Scientia Agricultura Sinica ›› 2021, Vol. 54 ›› Issue (3): 643-652.doi: 10.3864/j.issn.0578-1752.2021.03.017

• FOOD SCIENCE AND ENGINEERING • Previous Articles     Next Articles

The Influence of Low-Temperature and Long-Time Cooking on the Quality of Pork Products

WANG JingFan1(),HUANG Feng1,SHEN QingShan1,WEN YanTao2,GUO ZhiGang2,JING XiaoLiang2,ZHANG ChunHui1()   

  1. 1Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193
    2Jiangsu Chaoyue Agricultural Development Co. LTD, Taixing 225400, Jiangsu
  • Received:2020-06-19 Accepted:2020-10-14 Online:2021-02-01 Published:2021-02-01
  • Contact: ChunHui ZHANG E-mail:wangjingfansnnu3@163.com;dr_zch@163.com

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Abstract:

【Objective】The objective of this study was to investigate the effect of low-temperature and long-time (LTLT) cooking on water holding capacity (WHC) and tenderness of pork. It was expected to illustrate the potential mechanism for the change of moisture distribution, muscle fiber structure, and collagenolysis of the LTLT cooked pork, so as to provide a scientific basis for the actual industrial application. 【Method】The pork Longissmus dorsi was used as experimental material which was boiled at different low-temperature (55℃ and 60℃) for long-time (4 h, 8 h, and 24 h) respectively. The quality characteristics of LTLT cooked pork, including WHC, color and tenderness, were analyzed by cooking loss rate, area shrinkage, low field nuclear magnetic resonance (LF-NMR), magnetic resonance imaging (MRI), color, and Warner-Bratzler shear force. The structural changes of myofibrils and connective tissue were observed by histological analysis. Then the surface hydrophobicity, collagen content, and its thermal solubility were analyzed.【Result】With the increasing of heating time and temperature, the influence of LTLT cooking on the quality of pork products and the protein denaturation increased. The muscle fiber structure was damaged during heating. Specifically, the cooking loss rate and area shrinkage ratio increased significantly (P<0.05); LF-NMR and MRI analysis demonstrated that the transverse relaxation time (T22) and peak area (A22) decreased markedly (P<0.05); the b* value increased (P<0.05). The shrinkage of myofibrils and collagen fibers in the perimysium dissolving occurred, the surface hydrophobicity enhanced significantly (P<0.05). The content of collagen decreased observably (P<0.05), while heat solubility increased. 【Conclusion】Compared with heating time, heating temperature had more significant effects on meat quality and protein denaturation, and these effects could be alleviated by extending the heating time. At different heating temperatures, the difference in the longitudinal shrinkage ratio was more significant, which might be caused by different denaturation of collagen, especially the insoluble collagen.

Key words: pork, low-temperature long-time cooking, myofiber, connective tissue, protein denaturation

Fig. 1

Effects of heating temperature and time on cooking loss Different capital letters indicate significantly differences among different heating temperatures and the same heating time (P<0.05); Different lowercase letters indicate significantly differences among same heating temperature and different heating time (P<0.05). The same as below"

Fig. 2

Effects of heating temperature and time on shear force"

Table 1

Effect of heating temperature and time on color"

55℃ 60℃
4 h 8 h 24 h 4 h 8 h 24 h
L* 81.28±0.73Aa 81.59±0.54Aa 81.61±0.50Aa 82.63±0.36Aa 82.79±0.51Aa 82.80±0.42Aa
a* 6.18±0.42Aa 6.57±0.37Aa 6.64±0.20Aa 5.50±0.21Aa 5.64±0.42Aa 5.77±0.26Ba
b* 6.00±0.30Ba 6.05±0.32Ba 6.14±0.16Ba 6.75±0.11Ab 6.79±0.06Ab 7.30±0.17Aa
?E 27.56±1.80Aa 27.87±1.26Aa 27.88±1.22Aa 28.97±0.90Aa 29.14±1.26Aa 29.19±1.05Aa

Fig. 3

Effect of heating temperature and time on area shrinkage"

Table 2

Moisture distribution and composition of pork after different temperature and time heating"

T21 (ms) T22 (ms) T23 (ms) A21 (%) A22 (%) A23 (%)
55℃-4h 0.56±0.18Aa 36.59±1.90Ab 207.87±17.17Aa 2.66±0.01Bb 96.08±0.00Ba 0.97±0.00Aa
55℃-8h 0.57±0.15Aa 34.91±1.33Aab 217.70±17.34 Ba 3.00±0.00Bab 95.89±0.00Aa 1.11±0.00Aa
55℃-24h 0.58±0.12Aa 33.73±1.48Aa 222.98±20.32 Ba 3.22±0.00Ba 95.85±0.00Aa 0.93±0.00Aa
60℃-4h 0.40±0.02 Aa 32.22±1.80Ba 215.61±23.17Ac 3.46±0.00Ab 95.69±0.00Aa 0.86±0.00Aa
60℃-8h 0.43±0.01 Aa 29.38±1.82Bb 250.13±19.93Ab 3.86±0.00Aa 95.32±0.00Ba 0.77±0.00Ba
60℃-24h 0.37±0.05Ba 29.36±1.29Bb 280.90±24.19Aa 3.91±0.00Aa 95.55±0.00Aa 0.50±0.00Bb

Fig. 4

Proton density weighted pseudo color images of pork after different temperature and time heating"

Fig. 5

Sections of muscle tissue in meat during different temperature and time heating"

Fig. 6

Effect of heating temperature and time on protein surface hydrophobicity"

Table 3

Effect of heating temperature and time on collagen"

指标
Index		 55℃ 60℃
4 h 8 h 24 h 4 h 8 h 24 h
总胶原蛋白含量
Total collagen content (mg?g-1)		 1.34±0.09Aa 0.74±0.05Ab 0.61±0.03Ab 0.80±0.05Ba 0.55±0.02Bb 0.49±0.06Ab
热溶性胶原蛋白含量
Heat soluble collagen content (mg?g-1)		 0.10±0.07Ab 0.12±0.01Aab 0.13±0.00Aa 0.10±0.05Bb 0.14±0.00Aa 0.13±0.00Aa
胶原蛋白溶解度 Collagen solubility 0.09±0.01Bb 0.19±0.01Aa 0.17±0.01Aa 0.17±0.00Ab 0.17±0.02Ab 0.29±0.04Aa
[1] BERTRAM H C, AASLYNG M D, ANDERSEN H J. Elucidation of the relationship between cooking temperature, water distribution and sensory attributes of pork - A combined NMR and sensory study. Meat Science, 2005,70(1):75-81.
[2] DOMINGUEZ-HERNANDEZ E, SALASEVICIENE A, ERTBJERG P. Low-temperature long-time cooking of meat: Eating quality and underlying mechanisms. Meat Science, 2018,143:104-113.
pmid: 29730528
[3] WARNER R D, KAUFFMAN R G, GREASER M L. Muscle protein changes post mortem in relation to pork quality traits. Meat Science, 1997,45(3):339-352.
[4] BERHE D T, ENGELSEN S B, HVIID M S, LAMETSCH R. Raman spectroscopic study of effect of the cooking temperature and time on meat proteins. Food Research International, 2014,66:123-131.
[5] 孙红霞, 黄峰, 丁振江, 张春江, 张良, 张泓. 不同加热条件下牛肉嫩度和保水性的变化及机理. 食品科学, 2018,39(1):84-90.
SUN H X, HUANG F, DING Z J, ZHANG C J, ZHANG L, ZHANG H. Changes in tenderness and water-holding capacity and underlying mechanism during beef stewing. Food Science, 2008,39(1):84-90. (in Chinese)
[6] LEPETIT J. A theoretical approach of the relationships between collagen content, collagen cross-links and meat tenderness. Meat Science, 2007,76(1):147-159.
[7] ZIELBAUER B I, FRANZ J, VIEZENS B, VILGIS T A. Physical aspects of meat cooking: Time dependent thermal protein denaturation and water loss. Food Biophysics, 2016,11(1):34-42.
[8] TORNBERG E. Effects of heat on meat proteins-Implications on structure and quality of meat products. Meat Science, 2005,70(3):493-508.
pmid: 22063748
[9] HUGHES J M, OISETH S K, PURSLOW P P, WARNER R D. A structural approach to understanding the interactions between colour, water-holding capacity and tenderness. Meat Science, 2014,98(3):520-532.
doi: 10.1016/j.meatsci.2014.05.022
[10] 高儒松, 张春霞, 赵红艳. 肌肉组织学特性与肉品质的关系. 肉类研究, 2009(5):11-15.
GAO R S, ZHANG C X, ZHAO H Y. Muscular histological characteristics and meat quality. Meat Research, 2009(5):11-15. (in Chinese)
[11] CHRISTENSEN L, BERTRAM H C, AASLYNG M D, CHRISTENSEN M. Protein denaturation and water-protein interactions as affected by low temperature long time treatment of porcine Longissimus dorsi. Meat Science, 2011,88(4):718-722.
doi: 10.1016/j.meatsci.2011.03.002
[12] CHRISTENSEN L, ERTBJERG P, AASLYNG M D, CHRISTENSEN M. Effect of prolonged heat treatment from 48℃ to 63℃ on toughness, cooking loss and color of pork. Meat Science, 2011,88(2):280-285.
doi: 10.1016/j.meatsci.2010.12.035
[13] WANG F L, ZHANG Y W, LI J K, GUO X Y, CUI B W, PENG Z Q. Contribution of cross-links and proteoglycans in intramuscular connective tissue to shear force in bovine muscle with different marbling levels and maturities. LWT-Food Science and Technology, 2016,66:413-419.
[14] WANG C, WANG H, LI X, ZHANG C H. Effects of oxygen concentration in modified atmosphere packaging on water holding capacity of pork steaks. Meat Science, 2019,148:189-197.
doi: 10.1016/j.meatsci.2018.10.001 pmid: 30336963
[15] KONG F B, TANG J M, LIN M S, BARBARA RASCO. Thermal effects on chicken and salmon muscles: Tenderness, cook loss, area shrinkage, collagen solubility and microstructure. LWT-Food Science and Technology, 2008,41(7):1210-1222.
[16] LI S J, MA R C, PAN J F, LIN X P, DONG X P, YU C X. Combined effects of aging and low temperature, long time heating on pork toughness. Meat Science, 2019,150:33-39.
doi: 10.1016/j.meatsci.2018.12.001 pmid: 30562641
[17] MITRA B, RINNAN A, RUIZ-CARRASCAL J. Tracking hydrophobicity state, aggregation behaviour and structural modifications of pork proteins under the influence of assorted heat treatments. Food Research International, 2017,101:266-273.
pmid: 28941693
[18] STARKEY C P, GEESINK G H, HUTTON ODDY V, HOPKINS D L. Explaining the variation in lamb longissimus shear force across and within ageing periods using protein degradation, sarcomere length and collagen characteristics. Meat Science, 2015,105:32-37.
doi: 10.1016/j.meatsci.2015.02.011 pmid: 25768395
[19] 李超, 徐为民, 王道营, 高峰, 周光宏. 加热过程中肉嫩度变化的研究. 食品科学, 2009,30(11):262-265.
LI C, XU W M, WANG D Y, GAO F, ZHOU G H. Heat induced change of meat tenderness. Food Science, 2009,30(11):262-265. (in Chinese)
[20] CHRISTENSEN M, PURSLOW P P, LARSEN L M. The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue. Meat Science, 2000,55(3):301-307.
doi: 10.1016/s0309-1740(99)00157-6 pmid: 22061287
[21] 余小领, 李学斌, 陈会. 猪肉色泽和保水性的相关性研究. 食品科学, 2009(23):39-41.
YU X L, LI X B, CHEN H. Relationship between pork color and water-holding capacity. Food Science, 2009(23):39-41. (in Chinese)
[22] BERTRAM H C, WU Z, BERG F V D, ANDERSEN H J. NMR relaxometry and differential scanning calorimetry during meat cooking. Meat Science, 2006,74(4):684-689.
doi: 10.1016/j.meatsci.2006.05.020 pmid: 22063224
[23] 王策. 含氧气调包装对冷却肉持水性的影响机制[D]. 北京: 中国农业科学院, 2018.
WANG C. The effect of different oxygen concentrations in modified atmosphere packaging on water holding capacity of chilled meat[D]. Beijing: Chinese Academy of Agricultural Sciences, 2018. (in Chinese)
[24] DEL PULGAR J S, GAZQUEZ A, RUIZ-CARRASCAL J. Physico- chemical, textural and structural characteristics of sous-vide cooked pork cheeks as affected by vacuum, cooking temperature, and cooking time. Meat Science, 2012,90(3):828-835.
doi: 10.1016/j.meatsci.2011.11.024 pmid: 22154568
[25] TRAORE S, AUBRY L, GATELLIER P, PRZYBYLSKI W, JAWORSKA D, KAJAK-SIEMASZKO K, SANTE-LHOUTELLIER V. Effect of heat treatment on protein oxidation in pig meat. Meat Science, 2012,91(1):14-21.
pmid: 22209093
[26] 刘晶晶, 雷元华, 李海鹏, 谢鹏, 万红兵, 黄彩燕, 孙宝忠, 张松山. 加热温度及时间对牛肉胶原蛋白特性及嫩度的影响. 中国农业科学, 2018,51(5):977-990.
LIU J J, LEI Y H, LI H P, XIE P, WAN H B, HUANG C Y, SUN B Z, ZHANG S S. Effects of heating temperature and time on collagen properties and tenderness in beef. Journal of Integrative Agriculture, 2018,51(5):977-990. (in Chinese)
[27] WANG D, DONG H, ZHANG M, LIU F, BIAN H, ZHU Y Z, XU W M. Changes in actomyosin dissociation and endogenous enzyme activities during heating and their relationship with duck meat tenderness. Food Chemistry, 2013,141(2):675-679.
doi: 10.1016/j.foodchem.2013.04.034 pmid: 23790834
[28] PURSLOW P P. Contribution of collagen and connective tissue to cooked meat toughness; some paradigms reviewed. Meat Science, 2018,144:127-134.
doi: 10.1016/j.meatsci.2018.03.026 pmid: 29636208
[29] 刘越. 不同理化因素对牛肉肌红蛋白稳定性影响的研究[D]. 南京: 南京农业大学, 2017.
LIU Y. Study on the effect of different physical and chemical factors on the stability of beef myoglobin[D]. Nanjing: Nanjing Agricultural University, 2017. (in Chinese)
[30] 向丹. 不同理化因素对猪肉肌红蛋白稳定性的影响研究[D]. 重庆: 西南大学, 2010.
XIANG D. The effect of different physical and chemical factors on pork myoglobin stability[D]. Chongqing: Southwest University, 2010. (in Chinese)
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