Food and Fermentation Industries >

2020 , Vol. 46 >Issue 6: 163 - 169

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.022756

Effect of key processing point of western-style ham on the structure and flavor adsorption capacity of myofibrillar protein

  • HU Ke ,
  • CHANG Rui ,
  • ZHU Qiujin ,
  • TANG Pengyu ,
  • LIU Chunli ,
  • SONG Li ,
  • DENG Li ,
  • HU Ping ,
  • HE Laping ,
  • ZENG Xuefeng ,
  • YE Chun
Expand
  • 1 (School of Liquor & Food Engineering,Guizhou University, Guiyang 550025,China)
    2 (Guizhou Province Key Laboratory of Agricultural and Animal Products Storage and Processing, Guiyang 550025,China)

Received date: 2019-11-08

  Online published: 2020-04-24

Fold

Abstract

In order to explore the effects of the key processing operations of western-style ham on the structure and flavor adsorption capacity of myofibrillar proteins, the myofibrillar proteins of each key processing operations were extracted. Combining fourier transform infrared with ultraviolet and fluorescence spectroscopy information, the total amount of myofibrillar sulfhydryl content, surface hydrophobicity and secondary structure were analyzed. The effects of myofibrillar proteins on flavor adsorption were investigated by head-space solid-phase microextraction combined with gas chromatography-mass spectrometry (SPME-GC-MS). The result has shown that with the raw meat as the control, the total amount of sulfhydryl content in myofibrillar protein showed a downward trend and the content of chopping was the lowest (P<0.05). The surface hydrophobicity of myofibrillar protein was significantly increased (P<0.05) and the highest was in the vacuum rolling which was 61% higher than that of raw meat. The amide A band, the amide B band and the amide III band of myofibrillar protein had different degrees of movement at different key processing operations. The fluorescence peaks were red-shifted at the pickling, vacuum rolling and chopping and the maximum absorption peak of ultraviolet was also red-shifted at the pickling and vacuum rolling. Furthermore, it also showed that the structure of protein has changed and the microenvironment of amino acids changed to a polar environment that was favorable for flavor adsorption. The adsorption of 4-ethyl guaiacol was different in key processing operations and the myofibrillar protein adsorption capacity of vacuum rolling was strongest, reaching 30.21%. The result has important guiding significance for the application of liquid smoke in western-style ham production, and provide a reference for the research of meat production and flavor formation mechanism.

Key words： western-style ham; myofibrillar protein; flavour adsorption; structural of protein; vacuum rolling

Cite this article

HU Ke , CHANG Rui , ZHU Qiujin , TANG Pengyu , LIU Chunli , SONG Li , DENG Li , HU Ping , HE Laping , ZENG Xuefeng , YE Chun . Effect of key processing point of western-style ham on the structure and flavor adsorption capacity of myofibrillar protein[J]. Food and Fermentation Industries, 2020 , 46(6) : 163 -169 . DOI: 10.13995/j.cnki.11-1802/ts.022756

References

[1] WANG Y, JIANG,Y T, CAO J X, et al. Study on lipolysis-oxidation and volatile flavour compounds of dry-cured goose with different curing salt content during production[J]. Food Chemistry,2016,190:33-40.
[2] LOU X W, YANG Q L, SUN Y Y, et al. The effect of microwave on the interaction of flavour compounds with G-actin from grass carp (Catenopharyngodon idella)[J]. Journal of the Science of Food and Agriculture, 2017,97(12):3 917-3 922.
[3] SHEN H, ZHAO M M, SUN W Z. Effect of pH on the interaction of porcine myofibrillar proteins with pyrazine compounds. Food Chemistry, 2019,287:93-99.
[4] PÉREZ-JUAN, M, FLORES, M, TOLDRÁ, F. Binding of aroma compounds by isolated myofibrillar proteins: Effect of protein concentration and conformation[J].Food Chemistry,2007,105(3):932-939.
[5] ZHOU F B, ZHAO M M, SU G W, et al. Binding of aroma compounds with myofibrillar proteins modified by a hydroxyl-radical-induced oxidative system[J]. Journal of Agricultural and Food Chemistry,2014,62(39):9 544-9 552.
[6] LV T, WANG Y, PAN D D, et al. Effect of trypsin treatments on the structure and binding capacity of volatile compounds of myosin[J]. Food Chemistry,2017,214:710-716.
[7] 彭林,马良,戴宏杰,等.多酚与肌原纤维蛋白相互作用机制及其对蛋白特性的影响研究进展[J/OL].食品科学:1-11[2019-11-08].http://kns.cnki.net/kcms/detail/11.2206.ts.20190917.1752.129.html.
[8] 蒋丽施.西式火腿类低温肉制品品质变化研究[D]. 重庆:西南大学, 2012.
[9] 高宁宁,胡萍,朱秋劲,等. 烟熏液及其在肉制品中的应用研究进展[J]. 肉类研究, 2019,33(1):66-70.
[10] 刘登勇,王逍,吴金城,等. 肉制品烟熏风味物质研究进展[J]. 肉类研究, 2018,32(10):53-60.
[11] 王维君,张义,王稳航. 3种烟熏液的成分分析及其对肠衣性能的影响[J]. 食品研究与开发, 2016,37(6):161-165.
[12] SHEN H, HUANG M, ZHAO M, et al. Interactions of selected ketone flavours with porcine myofibrillar proteins: The role of molecular structure of flavour compounds[J]. Food Chemistry, 2019,298:125060.
[13] 吕彤,林俊杰,周昌瑜,等. 热处理强度对猪肉肌球蛋白结构及风味成分吸附特性的影响[J]. 农业工程学报, 2016,32(8):285-291.
[14] ZHANG Z, YANG Y, ZHOU P, et al. Effects of high-pressure modification on conformation and gelation properties of myofibrillar protein[J]. Food Chemistry, 2017,217:678-686.
[15] ZHANG Z, REGENSTEIN J M, ZHOU P, et al. Effects of high intensity ultrasound modification on physicochemical property and water in myofibrillar protein gel[J]. Ultrasonics Sonochemistry, 2017,34:960-967.
[16] 曹锦轩,张玉林,韩敏义,等.腊肉加工过程中肌原纤维蛋白结构的变化[J].中国农业科学,2013,46(18):3 871-3 877.
[17] XU Y, ZHAO J, WANG R, et al. Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins[J]. J Sci Food Agric, 2019,99(11):5 028-5 034.
[18] BOYER C, JOANDEL S, OUALI A, et al. Determination of surface hydrophobicity of fast and slow myosins from rabbit skeletal muscles: implication in heat-induced gelation[J]. Journal of the Science of Food and Agriculture, 1996,72(3):367-375.
[19] 蓝蔚青,胡潇予,阮东娜,等. 傅里叶红外结合拉曼分析卡拉胶寡糖对南美白对虾蛋白结构影响[J]. 光谱学与光谱分析, 2019,39(8):2 507-2 514.
[20] 李庆舒,程琳,邓红,等.三种多酚与牛血清蛋白相互作用的初步研究[J].食品与发酵工业,2020,46(3):128-135.
[21] 康怀彬, 邹良亮, 张慧芸, 等. 高温处理对牛肉蛋白质化学作用力及肌原纤维蛋白结构的影响[J]. 食品科学, 2018,39(23):80-86.
[22] 周昌瑜,蒋娅婷,曹锦轩,等.肌原纤维蛋白浓度对风味物质吸附能力的影响[J].核农学报,2016,30(5):904-911.
[23] ZHAO X, HAN G, SUN Q, et al. Influence of lard-based diacylglycerol on the rheological and physicochemical properties of thermally induced pork myofibrillar protein gels at different pH levels[J]. LWT, 2020,117:108 708.
[24] 胡熠,张进杰,唐艳,等. 没食子酸对海鳗肌原纤维蛋白氧化及凝胶特性的影响[J]. 核农学报, 2019,33(11):2 203-2 210.
[25] 鲁小川,窦川林,尚永彪.鼠尾草提取物对鲢鱼肌原纤维蛋白结构及功能特性的影响[J].食品与发酵工业,2019,45(15):100-107.
[26] 周丹蕾. 胞红蛋白的巯基修饰与光谱检测[J]. 光谱学与光谱分析, 2019,39(9):2 868-2 872.
[27] CHELH I, GATELLIER P, SANTÉ-LHOUTELLIER V. Technical note: A simplified procedure for myofibril hydrophobicity determination[J]. Meat Science, 2006,74(4):681-683.
[28] 曾斯杰,刘红,王友法,等. 近红外光谱在食品工业应用的研究进展[J]. 中国调味品, 2019,44(7):179-183.
[29] 冯静.脆肉鲩脆性形成过程中肌肉蛋白结构及风味成分变化研究[D]. 上海:上海海洋大学, 2017.
[30] LEFEVRE F, FAUCONNEAU B, THOMPSON J W, et al. Thermal denaturation and aggregation properties of atlantic salmon myofibrils and myosin from white and red muscles[J]. Journal of Agricultural and Food Chemistry, 2007,55(12):4 761-4 770.
[31] ANTOSIEWICZ J M, SHUGAR D. UV-Vis spectroscopy of tyrosine side-groups in studies of protein structure. Part 1: basic principles and properties of tyrosine chromophore[J]. Biophys Review, 2016,8(2):151-161.
[32] DUFOUR E, MARDEN M C, HAERTLÉ T. β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites[J]. FEBS Letters, 1990, 277(1－2): 223-226.
[33] VOILLEY C D A A. Effect of food composition and microstructure on volatile flavour release[J]. Trends in Food Science & Technology, 1997,8(11):364-368.
Options
Outlines

/

〈 〉

Powered by Beijing Magtech Co. Ltd,.