| 光谱学与光谱分析 |
|
|
|
|
|
| Effects of Freezing and Thawing Treatments on Beef Protein Secondary Structure Analyzed with ATR-FTIR |
| SUN Zhen, YANG Fang-wei, LI Xia, ZHANG Chun-hui*, XIE Xiao-lei |
| Institute of Agro-Products Processing Science and Technology，Chinese Academy of Agricultural Sciences/Comprehensive Key Laboratory of Agro-Products Processing，Ministry of Agriculture，Beijing 100193，China |
|
|
|
|
Abstract In order to further clarify the influence mechanism of different freezing temperature on meat quality in meat industry. The effects of freezing at -18, -23 and -38 ℃ on the stability of protein secondary structures of beef were studied. The attenuated total reflectance Fourier transfer infrared spectroscopy(ATR-FTIR)technique and automatic deconvolution, curve fitting and other calculation and analysis methods were used to analyze the changes of beef myofibrillar protein infrared spectra and secondary structures during -18, -23 and -38 ℃ freezing-thawing processes. ATR-FTIR results showed that the peak high and peak area of infrared spectra of beef myofibrillar protein in the freezing-thawing processes were changed, and the red shift or blue shift of wavenumbers occurred. The intensities of the absorption peak of 3 500~3 300 cm-1 in the infrared spectra of the frozen-thawed beef were reduced or even disappeared. This indicated that the intramolecular and intermolecular hydrogen bonding interactions, which formed by the bound water O—H group and the amino acid CO group, in thawed beef myofibrillar protein were broken. In other words, freezing can result in the destruction of beef myofibrillar protein secondary structures and protein advanced structures unfolded. Once the beef is thawed, the unfolded protein would reaggregation, and protein renaturation. Freezing could affect the stability of beef myofibrillar protein, the relative content of α-helix, β-sheet, and β-turn of beef myofibrillar protein were decreased, and the α-helix and ordered structures changed to the randon coil and disordered structures. After thawing, the increase of β-sheet relative content of beef myofibrillar protein at -38 ℃ was greater than that of -23 and -18 ℃. The stability of -38 ℃ frozen beef myofibrillar protein was the best, and the protein renaturation was also the best after thawing. That is, the lower the freezing temperature, the lower the measure of freezing denaturation of beef myofibrillar protein, and the better the secondary structures stability of beef myofibrillar protein. The experimental study based on the actual production condition of the meat industry. And the effect of freezing temperatures on beef protein denaturation and the possible mechanism were revealed at the micro-aspect. It can be seen that the ATR-FTIR technology can reflect the changes of protein secondary structures in the process of freezing-thawing of beef, and reveal the regularity of beef protein denaturation, which can be used to identify and evaluate the quality of frozen meat. The experimental results provide a reference for the freezing preservation process and a method for the quality evaluation of meat.
|
|
Received: 2015-11-19
Accepted: 2016-03-05
|
|
|
|
Corresponding Authors:
ZHANG Chun-hui
E-mail: dr_zch@163.com
|
|
[1] Leygonie C，Britz T J，Hoffman L C. Meat Science，2012，91(2)：96.
[2] Cheng J H，Sun D W. Comprehensive Reviews in Food Science and Food Safety，2015，14(4)：482.
[3] Glassford S E，Byrne B，Kazarian S G. Biochimica et Biophysica Acta-Proteins and Proteomics，2013，1834(12)：2850.
[4] Kazarian S G，Chan K L A. Analyst，2013，138(7)：1946.
[5] Cruz-Angeles J，Martínez L M，Videa M. Biopolymers，2015，103(10)：574.
[6] Li Yin，Jia Wei，Zhang Chunhui，et al. Food and Bioprocess Technology，2014，7：3370.
[7] Chelh I，Gatellier P，Sant-lhoutellier V. Meat Science，2006，74(4)：682.
[8] Gangidi R R，Proctor A，Pohlman F W. Journal of Food Science，2003，68(1)：124.
[9] Schmidt V，Giacomelli C，Soldi V. Polymer Degradation and Stability，2005，87：25.
[10] Ulrichs T，Drotleff A M，Ternes W. Food Chemistry，2015，172：914. |
| [1] |
FANG yao1, XIE Tian-hua2, GUO Wei1, BAI Xue-bing1, LI Xin-xing1*. On-Line Fast Detection Technology of Chilled Fresh Meat Quality Based on Hyperspectral and Multi-Parameter[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2021, 41(08): 2572-2577. |
| [2] |
SUN Zong-bao, WANG Tian-zhen, LI Jun-kui, ZOU Xiao-bo*, LIANG Li-ming, LIU Xiao-yu. Detecting Adulterated Beef Meatball Using Hyperspectral Imaging Technology[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2020, 40(07): 2208-2214. |
| [3] |
WANG Cai-xia, WANG Song-lei*, HE Xiao-guang, DONG Huan. The Identification of Beef Varieties by Fusing Image Information Based on Hypersepctral Image Technology[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2020, 40(03): 911-916. |
| [4] |
WEI Wen-song, PENG Yan-kun*, ZHENG Xiao-chun, WANG Wen-xiu. Research on Detection of Beef Freshness Parameters Based on Multi Spectral Diffuse Reflectance Method[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2019, 39(04): 1177-1185. |
| [5] |
XU Kun1, 2, 3, WANG Ju-lin1, 2, 3*, HE Qiu-ju4. The Influence of Alum in Alum Gelatin Solution on Cellulose，Calcium Carbonate and Gelatin in XUAN Paper[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2018, 38(06): 1829-1833. |
| [6] |
YE Song1，ZHANG Bing-ke1, 2，YANG Hui-hua1，ZHANG Wen-tao1，DONG Da-ming2*. Identification of Beef Spoilage Processes Using the Infrared Spectrum of Volatiles[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2017, 37(09): 2751-2755. |
| [7] |
PAN Sha-sha1, HUANG Fu-rong1*, XIAO Chi1, XIAN Rui-yi1, MA Zhi-guo2 . Rapid Identification of Epicarpium Citri Grandis via Infrared Spectroscopy and Fluorescence Spectrum Imaging Technology Combined with Neural Network[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2015, 35(10): 2761-2766. |
| [8] |
WANG Wei-wei1, 2, 3, WEI Wei-wei1, 2, 3, SONG Xiang-gang1, 2, 3, CHENG Ya-ting4, CHEN Chao1, 2, 3*, WANG Shu-mei1, 2, 3*, LIANG Sheng-wang1, 2, 3. Effects of Different Pretreatment Methods on the Phenylketonuria Screening Model by FTIR/ATR Spectroscopy[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2015, 35(05): 1218-1221. |
| [9] |
MA Shi-bang1, 2, XU Yang1*, TANG Xiu-ying1, TIAN Xiao-yu1, FU Xing1 . Prediction of Storage Time of Fresh Beef with Multi-Index Using Visible and Near-Infrared Spectroscopy [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2012, 32(12): 3242-3246. |
| [10] |
GE Shao-yang1,2, LIU Mei-yu4, ZHU Jun1,2, WANG Fang1,2, REN Fa-zheng1,2, ZHANG Lu-da3, GUO Hui-yuan1,2* . FTIR Analysis of Cosrelation between Emulsifying Properties and the Secondary Structure of the Proteins in Modified Egg Yolk Powder[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2011, 31(08): 2090-2093. |
| [11] |
WANG Yuan-feng1, WANG Lian-ming2, LI Bing1 . Exploration of the Broken Parts of a Brake Hose by ATR-FTIR and SEM [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2011, 31(04): 928-931. |
| [12] |
ZHANG Yong1, CAO Chun-yu1*, FENG Wen-ying1, XU Ming1, SU Zhen-hua1, LIU Xiao-meng2, Lü Wei-jun1 . Application of Fourier Transform Attenuated Total Reflection Infrared Spectroscopy in Analysis of Pulp and Paper Industry [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2011, 31(03): 652-655. |
| [13] |
LIU Yan-yan1, ZENG Xin-an1*，CHEN Xiao-dong2 . Effects of Pulsed Electric Fields and Heat Treatments on SPI Structure Analyzed by FTIR [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2010, 30(09): 2340-2344. |
| [14] |
WU Jian-hu, PENG Yan-kun*, CHEN Jing-jing, WANG Wei, GAO Xiao-dong, HUANG Hui . Study of Spatially Resolved Hyperspectral Scattering Images for Assessing Beef Quality Characteristics [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2010, 30(07): 1815-1819. |
| [15] |
YANG Jian-song，MENG Qing-xiang，REN Li-ping*，ZHOU Zhen-ming，XIE Xiang-xue . Rapid Evaluation of Beef Quality by NIRS Technology[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2010, 30(03): 685-687. |
|
|
|
|
