摘要
猪肉的生鲜品质具有复杂而多元的特性,对其形成机理、控制和评价一直是肉品科学研究的焦点。迄今为止,对猪肉生鲜品质的形成机理及其评价研究大量地集中在正常肉和劣质肉(如PSE肉)之间的差异及胴体瘦肉率等方面,而对不同品种、饲养方式特别是规模化快速养殖生产下猪肉生鲜品质的形成、控制和评价研究尚缺乏令人满意的解释和有效方法。
本研究以浙江优质地方品种金华两头乌和目前国内普遍养殖的纯外来的三元杂交品种“杜长大”为研究对象,利用差异蛋白质组学、低场核磁共振和电子舌等技术对现代猪肉生产条件下,不同品种和饲养时间的猪肉生鲜品质进行了深入的研究,通过宰前处理对宰后生鲜猪肉品质影响的机理和实际作用效果研究,探索并提出了提高生鲜猪肉品质可操作和实际应用的方法和途径;通过对构成肌肉的主要物质蛋白质表达的差异、水分存在状态的变化及其与抗氧化能力等之间的关系,探索了猪肉生鲜品质的形成机理,建立了用于品质评价的相应方法;利用本实验室前期研制的多频脉冲电子舌对肉质进行辩识和评价的研究,探索了利用电子舌对宰后各猪肉生鲜品质的评价监测和货架寿命(新鲜度)的控制方法。实验结果为不同品种,养殖时间,饲料和营养浓度,饲喂模式,动物福利,屠宰加工等变化导致的肉质差异进行快速监测、评定和等级标注提供了理论和技术依据。主要研究内容和结果如下:
1、一水肌酸和丁氨丙磷宰前处理对生鲜猪肉品质的影响
在杜长大肥育猪饲料中添加一水肌酸(CMH)(500g/t),可以有效改善宰后猪肉的品质。本研究结果表明,使用CMH后,肥育猪的眼肌面积提高了9.04%(P＜0.01),背最长肌比率提高了15.73%(P＜0.01),脂肪比率及第十肋骨处的背膘厚则有所下降;与对照组比较,背最长肌粗脂肪含量提高了34.75%(P＜0.01),而水分则下降了4.06%(P＜0.05),肌酸含量上升了14.27%(P＜0.01),糖原含量上升了8.81%(P＜0.05),肌苷酸含量提高29.21%(P＜0.01),肌苷含量提高32.14%(P＜0.01),而胶原蛋白下降了13.79%(P＜0.01);背最长肌24小时的滴水损失降低了30.43%(P＜0.01),肌酸激酶活率提高了16.4%(P＜0.01);血清中的游离脂肪酸和葡萄糖的含量,分别提高了13.33%(P＜0.05)和5.35%(P＜0.05),肌酸激酶的活率提高了18.84%(P＜0.05)。
宰前40-48小时开始用丁氨丙磷饮水处理,剂量为150mg/kg体重和300mg/kg体重,间隔8小时一次,可有效改善由于应激等对宰后肉质的影响。和对照组比较,试验组背最长肌24h的滴水损失分别下降25.1%和26.05%(p＜0.01);肌酸含量分别升高了12.85%和19.34%(p＜0.01);糖原含量分别上升了10.29%(p＜0.05)和16.87%(p＜0.01);而肌酸激酶的活率则提高了19.56%和24.18%(p＜0.05)。
2、基于双向电泳的猪肉生鲜品质的差异蛋白质组学研究
通过猪肉样品的制备和双向凝胶电泳实验条件方法的优化,建立了猪肌肉组织双向凝胶电泳(2-DE)方法,获得了具有统计学意义的图谱,并从图中筛选到了差异蛋白质点共345个,其中具有统计学意义(P＜0.05)又具有量分析意义的点共有33个,根据软件的进一步比对和分析,结合质谱的要求,选择了12个有意义的点作为后续质谱分析的待切点。利用MALDI-TOF-MS检测技术,对差异表达的蛋白质进行检出、分析和鉴定,通过利用肽质量指纹图谱(PMF)和MASCOT软件搜索对比分析,结果表明,地方品种猪金华“两头乌”和杜长大三元杂交猪宰后0h的样品得到了6个差异蛋白质和一个未知蛋白(斑点编号为1101),差异蛋白质分别为Predicted Protein、Actinchain A Hypothetical Protein、EST1和Myoglobin(chain B);同样,宰后24h的样品也得到了7个差异蛋白质,分别为β-2 globin、Lymphocyte antigen、SOD、β-globin、Myosin regulatory、Actin-cappingprotein和Dj-1 with sulfinic acid,提示宰后不同品种的猪背最长肌品质的差异可能是由于这些蛋白质量的变化即斑点的上调或者下调引起。由于地方品种金华“两头乌”和杜长大三元杂交猪的蛋白质数据库还没有建立,而且已建数据库中与猪肉品质相关的蛋白质也非常少,因此通过MALDI-TOF-TOF-MS只能鉴定出接近70%的差异蛋白质。
3、基于低场核磁共振的生鲜猪肉水分存在状态和分布规律研究
利用磁场强度为0.5T、共振频率为21-23MHz的核磁共振仪对宰后不同时间生鲜猪肉的横向弛豫时间T_2进行研究。结果表明,代表猪肉结合水的T_(21),各猪肉样品几乎没有差异且十分恒定一致;但代表猪肉不易流动水的T_(22),金华两头乌和杜长大存在较明显的差异,金华两头乌猪无论屠宰体重如何,在宰后的0h、12h、24h和36h的T_(22)明显大于杜长大所有屠宰体重的猪肉;从同一品种和屠宰体重来比较,金华两头乌猪肉的变化规律十分明显,而杜长大仅在宰后6h和30h稍有增加,其它时间始终维持在较低水平;反映自由水的T_(23),金华两头乌亦高于杜长大。宰后生鲜猪肉核磁共振的横向弛豫时间能很好地反映各时间点的滴水损失,通过对T_2的进一步区分,获得了宰后猪肉水分分布和变化的详细情形,这对于认识和理解不同品质猪肉之间不易流动水的分布具有重要意义。
4、宰后肌肉组织抗氧化性、酶学变化与生鲜猪肉持水性的关系研究
宰后生鲜猪肉的抗氧化能力金华猪明显大于杜长大,而且与肉的滴水损失高度相关。表现明显的主要有猪肉超氧化物歧化酶活力、谷胱甘肽过氧化物酶(GSH-PX)活力、猪肉抑制羟自由基能力、宰后肌肉的总抗氧化能力、猪肉游离脂肪酸的含量等。谷胱甘肽过氧化物酶(GSH-PX)活力在金华猪,不管其上市体重如何,均明显高于杜长大猪,平均高出6-8倍(P＜0.05);宰后肌肉的总抗氧化能力大大高于杜长大猪,以宰后0h的数据看,60Kg的金华猪分别比各上市体重的杜长大高588%、439%和327%;75Kg的则分别高533%、395%和293%;90Kg的则分别高616%、452%和337%。对于杜长大猪,体重越小,总抗氧化能力越差,其中90Kg的比75Kg高27.7%,105Kg的则高61.1%;宰后生鲜猪肉游离脂肪酸的含量和品种关系较大,而与上市体重影响较小,金华猪明显高于杜长大(平均在3倍以上)。宰后生鲜猪肉的pH值金华猪均明显高于杜长大猪,但变化规律两个品种及各上市体重之间十分一致,即在0-12h内逐渐下降并在12h时至最低,后基本不变;杜长大猪在各个时间点的滴水损失均大于金华猪,而且随着屠宰体重的增大,滴水损失也随之增大,105Kg的杜长大猪肉在24h的滴水损失比75Kg的大87.29%,比90Kg的大64.98%;48h的滴水损失,75Kg和105Kg的杜长大均明显升高,但90Kg的滴水损失则与24h时的基本一致,72h的滴水损失75Kg明显下降,但105Kg的则仍继续增大,达5.48%,比75Kg高232%。金华猪的滴水损失的也有随屠宰体重增大而升高的趋势,但没有杜长大明显,而且在随宰后时间变化的影响较小。
5、不同品种生鲜猪肉质构变化的比较研究
对不同品种的生鲜猪肉质构研究表明,宰后生鲜猪肉的硬度、咀嚼性、胶着性变化不仅与上市体重相关,而且与品种也有很大的关系,但弹性的变化与品种无关。金华猪不论大小,其总的硬度比杜长大要高(三个上市体重的硬度平均大1倍以上);而咀嚼性整体高于杜长大猪(高1.5-2倍)。
6、生鲜猪肉品质的电子舌评价研究
利用本实验室前期研制的多频大幅脉冲电子舌,对其在宰后肉质整体特性品质辩识及评价中应用的关键技术进行了研究,通过铂金电极、金电极、钛电极、钨电极和钯电极等传感器阵列及相关检测参数的比较研究,建立了电子舌用于生鲜猪肉品质评价和新鲜度监测的方法。适合生鲜猪肉整体特性品质差异区分辨识的传感器阵列为铂金电极、金电极、钛电极、钨电极和钯电极;猪肉样品采用1∶5(g/ml)的匀浆配比检测结果较稳定;盲样检测结果表明,电子舌的辨识准确率可达85%以上(p＜0.05);基于比较计算类别之间判别距离(马氏距离)与区分效果之间的关系,发现当不同肉样之间的判别距离d＞2时,即可实现有效区分;结合主成分分析与余弦夹角度量方式,设计了评价生鲜猪肉品质的相似度,结果表明,在预先给定标准样品的情况下,利用本研究设计的相似度,可以对不同品种、贮藏时间下的各肉样进行了有效评价,且方便有效地解决了肉品新鲜度和货架寿命的监控指标和方法。
以上结果表明,宰后猪肉生鲜品质虽涉及很多因素,然后利用差异蛋白质组学、核磁共振技术来研究蛋白质表达变化和水分分布及存在状态,不仅为宰后猪肉生鲜品质的形成机理探索,而且为其评价提供了创新的思路和方法;肉品品质的电子舌研究更为现代集约化养殖下肉品质量的分级、标注以及新鲜度(货架寿命)的监测控制提供了全新的技术和方法。
The quality of fresh pork meat is a complicated and multipleunit character. Studies on its intrinsic mechanism, evaluation and management are always the hottest research fields of the meat science. Such kinds of researches have been generally focused on lean rates and differences in the quality between normal and poor meat (such as PSE). However, studies on why or how different species or feed modes especially in intensive and fast breeding conditions influence the quality of the fresh pork have not been investigated yet. Moreover, methods for effectively evaluating the quality of the fresh pork are still not well established as far as we know.
Therefore, this study was conducted to evaluate the quality of fresh pork of two different species (Jinhua pigs in the original area of Zhejiang, China (termed as JH), and hybrid pigs of Duroc×Landrace×Yorkshire, termed as DLY) with different feeding periods by using technologies of differential proteomics, low field nuclear magnetic resonance (NMR) and electronic tongue. Intrinsic mechanism underlying the determination of the quality was investigated by analyzing differences in protein expression profiles, moisture existence and antioxidative abilities among different fresh porks. In addition, feasible methods and approaches for improving the meat quality were also determined according to effects of preslaughter treatment on the quality of fresh pork. Results obtained in the present study not only provided evidence for understanding the intrinsic mechanism of the meat quality, but also valuable methods for quick monitor, evaluation and grade mark of meat quality under different conditions such as species, period, feed, breeding mode, animal welfare, slaughter and processing. The main results of the present study were as follows.
1. Effects of pre-slaughter treatment of creatine monohydrate and butafosfan on the quality of fresh pork
Creatine monohydrate (CMH) supplemented into diet of DLY at the level of 500 g/t could effectively improve the quality of fresh pork in the present study. The results showed that eye muscle area and rate of longissimus dorsi muscle after CMH-treatment increased (p < 0.01) by 9.04% and 15.73%, respectively. The contents of crude fat, moisture, creatine, glycogen, inosinic acid, and inosine in treatment groups (12.02%, 71.02%, 41.63umol/g, 92.73mg/100g, 2.30mg/g and 0.39mg/g, respectively) were significantly increased or decreased (p < 0.01) as compared with respective ones of the control group (8.92%, 74.21%, 36.43umol/g, 85.21mg/100g, 1.78mg/g and 0.28 mg/g, respectively). Moreover, CMH-treatment caused a remarkable decrease in drip loss (p < 0.01) and a significant increase in creatine kinase activity (p < 0.01) in longissimus dorsi after 24h postmortem. As for the free fat acid and glucose concentrations and creatine kinase activity in blood serum treated with CMH, they were increased (p < 0.05) by 13.33%, 5.35% and 18.84%, respectively, as compared with that of the control.
Butafosfan (T1 and T2, 150 mg/kg and 300 mg/kg by body weight, respectively) supplemented into drinking water beginning at 40-48 h of pre-slaughter (once at 8h-interval) could improve availably the influence of environment such as stress on the pork quality. Drop losses of longissimus dorsi treated with T1 and T2 were decreased (p < 0.01) by 25.10% and 26.05%, respectively, as compared with that of the control. In contrast, the contents of creatine, glycogen and creatine kinase in longissimus dorsi of both treatment groups (42.13umol/g, 93.52mg/100g and 188.36U/mg in the T1-treated group; 44.53umol/g, 99.72mg/100g, 195.63U/mg in the T2-treated group, respectively) were significantly higher than the respective one of the control (37.33umol/g, 84.79mg/100g, 157.54U/mg).
2. Differential proteomics of fresh pork
The procedure and method of differential proteomics of fresh pork were established with the pork sample preparation and experimental optimization of 2-DE. Differences in the expression profile of 345 pretein were observed between the fresh pork of JH and DLY. Among them, the profile of 33 proteins showed a significant difference as compared with their corresponding ones. Twelve points were chosen from the 33 protein points before the next measurement according to the statistical and quantity analysis and the demand of mass spectrum (MS). Then different expressed proteins were identified using the MALDI-TOF-MS and contrastively analyzed with the peptide mass fingerprinting (PMF) and MASCOT software. The results obtained from the samples prepared at 0 h indicated that there were six different proteins (predicted protein; actin chain A; hypothetical protein; EST1 and myoglobin, chain B) and an unknown protein (No. 1101) between two species of pig. As for the samples at 24 h, seven differential proteins (β-2 globin; lymphocyte antigen; SOD;β-globin; myosin regulatory; Actin-capping protein and Dj-1 with sulfinic acid) were observed. These results suggested that meat quality of porcine longissimus dorsi might be associated with these differential proteins. However, only 70% of differential proteins were identified using MALDI-TOF-TOF-MS because of the scarcity of the protein database responding to pork meat quality.
3. Effect of water-holding capacity, water status and muscle antioxidation on meat quality
Transverse relaxation time (T_2) of fresh pork sampled at different postmortern time was studied using NMR under magnetic field intensity 0.5T and resonance frequency 21-23 MHz. T_(21) representing bound water indicated that there was no significant difference in each pork meat. However, T_(22) representing uneasy fluid of water was higher (P < 0.05) in JH meat at all postmortem time (0h, 12 h, 24 h and 36 h) than that of DLY and showed significant trend from the same species or slaughter weight. The T_(22) of DLY was relatively low in the present study except the samples prepared at 6 h and 30 h. As for T_(23) representing free water, similar results were observed. The data suggested that T2 could well reflect the drip loss of each period and the detailed water distribution and variety could be obtained with the T_2 subdivision. Thus, results obtained here would provide important cues for the recognition of uneasy flow water distribution in pork meat taken from different pig species.
The antioxidation and specific enzyme activities of different meat samples were also determined. As a result, the antioxidative activity of JH fresh meat represented by some factors such as SOD, GSH-Px, inhibition ability of hydroxyl radical, total antioxidant capacity and free fat acid concentration was higher than that of DLY and exhibited a positive correlation with drip loss and texture. The activity of GSH-Px in JH was 6-8 times higher (p<0.05) than that of DLY. Total antioxidant capacity (TOAC) of JH was also greatly stronger than that of DLY. For example, TOAC in the meat of 60kg-JH at 0h-postmortern point showed about 6-, 4- and 3-fold higher than that of all three weight of DLY, respectively. And TOAC in the meat of 75kg- or 90kg-JH was about 5-, 4- and 3-fold higher, or 6-, 5- and 3-fold higher than that of all three weight of DLY, respectively. With regard to TOAC in the meat of DLY, it increased with the increase in the body weight. Free fat acid concentrations in the postmortern meat were greatly associated with the pig species, while they were almost not affected by the market weight. The free fat acid concentrations in JH meat were significantly higher (p < 0.05) than those of DLY meat, being more than 3-fold higher at average.
The results in meat texture, pH and drip loss showed that pork hardness, chewiness and gumminess were not only associated with the market weight, but also greatly depended on pig species. However, the meat elasticity was not associated with the pig species. Higher meat hardness, chewiness and pH were observed in JH pork as compared with those in DLY pork, respectively. The variation trends of pH in JH pork were consistent with that of DLY pork based on the same market weight. The pH values in pork of both species decreased continiously from 0h to 12h postmortem and then kept unchanged almostly. Drip loss of DLY pork at each postmortem period was higher than that of JH pork and increased obviously with the slaughter weight. As for JH pork, the drip loss also increased with the slaughter weight. However, no significant difference (p > 0.05) was observed.
4. Evaluation of electronic tongue on fresh pork quality
The core technique in whole characters for identificating and evaluating postmortem pork quality was studied using the pulse electronic tongue with multi-frequency and broad width prepared previously in our laboratory. And the corresponding methods and procedures were established. The sensors array and correlated test parameters were analyzed comparatively with the different electrodes and the adaptive electrodes were manufactured by platinum, aurum, titanium, tungsten and palladium. The results indicated that the homogenate proportion of pork samples was 1:5 (g/ml) and the identification accuracy of electronic tongue was up to 85% (p < 0.05) using the blind sample analysis. Different pork samples were identified effectively when the Mahalanobis distance (d) was more than 2 based on the correlation between distance arithmetic and identification result. Moreover, the similarity to assess the fresh pork quality was designed and determined by combinations with the principal component analysis and cosine angle metric mode. Thus, the meat samples from different species and storage time were evaluated effectively using the above similarity under the standard samples and the control indexes. Moreover, these methods were also confirmed to solve the corresponding problems of meat freshness and shelf life.
Based on the findings of the presnt study, the innovative approaches and methods including differential proteomics, water-holding capacity and water status were provided to discuss the intrinsic mechanism and quality evaluation of the postmortern pork characters. Furthermore, electronic tongue developed in the present study would provide one of the new methods for meat classification, label and freshness (shelf life) control under modern intensive swine production.
引文
陈华才,姜曲海.猪瘦肉型品系基础亲本的肥育性能胴体品质和血液生化指标比较[J].江苏农业科技,2000,4:61-64
陈润生,徐士清.猪肉质评定方法[J]-东北农学院学报,1983,4:39-46
陈润生.关于改善猪肉品质研究的进展[J].国外畜牧科技,1981,3:32-35
陈韬,周光宏,徐幸莲.不同持水性冷却肉的品质比较和蛋白质的DSC测定[J].食品科学,2006,27(6):31—34
陈韬,周光宏,徐幸莲.磷脂酶活性对冷却肉持水性的影响[J].食品与发酵工业,2006,32(4):153-156
陈韬,周光宏,徐幸莲.宰后肌肉蛋白质变化对冷却肉持水性的影响[J].食品工业科技,2006,27(10):87-92
邓少平,田师一.电子舌:技术背景与研究进展[J].食品与生物技术学报,2007,26(4):110-116
哈斯苏荣,杜小燕,朱蓓蕾,等.复方丁氨丙磷溶液对小鼠耐力和能量代谢的影响[J],畜牧兽医学报,2004,35(3):290-294
哈斯苏荣,蒋金书,朱蓓蕾,等.复方丁氨丙磷溶液的抗热应激作用及其机理研究[J].畜牧兽医学报,2005,36(12):1334-1338
韩剑众,董文明,葛长荣,等.中草药添加剂饲喂猪肉中CPK、GPI活性和肉质关系的研究[J].云南农业大学学报,2002,17(1):91-93
韩剑众.肉品品质及其控制[M].北京:中国农业科技出版社,2005
何大澄,肖雪媛.差异蛋白质组学及其应用[J].北京师范大学学报(自然科学版),2002,8(4):558-562
梁逸曾,俞汝勤.化学计量学[M].北京:高等教育出版社,2003
倪德斌,熊远著,邓昌彦,等.宰前处理对猪肌肉品质影响的探讨[J].华中农业大学学报,1997,16(5):380-385
钱小红,贺福初.蛋白质组学:理论与方法[M].北京:科学出版社,2004
沈元新,等.金华猪及其杂种肌肉组织学特性与肉质的关系[J].1984,2:34-41
孙玉民,等.莱芜猪及其杂种猪血液指标与胴体品质性状关系的研究[J].中国畜牧杂志,1999,35(1):14—16
陶新,许梓荣,汪以真.营养物质对生物自由基产生及清除影响的研究进展[J].中国畜牧杂志,2005,41(10):61—64
王悦先.金华猪肉质的研究-生化特性测定[J].浙江农业大学学报,1982,4:59—63
武艳萍,张绍增.血清酶活性与猪肉品质关系研究[J].山西农业大学学报,1995,15(1):69-70
夏其昌,曾嵘.蛋白质化学与蛋白质组学[M].北京:科学出版社,2004
徐士清.猪肉品质研究参考资料汇编(第二册),1988
曾士元.食肉质量的酶学研究[J].肉类研究,1989,3:1-4
曾勇庆,孙玉民,张万福,等.莱芜猪肌肉组织学特性与肉质关系的研究[J].畜牧兽医学报,1998,29(6):486-492
占秀安,许梓荣.不同硒源对肥育猪鲜肉肉色和滴水损失的影响[J].畜牧兽医学报,2004,35(5):505-509
张伟力.猪肉品质改进与评定方法进展[J].养猪,2001,3:31—33
周光宏,徐幸莲.肉品学[M].北京:中国农业科技出版社,1999
朱建和,张伟力.宰前配方对猪胴体肉质的影响[J].动物科学与动物医学,2005,2:11—14
Ackermann B.L.,Hale J.E.,Duffin K.L..The role of mass spectrometry in biomarker discovery and measurement[J].Curr Drug Metab,2006,7(5):525-539
Ames B.W.,Goodband R.D.,et al..Effect of creatine monohydrate on fishing pig growth performance,carcasscharacteristics and meat quality[J].J.Anim.Sci.,2000,78(suppl,I):824(Abstr.)
Asghar A.,Gray J.I.,Booren A.M.,et al..Effect of supranutritional dietary vitamin E levels on subcellular deposition of a-tocopherol in the muscle and on pork quality[J].J.Sci.FoodAgric.,1991,57:31-34
Barrett J.,Brophy P.M.,Hamilton J.V..Analyzing proteomic data[J].International Journal for Parasitology,2005,35:543-553
Bee G.,Lonergan S.M.,Huff-Lonergan E..Early postmortem pH influences proteolysis of cytoskeletal proteins during aging in porcine longissimus muscle[J].Journal of Animal Science,2004,182(Suppl):13
Bee G..Muscle glycogen and lactate content and pork quality traits as affected by available dietary carbohydrate in pigs[J].Journal of Animal Science,2001,79(suppl,I):19
Bendall J.R.,Swatland H.J..A review of the relationships of pH with physical aspects of pork quality[J].Meat Science,1988,24:85-126
Bendixen E..The use of proteomics in meat science[J].Meat Science,2005,71:138-149
Berg E.P.,Allee G.L..Creatine monohydrate supplemented in swine fishing diets and fresh pork quality:I.A controlled laboratory experiment[J].J.Anita.Sci.,2001,79:3075-3080
Berg E. P., Linville M. L., et al.. Dose creatine monohydrate supplemented to swine fishing rations affect pork quality[J]. J. Anim. Sci., 2000 (b) ,78 (supppl.I) : 671 (Abstr)
Berg E. P., Linville M. L., et al.. Evaluation of short-term supplementation of creatine monohydrate and alpha-lipoic acid as a means to improve fresh pork quality[J]. J. Anim. Sci., 2000 (a) ,78 (supppl.I) : (Abstr.)
Berg E. P., Spencer J. D., et al.. Dietary supplementation of creatine monohydrate in swine fishing diets improves fresh pork quality [J]. Exp. Stat. Rep. University of Missouri, Columbia, 99-103
Bertram H. C., Petersen J. S., Andersen H. J.. Relationship between RN-genotype and drip loss in meat from Danish Pigs[J]. Meat Science, 2000, 56: 49-55
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[J]. Meat science, 2005, 70: 75-81
Bertram H. C., Purslow P. P., Andersen H. J.. Relationship between Meat Structure, Water Mobility, and Distribution: A Low-Field Nuclear Magnetic Resonance Study[J]. Meat science, 2002,50: 824-829
Bertram H. C., Wu Z. Y., Berg F. V., et al.. NMR relaxometry and differential scanning calorimetry during meat cooking[J]. Meat science, 2006, 74: 684-689
Bertram H. C., Kristensen M., Andersen H. J., et al.. Functionality of myofibrillar proteins as affected by pH ionic strength and heat treatment-a low-field NMR study [J]. Meat science, 2004, 68:249-256
Bertram H. C, Schafer A., Andersen H. J.. Physical changes of significance for early post mortem water distribution in porcine M. longissimus[J]. Meat Science, 2004, 66: 915-924
Bertram H. C., Straadt I. K., Jensen J. A.. Relationship between water mobility and distribution and sensory attributes in pork slaughtered at an age between 90 and 180 days[J]. Meat Science, 2007,77: 190-195
Bertram H. C., Zhiyun W., Frans B., et al.. NMR relaxometry and differential scanning calorimetry during meat cooking[J]. Meat science, 2006, 74: 684-689
Bertram H. C., Andersen R. H., Andersen H. J.. Development in myofibrillar water distribution of two pork qualities during 10-month freezer storage[J]. Meat Science, 2007, 75: 128-133
Bertram H. C., Andrew K. W., Andersen H. J.. Visualization of drip channels in meat using NMR microimaging[J]. Meat Science, 2004, 68: 667-670
Bertram H. C., Annette S., Katja R., et al.. Physical changes of significance for early post mortem water distribution in porcine M. longissimus[J]. Meat Science, 2004, 66:915-924
Bertram H. C., Donstrup S., Karlsson A. H., et al.. Continuous distribution analysis of T2 relaxation in meat-an approach in the determination of water-holding capacity[J]. Meat Science, 2002, 60: 279-285
Bertram H. C., Henrik J. A., Anders H. K.. Comparative study of low-field NMR relaxation measurements and two traditional methods in the determination of water holding capacity of pork[J]. Meat science, 2001, 57: 125-132
Bertram H. C., Aaslyng M. D.. Physical changes of significance for early post mortem water distribution in porcine M. longissimus[J]. Meat science, 2007, 76: 524-535
Bertram H. C., Donstrup S., Karlsson et al.. Postmortem energy metabolism and pH development in porcine M. longissimus dorsi as affected by two different cooling regimes-A P-NMR spectroscopic srudy[J]. Magnetic Resonance Imaging, 2001,19: 993-1000
Bertram H. C., Purslow P. P., Andersen H. J.. Relationship between meat structure water mobility, and distribution: a low-field nuclear magnetic resonance study[J]. Journal of Agricultural and Food Chemistry, 2002, 50: 824-829
Bertrama H. C., Engelsenb S., Buska B. H., et al.. Water properties during cooking of pork studied by low-field NMR relaxation: effects of curing and the RN-gene[J]. Meat Science, 2004, 66: 437-446
Bertrama H. C., Henrik A. H., Andersena K. J.. The significance of cooling rate on water dynamics in porcine muscle from heterozygote carriers and non-carriers of the halothane gene-a low-field NMR relaxation study[J]. Meat science, 2003, 65: 1281-1291
Bertrama H. C., Jorgensen H. S., Karlssona A. H., Andersena H. J.. Post mortem energy metabolism and meat quality of porcine M. longissimus dorsi as influenced by stunning Method—A 31P NMR spectroscopic study [J]. Meat Science, 2002, 62: 113-119
Bertrama H. C., Whittaker A. K., Andersen H. J., Karlsson A. H.. Visualization of drip channels in meat using NMR microimaging[J]. Meat science, 2004, 68: 667-670
Bertrama H. C., Whittakerc A. K., Shorthosed W. R., et al.. Water characteristics in cooked beef as influenced by ageing and high-pressure treatment—an NMR micro imaging study[J]. Meat science, 2004, 66: 301-306
Birch R., Noble D., et al.. The influence of dietary creatine supplementation on performance during repeated bouts of maximal isokinetic cycling in man[J]. Eur. J. Appl. Physiol., 1994, 69: 268-270
Borisova M. A., Oreshkin E. F.. On The Water Condition in Pork Meat[J]. Meat science, 1992, 31: 257-265
Bouley J., Meunier B., Chambon C., De Smet S., Hocquette J. F. and Picard B.. Proteomic analysis of bovine skeletal muscle hypertrophy [J]. Proteomics., 2005, 5(2): 490-500
Bouley J., Chambom C., Picard B.. Mapping of bovine skeletal muscle proteins using two-dimensioned gel electrophoresis and mass spectrometry[J]. Proteomics., 2004,4(6): 1811-1824
Brannon T. A., Adams G. R., et al.. Effects of creatine loading and training on running performance and biochemical properties of rat skeletal muscle. [J]. Med Sci Sports Exerc.1997, 29: 489-495
Brundum J., Muncka L., Henckelc P., et al.. Prediction of water-holding capacity and composition of porcine meat by comparative spectroscopy[J]. Meat science, 2000, 55: 177-185
Campo, et al.. Creatinine, creatine and protein in cooked meat products[J]. Food Chemistry, 1998,63 (2) : 187-190.
Canas B., Pineiro C., Calvo E., et al.. Trends in sample preparation for classical and second generation proteomics[J]. Journal of Chromatography A, 2007, 1153: 235-258
Carbonaro M.. Proteomics: present and future in food quality evaluation [J]. Trends in Food Science & Technology, 2004, 3 (15) : 209-216
Carson J. A., Nettleton D., Reecy J. M.. Differential gene expression in the rat soleus muscle during early work overload-induced hypertrophy [J]. The Federation of American Societies for Experimental Biology Journal, 2002, 16 (2) : 207-209
Casey et al., Dose dietary creatine supplementation play a role in skeletal muscle metabolism and performance[J]. Amer. J. Clin. Nutr, 2000,72 (suppl)
Cen H., He Y.. Theory and application of near infrared reflectance spectroscopy in determination of food quality[J]. Trends in Food Science & Technology, 2007, 18: 72-83
Channon H. A., Baud S. R., Kerr M., Getal.. Effect of low voltage electrical stimulation of pig carcasses and aging in sensory attributes of fresh pork[J]. Meat Science, 2003, 65: 1315-1324
Channon H. A., Walker P. J., Kerr M., et al.. Application of constant current, low voltage electrical stimulation systems to pig carcasses and its effects on pork quality[J]. Meat Science, 2003, 65: 1309-1313
Chaze T., Bouley J., Chambon C., Barboiron C. and Picard B.. Mapping of alkaline proteins in bovine skeletal muscle[J]. Proteomics., 2006, 6(8): 2571-2575
Cheah K. S., Cheah A. M. and Waring J. C.. Phospholipase A2 activity, calmodulin, Ca2+ and meat quality in young and adult halothane-sensitive and halothane-insensitive British Landrace Pigs[J]. Meat Science, 1986, 17: 37-53
Cheah K. S., Chreah A. M. and Krausgrill D. J.. Effect of dietary supplementary vitamin E on pig meat quality [J] .Meat Science, 1995,39: 255-265
Corino C, Oriani G., Pantaleo L., et al.. Influence of dietary vitamin E supplementation on "heavy" pig carcass characteristics, meat quality, and vitamin E ststus[J]. J. Anim. Sci., 1999, 77:1755-1761
Corton M, Villuendas G., Botella J. I., San Millan J. L., Escobar-Morreale H. F. and Peral B.. Improved resolution of the human adipose tissue proteome at alkaline and wide range pH by the addition of hydroxyethyl disulfide[J]. Proteomics., 2004,4(2): 438-441
D'Souza D. N., Dunshea F. R., Warner R. D., et al.. The effect of handling pre-slaughter and carcass processing rate post-slaughter on work quality[J]. Meat Sci., 1998, 50: 429-437
D'Souza D. N., Warner R. D., Dunshea F. R., et al.. Comparison of different dietary magnesium supplements on pork quality[J]. Meat Sci., 1999, 51: 221-255
D'Souza D. N., Warner R. D., Leury B. J., et al.. Effect of dietary magnesium aspartate supplements on pork quality[J]. J. Anim. Sci., 1998, 76: 104-109
Davis K. J., Sebranek J. G., Huff-Lonergan E., et al.. The effects of aging on moisture-enhanced pork loins[J]. Meat Science, 2004, 66: 519-524
Den M. J., Hertog Meischke A. F., Smulders J. M., et al.. The effect of dietary vitamin E supplementation on drip loss of bovine longissiums lumborum,psoas major and semitentendinosus muscles[J]. Meat Sci., 1997,45 (2) : 153-160
Deng Y., Rosenvold K., Karlsson A. H., et al.. Relationship between thermal denaturation of porcine muscle proteins and water-holding capacity[J]. Journal of Food Science, 2002, 67 (5) : 1642-1647
Dick F. M., Wiel V. D., Zhang W. L.. Identification of pork quality parameters by proteomics[J]. Meat Science, 2007, (77) : 46-54
Dikeman M. E.. Effects of metabolic modifiers on carcass traits and meat quality[J]. Meat Science, 2007, (77) : 121-135
Doherty M. K., Mclean L., Hayter J. R., et al.. The proteome of chicken skeletal muscle: Changes in soluble protein expression during growth in a layer strain[J]. Proteomics., 2004, 4(7): 2082-2093
Domon B., Aebersold R.. Mass spectrometry and protein analysis[J]. Science, 2006, 312 (5771 ) : 212-217
Eambrecht E. J., Eissen J., Nooijen R. I. J., et al.. Preslaughter stress and muscle energy largely determine pork quality at two commercial processing plants[J]. J. Anim. Sci., 2004, 82: 1401-1409
Earnest, et al.. The effect of creatine monohydrate ingestion on anaerobic power Indices, muscular strength and body composition [J]. Acta. Physiol. Scand., 1995, 153
Eikelenboom G., Bolink A. H.. The effect of feedstuff composition, sex and age of slaughter on pork quality[J]. In Proceedings of the 37th International Congress on Meat Science & Techonlogy, 1991, Kulmbach, Germany
Fenselau C.. A review of quantitative methods for proteomic studies[J]. Journal of Chromatography B, 2007, (855) : 14-20
Fialka I., Pasquali C., Lottspeich F.. Subcellular fractionation of polarized epithelial cells and identification of organelle-specific proteins by two-dimensional gel electrophoresis[J]. Electrophoresis, 1997, 18 (14) : 2582-2590
Freking B. A., Murphy S. K., Wylie A. A., et al.. Identification of the single base change causing the callipyge muscle hypertrophy phenotype, the only known example of polar over dominance in mammals[J]. Genome Research, 2002, 12 (10) : 1496-1506
Fung B. M., Puon P. S.. Nuclear magnetic resonance transverse relaxation in muscle water[J]. Biophysical Society, 1981, 33: 27-38
Gardner M. A., Huff-Lonergan E., Lonergan S. M.. Prediction of fresh pork quality using indictors of protein degradation and calpain activation [J]. In Proceedings, 51st international congress of meat science and technology, 2005, 51
Garniera J. P., Klont R., Plastow G.. The potential impact of current animal research on the meat industry and consumer attitudes towards meat[J]. Meat Science, 2003, (63) : 79-88
Gispert M., Font I., Furnols M., et al.. Relationships between carcass quality parameters and genetic types[J]. Meat science, 2007, (77) : 397-404
Goodband R. D., et al.. Effects of creatine monohydrate on fishing pig growth performance, carcass characteristics and meat quality[J]. J. Anim. Feed Sci. Tech., 2002, (96) : 135
Gorg A., Obermaier C., Boguth G., et al.. The current state of two-dimensional electrophoresis with immobilized pH gradients[J]. Electrophoresis, 2000, 21: 1037-1053
Gorg A., Weiss W., Michael J. D.. Current two-dimensional electrophoresis technology for proteomics [J]. Proteomics., 2004, 4 (12) .3665-3685
Gottlieb D. M., Schultz J., Petersen M., et al.. Determination of wheat quality by mass spectrometry and multivariate data analysis[J]. Rapid Communication in Mass Spectrometry, 2002,16:2034-2039
Greenhaff P. L.. Creatine supplement: Recent developments[J]. Br. J. sports. Med., 1996, 30: 276-277
Greenhaff P. L.. The nutritional biochemistry of creatine[J]. J. Nutr. Biochem., 1997, 8
Griffin J. L., Williams H. J., Sang E., et al.. Proteomic analysis of rat soleus and tibialis anterior muscle following immobilization[J]. Analytical Biochemistry, 2001, 1 (293) : 16-21
Hamilton D. N.. On-farm and pre-slaughter magement approacher to reducing stress respons and improving pork quality in pigs[J]. 2002a, http://www.lib.global.umi.com/dissertations/preview-ad3070315
Hamilton D. N., Ellis M., Hermann M. D., et al.. The impact of longissimus glycolytic potential and short-term feeding of magnesium sulfate heptahydrate prior to slaugher on carcass characteristics and pork quality[J]. J. Anim. Sci., 2002, 80: 1586-1592
Han J. Z., Wan Y. B.. Proteomics: present and future in food science and technology[J]. Trends in Food Science & Technology, 2008, 19 (1) : 26-30
Harris R. C., Soderlund K., et al.. Evaluation of creatine in resting and exercised muscle of normal subjects by creatine supplemention[J]. J. Clin. Sci., 1992, 83: 367-374
Hasty J. L., Van Heugten E., See M. T., et al.. Efect of vitanin E on improving fresh pork quality in Berkshire and Hampshire-sired pigs[J]. J. Anim. Sci., 2002, 80: 3230-3237
Hazlewood C., Chang D. C., Bufordl D. C., et al.. Nuclear Magnetic Resonance Transverse Relaxation Times of Water Protons in Mkeletal Muscle[J]. Biophysical Journal, 1974, 14
Hazlrwood C. F., Nichols B. L.. Evidence for the Existence of a Minimum of Two Phases so Ordered Water in Skeletal Muscle[J]. Nature, 1969, 222,24
Hedegaard J., Horn P., Lametsch R., et al.. UDP-Glucose pyrophosphorylase is upregulated in carriers of the porcine RN-mutation in the AMP-activated protein kinase[J]. Proteomics., 2004, 42: 448-2454
Herbert B. R., Molloy M. P., Gooley A. A.. Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent[J]. Electrophoresis, 1998, 19 (5) : 845-851
Hollung K., Veiseth E., Jia X. H., el al.. Application of proteomics to understand the molecular mechanisms behind meat quality[J]. Meat Science, 2007, (77) : 97-104
Holm L., Hoff A., Erichsen L., et al.. Social and cultural acceptability of fat reduced diets among Danish overweight subjects: High-protein versus hing-carbohydrate diets[J]. Food Quality and Perference, 2008, 19:43-50
Huff-Lonergan E., Parrish F. C.. Effects of postmortem aging time,animal age and sex on degradation of titin and nebulin in bovine longissimus muscle[J]. J. Anim. Sci., 1995,73: 1064-1073
Huff-Lonergan E., lonergan S. M.. Postmortem mechanisms of meat tenderization: the roles of the structural proteins and the calpain system[J]. In:Y. L. Xiong, C. T. Ho and F shahidi, Editors, Quality attributes of muscle foods, Kluwer Academic/Plenum Publishers, New York, 1999
Huff-Lonergan E., Huff-Lonergan S.. Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes[J]. Meat Science, 2005,71: 194-204
Hullberg A., Bertram H. C.. Relationships between sensory perception and water distribution determined by low-field NMR T_2 relaxation in processed pork-impact of tumbling and RN-allele[J]. Meat Science, 2005, 69: 709-720
Hultman E., Soderlund K., et al.. Muscle creatine loading in men[J]. J. Appl. Physiol., 1996, 81: 232-237
Hwang I. H., Park B. Y., Kim J. H., et al.. Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus[J]. Meat Science, 2005, 69: 79-91
Hwang I. H., Devine C. E., Hopkins D. L.. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness[J]. Meat Science, 2003, 65 (2) : 677-691
Isfort R. J.. Proteomic analysis of striated muscle[J]. Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, 2002, 1 ( 771) : 155-165
Isfort R. J., Wang F., Greis K. D., et al.. Proteomic analysis of rat soleusmuscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy[ J ]. Proteomics., 2002, 2 (5) : 543-550
Isfort R. J., Wang F., Greis K. D., et al.. Proteomic analysis of rat soleus and tibialis anterior muscle following immobilization[J]. J. Chromatogr B Analyt. Technol. Biomed Life Sci., 2002, 2 (769) :323-332
Jensen C., Guidera J., Skovgaard, et al.. Effects of dietary alpha-tocopheryl acetate supplementation on alpha-tocopherol deposition in porcine m. psoas major and m. longissimus dorsi and on drip loss, colour stability and oxidative stability of pork meat[J]. Meat science, 1997,45:491-500
Joo S. T., Kauffman R. G., Kim B. C., et al.. The relationship of sarcoplasmic and myofibrillar protein solubility to color and water-holding capacity in porcine longissimus muscle[J]. Meat Science, 1999, 52: 291-297
Juhn M. S., Tarnopolsky M.. Oral creatine supplementation and athletic performance: A crtical review[J]. Clin. J. Sport Med., 1998, 8: 286-297
Juncher D., Ronn B., Mortensen E. T. et al.. Effect of pre-slaughter physiological conditions on the oxidative stability of colour and lipid during chill storage of pork[J]. Meat Science,2001,58:347-357.
Kanski J., Alterman M. A., Schoneich C.. Proteomic identification of age-dependent protein nitration in rat skeletal muscle[J]. Free Radical Biology and Medicine, 2003, 10 (35) : 1229-1239
Kauffman R. D., Greaser R.G. Muscle protein changes post mortem in relation to pork quality traits[J]. Meat Science, 1997,45: 339-352
Kent M. R, Spencer M. J., Koohmaraie M.. Postmortem proteolysis is reduced in transgenic mice over expressing calpastatin[J]. Journal of Animal Science, 2004,2(3): 794-801
Koohmaraie M., Shackelford S. D., Wheeler T. L., et al.. A muscle hypertrophy condition in lamb (callipyge) : characterization of effects on muscle growth and meat quality traits[J]. Journal of Animal Science, 1995, 73 (12) : 3596-3607
Kreider, et al., Effects of creatine supplementation on body composition, strength, and sprint performance[J]. Med. Sci. Sports Exerc., 1998, 30: 73-82
Kristensen L., Purslow P. P.. The effect of ageing on the water-holding capacity of pork : role of cytoskeletal proteins[J]. Meat Science, 2001, 58: 17-23
Lametsch R., Bendixen E.. Proteome analysis applied to meat science: characterizing postmortem changes in porcine muscle[J]. Journal of Agricultural and Food Chemistry, 2001, 49 (10) : 4531-4537
Lametsch R., Karlsson A., Rosenvold K.. Postmortem proteome changes of porcine muscle related to tenderness[J]. Journal of agricultural and food chemistry, 2003, 51: 6992-6997
Lametsch R., Kristensen L., Larsen M. R., et al.. Changes in the muscle proteome after compensatory growth in pigs[J]. Journal of Animal Science, 2006, 4 (84) : 918-924
Lametsch R., Roepstorff P., Bendixen E.. Identification of protein degradation during postmortem storage of pig meat[J]. Journal of Agricultural and Food Chemistry, 2002, 50 (20) : 5508-5512
Lametsch R., Roepstorff P., Moller H. S., et al.. Identification of myofibrillar substrates for I-calpain[J], Meat Science, 2004. 68 (4) : 515-521
Laurent W., Bonny J. M., Renou J. P.. Muscle characterization by NMR imaging and spectroscopic techniques[J]. Food Chemistry, 2000, 69:419-426
Lauridsen C., Nielsen J. H., Henckel P., et al.. Antioxidative and Oxidative status in muscles of pigs fed rapeseed oil, vitamin E, and copper[J]. Journal of Animal Science, 1999,77: 105-115
Laville E., Sayd T., Morzel M., et al.. Characterisation of PSE zones in semimembranosus pig muscle[J]. Meat Science, 2005, 1 (70) : 167-172
Lawson M. A.. The role of integrin degradation on postmortem drip loss in pork[J]. Meat Science, 2004, 68: 559-566
Leheaks J. M., Wulf D. M., Maddock R. J.. Effect of fasting and transportation on pork quality development and extent of postmortem metabolism [J]. Meat Science, 1996, 74: 934-943
Leheska J. M., Wulf D. M., Clapper J. A., et al.. Effects of high-protein/low-carbohydrate swine diets during the final finishing phase on pork muscle quality[J]. Journal of Animal Science, 2002,80: 137-142
Luccia A. D., Picariello G., Gacace G., et al.. Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams[J]. Meat Science, 2005, 3 (69) : 479-491
Lundstrom K., Andersson Aand, Hansson I.. Effect of the RN gene on technological and sensory meat quality in crossbred pigs with Hampshire as Terminal sire[J]. Meat Science, 1996, 42: 145-153
Maddock R J., Bidner B. S.,et al.. Supplementation with creatine monohydrate improved the lean quality of fresh pork of two different genotypes[J]. In:Proc, 53~(rd) Ammual Recip. Meat Conf. p118
Maddock R. J., Bidner B. S., Carr S. N., et al.. Creatine monohydrate supplementation and the quality of fresh pork in normal and halothane Carrier pigs[J]. J. Anim. Sci., 2002, 80: 997-1004
Mcdonough J., Marban E.. Optimization of IPG strip equilibration for the basic membrane protein mABCI[J]. Proteomics., 2005, 5 (11) : 2892-2895
Miller E. R., Baltzer B. V., et al.. Creatine in the diet of the baby pig[J]. J. Anim. Sci., 1962, 21: 458-490
Miller I., Crawford J., Gianazza E.. Protein stains for proteomic applications: Which, when, why?[J], Proteomics., 2006, 6: 5385-5408
Mlody J. L., Lonergan S. M., Rowe L. J., et al.. Earlly postmoetem biochemical facts influence tenderness and water holding capacity of three porcine muscles[J]. Journal of Animal Science, 2004,82: 1195-1205
Molette C., Remignon H. and Babile R.. Early post-mortem pH and turkey breast meat quality. Proceeding of the XVI European Symposium on the Quality of Poultry Meat[J]. Saint-Brieuc (France) ,2003,23-23,48-53
Molette C., Remignon H. and Babile R.. Modifications of glycolyzing enzymes induce a lowest meat quality in turkey[J]. Poultry Science, 2005, 84:119-127
Monahan F. J.,Gray J. I., Asghar A., et al.. Influence of diet on lipid oxidation and membrane structure in porcine muscle microsomes[J]. J. Agric. Food Chem., 1994,42: 59-63
Monin G., Laborde D.. Water holding capacity of pig muscle protein: Interaction between the myofibrillar protein and sarcoplasmic compounds[J]. Science Aliments, 1985, (5) : 341-345
Mortensen M., Andersen H. J., Engelsen S. B., Bertram H. C., et al.. Effect of freezing temperature, thawing and cooking rate on water distribution in two pork qualities[J]. Meat science, 2006, 72: 34-42
Morzel M., Chambon C., Hamelin M., et al.. Proteome changes during pork meat ageing following use of different pre-slaughter handling procedures [J]. Meat Science, 2004, 67: 689-696
Mullen A. M., Stapleton P. C., Corcoran D., et al.. Understanding meat quality through the application of genomic and proteomic approaches[J]. Meat Science, 2006, (74) : 3-16
Napolitano F., Caporale G., Carlucci A., et al.. Effect of information about animal welfare on consumer willingness to pay for yogurt[J].Food quality and preference,2008,91:910-917.
Offer G., Knight P.. The structural basis of water-holding in meat. Part Ⅱ :Drip Losses [J]. Developments in meat science, 1988: 173-241
Offer G., and Knight P.. The structural basis of water-holding capacity in meat. Part2: drip losses InLR. Lawrie, Editor, Developments in meat science Vol.4, Elsevier science Publications, London
Offer G., Kinght P., Jeacocke R., Almond, et al.. The structural basis of the water-holding,appearance and toughness of meat and Meat-Products[J]. Food Microstrucrure, 1989,8: 151-170
Offer G.. Modeling of the formation of pale, soft and exudative meat- Wffects of chilling regime and rate and extent of glycolysis[J]. Meat Science, 1991,30: 157-184
Op'tEijnde B., Richter E. A., et al.. Effect of creatine supplementation on creatine and glycogen content in rat skeletal muscle[J]. Acta. Physiologica. Scandinavica, 2001, 171: 69-76
Park B. Y., Kim N. K., Hwang I. H., et al.. Effect of fiber type on postmortem proteolysis in longissimus muscle of Landrace and Korean native black pigs[J]. Meat Science, 2007,4 (77) : 482-491
Pasquali C., Fialka I., Huber L. A.. Preparative two-dimensional gel electrophoresis of membrane proteins[J]. Electrophoresis, 1997,18 (14) : 2573-2581
Pitombo R. N., Lima G. A.. Nuclear magnetic resonance and water activity in measuring the water mobility in Pintado (Pseudoplatystoma corruscans) fish[J]. Journal of Food Engineering, 2003, 58: 59-66
Quinn, et al., Effects of modified tall oil and creatine monohydrate on growth performance, carcass characteristics, and meat quality of growing-finishing pigs[J]. Anim. Sci., 2000,78 (3) :2376-2382.
Rabilloud T.. Solubilization of proteins for electrophoretic analyses[J]. Electrophoresis, 1996, 17 (5) : 813-829
Rabilloud T., Adessi C., Giraudel A.. Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients[J]. Electrophoresis, 1997, 18 (324) : 307-316
Remignon H., Molette C., Babiler R., et al.. Current advances in proteomic analysis and its use for the resolution of poultry meat quality problems[J]. World's Poultry Science Journal, 2006, 62: 123-130
Renou J. P., Foucat L., Bonny J. M.. Magnetic resonance imaging studier of water interactions in meat[J]. Food Chemistry, 2003, 82: 35-39
Requejo R., Tena M.. Proteome analysis of maize roots reveals that oxidative stress is a main contributing factor to plant arsenic toxicity[J]. Phytochemistry, 2005, 66: 1519-1528
Rongrong L. I., Kerr W. L., Toledo R. T., et al.. ~1H NMR Studies of Water in Chicken Breast Marinated with Different Phosphates[J]. Food Chemistry and Toxicology, 2000, 65 (4) : 575
Rosenvold K., Andersen H. J.. Factors of significance, for pork quality—a review[J]. Meat Science, 2003,64:219-237
Rosenvold K., Essen J. S. P., Lerke H. N., et al.. Muscle glycogen stores and meat quality as effected by strategic finishing feeding of slaughter pigs[J]. Journal of Animal Science, 2001b, 79: 382-391
Rosenvold K., Lsrke H. N., Jensen, et al.. Manipulation of critical quality indicators and attributes in pork through vitamin E supplementation level, muscle glycogen reducing finishing feeding and pre-slaughter stress[J], Meat science, 2002, 62: 485-496
Rosenvold K., Lsrke H. N., Jensen, et al.. Strategic finishing feeding as a tool in the control of pork quality[J]. Meat Science, 2001a, 59: 397-406
Rothschild M. F.. Porcine genomics delivers new tools and results: this little piggy did more than just go to market[J]. Genetic Research, 2004,1 (83) : 1-6
Rowe L. J., Maddock K. R., Lonergan S. M., et al.. Influence of early postmortem protein oxidation on beef quality[J]. Journal of Animal Science, 2004a, 82: 785-793
Ruiz-Cabrera M. A., Goub P., Foucat L., et al.. Water transfer analysis in pork meat supported by NMR imaging[J]. Meat science, 2004, 67: 169-187
Savage A. W. J., Warriss P. D., Jolley P. D.. The amount and composition of the proteins in drip from stored pig meat[J]. Meat Science, 1990, 27: 289-303
Savenije B., Geesink G. H., Vander J. G., et al.. Prediction of pork quality using visible/near-infrared reflectance spectroscopy[J]. Meat Science, 2006, 73: 181-184
Schafer A., Rosenvold K., Purslow P. P., et al.. Physiological and structural events postmortem of importance for drip loss in pork[J]. Meat Science, 2003, 61: 355-366
Shaarani S. M., Nott K. P., Hall L. D.. Combination of NMR and MRI quantitation of moisture and structure changes for convection cooking of fresh chicken meat[J].Meat Science, 2006, 72:398-403.
Sorland G. H., Larsena P. M., Lundby F., et al.. Determination of total fat and moisture content in meat using low field NMR[J]. Meat Science, 2004, 66: 543-550
Stahl C. A., Allee G. L.. Creatine monohydrate supplemented in swine finishing diets and fresh pork quality, ii .Commercial applications[J]. J. Anim. Sci., 2001, 79: 3081-3086
Stahl C. A., Allee G. L., Berg E. P.. Creatine monohydrate supplemented in swine finishing diets and fresh pork quality. Commercial applications[J]. J. Anim. Sci., 2001, 79: 3081-3086
Shaarani,S.M.,Nott,K.P.,Hall,L.D..Combination of moisture and structure changes for convection cooking of fresh chicken meat[J]. Meat science, 2006, 72: 398-403
Taylor R. G., Geesink G. H., Thompson V. R, et al.. Is Z-disk degradation responsible for postmortem tenderization[J]. Journal of Animal Science, 1995, 73 (5) : 1351-1367
Tian S. Y., Deng S. P., Chen Z. X.. Multifrequency large amplitude pulse voltammetry: A novel electrochemical method for electronic tongue[J]. Sensors and ActuatorsB, 2007a, 123: 1049-1056
Toko K... Electronic tongue[J]. Biosensors and Bioelectronics, 1998, 3: 701-709
Toko K.. Taste sensor[J]. Sensors and ActuatorsB, 2000, 64: 205-215
Van Laack R... The effect of magnesium supplementation on pork quality[J]. J. Anim. Sci., 2000, 78: 154
Vestergaard M., Madsen N. T., Bligaard H. B., et al.. Consequences of two or four months of whishing feeding of culled dry dairy cows on carcass characteristics and technological and sensory meat quality [J]. Meat Science, 2007 (76) : 635-643
Vitorino R., Ferreira R., Neuparth M., et al.. Sofia Guedes Subcellular proteomics of mice gastrocnemius and soleus muscles[J]. Analytical Biochemistry, 2007, 2 (366) : 156-169
Warner R. D., Kauffman R. G., Greaser M. L.. Muscle protein changes post mortem in relation to pork quality traits[J]. Meat Science, 1997, 3 (45) : 339-352
Warner R. D., Kauffman R. G., Greaser M. L.. Muscleprotein changes postmortem in relation to pork quality traits[J]. Meat Science, 1997,45: 339-352
Warriss P. D., Bevis E. A., Ekins P. J.. The relationships between glycogen stores and muscle ultimate pH in commercially slaughtered pigs[J]. Br. Vet. J., 1989, 145: 378-383
Warriss P. D., Brown S. N., Adams S. J. M.. Relationships between subjective and objective assessments of stress at slaughter and meat quality in pigs[J]. Meat Sci., 1994, 38: 329-340
Warriss P. D., Brown S. N., Nute G. R., et al.. Potential interacitions between the effects of preslaugter stress and post-mortem electrical stimulation of the carcasses on meat quality in pig[J]. Meat Science, 1995,41: 55-68
Winquist F., Wide P., Lundstrom 1., et al.. An electronic tongue based on voltammetry[J]. Analytica Chimica. Acta., 1997, 357: 21-31
Winquist F., Lundstrom I., Wide P.. The combination of an electronic tongue and an electronic nose[J]. Sensors and Actuators B, 1999, 58: 512-517
Winquist R, Holmin S., Krantz-Rulcker C., et al.. A hybrid electronic tongue[J]. Analytica Chimica. Acta., 2000, 406: 147-157
Winquist F., Rydberg E., Holmin S., et al.. Flow injection analysis applied to a voltammetric electronic tongue[J]. Analytica Chimica. Acta., 2002, 471: 159-172
Winquist R, Soderstrom C, Krantz-Riilcker C.. Recognition of six microbial species with an electronic tongue[J]. Sensors and Actuators B, 2003, 89: 248-255
Winquist F., Bjorklund R., Krantz-Riilcker C., et al.. An electronic tongue in the dairy industry[J]. Sensors and Actuators B, 2005, 111-112: 299-304
Wu S. M., Wang J., Liu B. Y., et al.. Determination of Sodium Ion Addition Sites of Peptides by Nanoelectrospray MS/MS Sequence Docking[J]. Chinese Journal of Analytical Cheemistry, 2006,34 (1) : 1-4
Wu W. W., Wang G. H., Baek S. J., et al.. Comparative Study of Three Proteomic Quantitative Methods, DIGE, cICAT, and iTRAQ, Using 2D Gel or LC-MALDI TOF/TOF[J]. Journal of Proteome Research, 2006,5: 651-658
Juncher D.,Ronn B.,Mortensen E.,et al..Effect of pre-slaugter physilogical conditions on the oxidative stability of colour and lipid during chill storage of pork[J].Meat Science,2001,58:347-357 (11) .
Jiang L., He L., Fountoulakis M.. Comparison of protein precipitation methods for sample preparation prior to proteomic analysis[J]. Journal of Chromatography A, 2004, (1023) : 317-320
Xiong Y. L., Mullins O. E., Stika J. F., et al.. Tenderness and oxidative stability of post-mortem muscles from mature cows of various ages[J]. Meat Science, 2007, (77) : 105-113
Yan J. X., Harry R. A., Wait R., et al.. Separation and identification of rat skeletalmuscle proteins using two-dimensional gel electrophoresis and mass spectrometry[J]. Proteomics., 2001, 1 (3) :1424-1434
Zhou G. H., Zhao G. M.. Biochemical changes during processing of traditional Jinhua ham[J]. Meat Science, 2007 (77) : 114-120
Zolodz M. D., Wood K. V., Regnier F. E., et al.. New Approach for Analysis of the Phosphotyrosine Proteome and Its Application to the Chicken B Cell Line, DT40[J]. Journal of Proteome Research, 2004, 3: 743-750