低温长时蒸煮对猪肉品质的影响

doi:10.3864/j.issn.0578-1752.2021.03.017

摘要/Abstract

摘要：

【目的】明确不同低温长时蒸煮条件对猪肉持水性、嫩度等食用品质的影响,从水分分布、肌纤维结构及胶原蛋白溶解方面揭示其潜在机理,为应用低温长时蒸煮加工猪肉提供理论基础。【方法】以猪背最长肌为试验材料,经不同低温（55℃和60℃）长时（4、8和24 h）加热处理后,检测蒸煮损失、体积收缩率、低场核磁共振波谱、氢质子成像、色差和剪切力,分析猪肉持水性、色泽和嫩度等品质特征;通过组织切片观察猪肉肌原纤维和结缔组织的变化,分析蛋白质表面疏水性和胶原蛋白含量及热溶解性变化。【结果】随着加热时间的延长与温度的升高,低温长时蒸煮处理对猪肉食用品质的影响逐渐增大,破坏肌纤维结构,增强蛋白质热变性程度,具体表现为:蒸煮损失显著增大（P<0.05）,体积收缩变大,不易流动水T₂弛豫时间左移（P<0.05）,且含量显著减少（P<0.05）。b*值明显增大（P<0.05）,肌原纤维收缩,肌内结缔组织逐渐溶解,肌纤维结构被破坏;蛋白质表面疏水性增大（P<0.05）;胶原蛋白含量减少（P<0.05）,溶解度增大。【结论】相对加热时间而言,加热温度对肉品食用品质和蛋白变性程度影响更为显著,延长加热时间可在一定程度上降低这种影响。加热温度不同,肉品的纵向收缩率变化更为显著,可能与不同温度下胶原蛋白尤其是不溶性胶原蛋白变性程度不同有关。

关键词: 猪肉, 低温长时蒸煮, 肌原纤维, 肌内结缔组织, 蛋白变性

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

王静帆,黄峰,沈青山,温彦涛,郭志刚,景晓亮,张春晖. 低温长时蒸煮对猪肉品质的影响[J]. 中国农业科学, 2021, 54(3): 643-652.

WANG JingFan,HUANG Feng,SHEN QingShan,WEN YanTao,GUO ZhiGang,JING XiaoLiang,ZHANG ChunHui. The Influence of Low-Temperature and Long-Time Cooking on the Quality of Pork Products[J]. Scientia Agricultura Sinica, 2021, 54(3): 643-652.

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参考文献 30

[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)

	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

	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

指标 Index	55℃			60℃
指标 Index	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