,et al.Inflence of light sources and intensity on lipid oxidation and color changes in pork[J].Journal of China Agricultural University,2006,11(4):47-50.
[18] LIU Z L,XIONG Y L,CHEN J.Identification of restricting factors that inhibit swelling of oxidized myofibrils during brine irrigation[J].Journal of Agricultural and Food Chemistry,2009,57(22):10 999-11 007.
[19] XING T,ZHAO X,HAN M Y,et al.A comparative study of functional properties of normal and wooden breast broiler chicken meat with NaCl addition[J].Poultry Science,2017,96(9):3 473-3 481.
[20] 贡汉坤, 焦云鹏.鮰鱼下脚料蛋白质的回收及其凝胶特性研究[J].食品与机械,2012,28(5):107-110.
GONG H K,JIAO Y P.Protein recovered from channel catfish processing by-products via isoelectric solubilization/precipitation and its gelation properties[J].Food & Machinery,2012,28(5):107-110.
[21] 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.
[22] LEVINE R L,WILLIAMS J A,STADTMAN E P,et al.Carbonyl assays for determination of oxidatively modified proteins[J].Methods in Enzymology,1994,233:346-357.
[23] 李春强. 肌原纤维蛋白的氧化程度对谷氨酰胺转移酶催化交联作用的影响及其机理研究[D].无锡:江南大学,2013.
LI C Q.Mechanism of transglutaminase-catalyzed cross-linking of oxidatively stressed myofibrillar protein[D].Wuxi:Jiangnan University,2013.
[24] LIU G,XIONG Y L,BUTTERFIELD D A.Chemical,physical,and gel-forming properties of oxidized myofibrils and whey-and soy-protein isolates[J].Journal of Food Science,2000,65(5):811-818.
[25] THANNHAUSER T W,KONISHI Y,SCHERAGA H A.Analysis for disulfide bonds in peptides and proteins[J].Methods in Enzymology,1987,143:115-119.
[26] 陈骋. 脂质氧化和抗氧化因子对牦牛肉肌红蛋白稳定性及高铁肌红蛋白还原能力的影响[D].兰州:甘肃农业大学,2016.
CHEN C.Effects of lipid oxidation and antioxidant factors on color stability and metmyoglobin reducing ability of yak muscle[D].Lanzhou:Gansu Agricultural University,2016.
[27] KIM H W,CHOI Y S,CHOI J H,et al.Antioxidant effects of soy sauce on color stability and lipid oxidation of raw beef patties during cold storage[J].Meat Science,2013,95(3):641-646.
[28] KRZYWICKI K.The determination of haem pigments in meat[J].Meat Science,1982,7(1):29-36.
[29] SOYER A,ÖZALP B,DALMIŞ Ü,et al.Effects of freezing temperature and duration of frozen storage on lipid and protein oxidation in chicken meat[J].Food Chemistry,2010,120(4):1 025-1 030.
[30] SAEED S,FAWTHROP S A,HOWELL N K.Electron spin resonance (ESR) study on free radical transfer in fish lipid-protein interaction[J].Journal of the Science of Food and Agriculture,1999,79(13):1 809-1 816.
[31] ESTÉVEZ M.Protein carbonyls in meat systems:A review[J].Meat Science,2011,89(3):259-279.
[32] XIONG Y L,PARK D,OOIZUMI T.Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments[J].Journal of Agricultural and Food Chemistry,2009,57(1):153-159.
[33] XU Y S,XIA W S,JIANG Q X,et al.Acid-induced aggregation of actomyosin from silver carp (Hypophthalmichthys molitrix)[J].Food Hydrocolloids,2012,27(2):309-315.
[34] KO W C,YU C C,HSU K C.Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment[J].LWT-Food Science and Technology,2007,40(8):1 316-1 320.
[35] ZHANG Y M,ERTBJERG P.On the origin of thaw loss:Relationship between freezing rate and protein denaturation[J].Food Chemistry,2019,299:125 104.
[36] AKTAŞ N,KAYA M.Influence of weak organic acids and salts on the denaturation characteristics of intramuscular connective tissue.A differential scanning calorimetry study[J].Meat Science,2001,58(4):413-419.
[37] 孟祥忍, 王恒鹏,杨章平.食盐添加量对鸡肉糜热性质及流变性的影响[J].中国家禽,2015,37(16):39-43.
MENG X R,WANG H P,YANG Z P.Effect of salt supplementation on thermal and rheological properties of chicken meat paste[J].China Poultry,2015,37(16):39-43.
[38] THANONKAEW A,BENJAKUL S,VISESSANGUAN W,et al.The effect of metal ions on lipid oxidation,colour and physicochemical properties of cuttlefish (Sepia pharaonis) subjected to multiple freeze-thaw cycles[J].Food Chemistry,2006,95(4):591-599.
[39] LIU Q,CHEN Q,KONG B H,et al.The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi[J].LWT,2014,57(2):603-611.
[40] CHANARAT S,BENJAKUL S.Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial transglutaminase[J].Food Hydrocolloids,2013,30(2):704-711.
文章导航

/