不同类型电场辅助冰温贮藏对生鲜猪肉保水性的影响

为研究不同类型电场辅助冰温贮藏对生鲜猪肉保水性的影响,以猪背最长肌为研究对象,对比分析在交变电场辅助冰温、静电场辅助冰温及普通冰温（对照组）贮藏条件下生鲜猪肉水分含量、贮藏损失、蒸煮损失、横向弛豫时间T2、肌原纤维蛋白表面疏水性及结构的变化。结果表明：交变电场和静电场处理组生鲜猪肉水分含量和不易流动水弛豫峰面积比例P21显著高于对照组（P＜0.05）,贮藏损失、蒸煮损失、肌原纤维蛋白表面疏水性及自由水弛豫峰面积比例P22显著低于对照组（P＜0.05）,但交变电场处理组和静电场处理组各指标之间无显著差异。综上,输出电压为3 300～4 000 V所产生的交变电场和输出电压为3 800 V所产生的静电场辅助冰温贮藏均可延缓肌原纤维蛋白降解及不易流动水向自由水转化,从而提高生鲜猪肉的保水性,降低贮藏过程中的汁液损失。     

氧化条件下茶多酚对猪肉肌原纤维蛋白理化和凝胶特性的影响

研究茶多酚质量浓度（0、0.02、0.2、1.0?mg/mL）对羟自由基氧化体系中猪肉肌原纤维蛋白侧链结构、凝胶保水性和水分分布状态的影响。结果表明,氧化处理后未加茶多酚的0?mg/mL组与空白对照组相比,游离巯基含量显著减少,表面疏水性和二聚酪氨酸含量显著增加,内源色氨酸荧光强度降低,保水性显著下降,自由水含量显著增加（P＜0.05）。氧化处理后,随着茶多酚质量浓度的增加,蛋白质游离巯基和内源色氨酸荧光强度逐渐增加,表面疏水性呈下降趋势,凝胶保水性呈升高趋势,不易流动水含量显著增加,自由水含量显著降低（P＜0.05）。在氧化体系中添加茶多酚,可以保护肌原纤维蛋白侧链结构,提高凝胶保水性。     

冰温和冷鲜贮藏对鸡肉肌原纤维蛋白凝胶性能和水分状态的影响

以鸡胸肉为原料,研究4℃冷鲜和-0.7℃冰温贮藏期间鸡肉肌原纤维蛋白凝胶强度、保水性和水分分布状态变化。采用动态流变仪测定其凝胶强度,用离心法测定凝胶的保水性,用低场核磁共振分析凝胶的水分状态变化情况。结果表明:随着贮藏时间的延长,冷鲜和冰温组鸡胸肉肌原纤维蛋白凝胶强度和保水性均呈下降趋势,冰温组蛋白凝胶强度和保水性显著高于冷鲜组(P0.05);低场核磁共振分析表明持水性的下降与不易流动水比例降低和自由水比例提高有关;冰温组蛋白凝胶不易流动水下降和自由水的上升幅度显著低于冷鲜组(P0.05)。冰温贮藏可以更好地保持肌原纤维蛋白的热诱导凝胶性能,从而保证鸡肉的加工品质。     

冷冻贮藏过程中氧化诱导牦牛肉肌原纤维蛋白结构的变化

探讨在普通包装和真空包装冻藏条件下的牦牛背最长肌和股二头肌的肌原纤维蛋白氧化变化。结果表明：羰基含量60 d时显著增加（P＜0.05）,除股二头肌普通包装组在90 d保藏时的羰基含量显著升高外,其他处理组都呈下降趋势（P＞0.05）;总巯基含量在冻藏60 d内总体上升（P＜0.05）,60 d之后呈下降趋势;采用真空包装的两个处理组的表面疏水性在冷冻贮藏90 d以后都比普通包装的低;背最长肌的Ca2＋-ATP酶活性比股二头肌的低,而K-ATP酶活性则无显著差异。背最长肌肌原纤维蛋白溶解性在整个实验周期中有显著变化（P＜0.05）,股二头肌肌原纤维蛋白溶解性的变化不显著（P＞0.05）。此外,冷冻贮藏期间的蛋白质条带发生了变化,肌球蛋白重链和肌动蛋白随着冻藏时间的延长都发生了不同程度的降解。该结果说明随着冷冻贮藏时间的延长,肌原纤维蛋白发生了氧化。且随时间延长,蛋白氧化越严重,表面疏水性和溶解性越低,总巯基含量、K-ATP酶活性和Ca-ATP酶活性含量越高。     

EGCG浓度对肌原纤维蛋白侧链结构和凝胶水分分布的影响

以猪肉肌原纤维蛋白为研究对象,在羟自由基氧化体系中添加不同浓度（0、0.1、0.2、0.5、1.0、2.0 mmol/L）表没食子儿茶素没食子酸酯（epigallocatechin gallate,EGCG）,以未加EGCG和氧化剂的肌原纤维蛋白溶液作为空白对照组,研究肌原纤维蛋白侧链结构以及蛋白凝胶水分分布的变化规律。结果表明,EGCG降低了肌原纤维蛋白游离巯基和总巯基含量,0.1 mmol/L～2.0 mmol/L EGCG组显著低于空白对照组（P＜0.05）;肌原纤维蛋白侧链形成的羰基和二聚酪氨酸含量随EGCG浓度的增加而逐渐下降,2.0 mmol/L EGCG组下降最明显。凝胶储能模量（G''）随EGCG浓度的增加而升高。随EGCG浓度的增加,凝胶保水性逐渐升高,凝胶中不易流动水含量增加,自由水含量降低,2.0 mmol/L EGCG组降低效果最显著。相关性分析表明,EGCG浓度与蛋白质侧链羰基含量、游离氨基含量和表面疏水性呈极显著负相关（P＜0.01）,凝胶保水性与游离巯基含量、总巯基含量、羰基含量、表面疏水性呈极显著负相关（P＜0.01）。     

微冻贮藏过程中能量代谢酶活性和蛋白质氧化降解对鲈鱼质构特性的影响

为了研究微冻贮藏过程中鲈鱼质构特性与能量代谢酶和蛋白质氧化之间的关系,分析了3 种不同处理方式（空气包装处理、真空包装处理、茶多酚结合真空包装处理）对微冻（－2 ℃）贮藏过程中鲈鱼的剪切力、组织结构、差式扫描量热曲线、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、巯基含量和3 种能量代谢酶（乳酸脱氢酶、Ca2＋-ATP酶、Mg2＋-ATP酶）活力的影响。结果表明：随微冻贮藏时间的延长,3 种不同处理方式下鲈鱼的剪切力、总巯基含量和能量代谢酶活力均显著下降（P＜0.05）,而茶多酚结合真空包装处理组各指标显著高于其他两个处理组（P＜0.05）,表明茶多酚对微冻贮藏过程中鲈鱼品质有保护作用。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳图谱和差示扫描量热曲线结果表明,在微冻条件下贮藏21 d鲈鱼肌球蛋白发生轻微变性;经过相关性分析得出,3 种能量代谢酶活力均与总巯基含量呈显著正相关（P＜0.01,r＝0.99）,表明ATP酶和乳酸脱氢酶活力与肌原纤维蛋白的降解密切关,总巯基含量和ATP酶活力、剪切力之间也呈现极显著正相关性（P＜0.01,r＝0.92）,表明鲈鱼肌原纤维蛋白氧化会导致质构的劣化。     

不同冻结温度下牛肉的肌原纤维蛋白变性与肌肉持水性

为明确冷冻温度对牛肉肌原纤维蛋白变性和肌肉持水性（water-holding capacity,WHC）的影响、探讨肌 原纤维蛋白变性与WHC的相关性。以牛背最长肌作实验材料,探究－9、－18、－23、－38 ℃下冻结后肌原纤维 蛋白理化特性和牛肉WHC。通过测定巯基含量、蛋白质溶解度、Ca2＋-三磷酸腺苷酶（adenosine triphosphatase, ATPase）活力及蛋白质热稳定性考察牛肉冻结后肌原纤维蛋白变性情况,利用解冻汁液流失与加压失水率指标衡 量牛肉WHC,采用低场核磁共振（low field-nuclear magnetic resonance,LF-NMR）波谱和磁共振成像（magnetic resonance imaging,MRI）技术对比分析了肌肉水分分布情况,并于4 ℃解冻后测定了色差与剪切力。结果表明： －23 ℃与－38 ℃下冻结试样较－9 ℃与－18 ℃肌原纤维蛋白变性程度小：－23 ℃与－38 ℃下冻结试样蛋白质溶解 度、Ca2＋-ATPase活力、巯基含量和总变性焓相比－9 ℃与－18 ℃实验组较高（P＜0.05）。－23 ℃与－38 ℃下冻 结牛肉解冻后L*值、b*值、剪切力、解冻汁液流失和加压失水率显著低于－9 ℃与－18 ℃（P＜0.05）。LF-NMR 及MRI结果相互佐证了肉样在－23 ℃与－38 ℃冻结下肌肉WHC高于－9 ℃与－18 ℃的实验结果。肌原纤维蛋白理 化特性（蛋白质溶解度、Ca2＋-ATPase活力、巯基含量、总变性焓）与WHC（解冻汁液流失率、加压失水率）均呈 极显著相关（P＜0.01）,L*、b*值及剪切力亦与WHC存在极显著相关（P＜0.01）。相关性分析结果验证了牛肉冻结 过程中肌原纤维蛋白变性对肌肉持水性存在显著影响,进而导致牛肉解冻后出现肉色劣变、嫩度下降及汁液流失。     

冰温保鲜对牛肉肌原纤维蛋白结构和功能特性的影响

以冷藏(4℃)的牛肉为对照,通过测定牛肉肌原纤维蛋白的ATP酶活性、巯基含量、溶解性、热稳定性和电泳等指标,研究冰温(-1℃)保鲜对牛肉蛋白结构和功能特性的影响。结果表明:随着贮藏时间的延长,牛肉肌原纤维蛋白的功能性显著降低。SDS-PAGE表明蛋白质发生不同程度的降解。在相同贮藏时间内,冰温保鲜比冷藏条件可减少蛋白质结构和功能性的变化。贮藏至第12天时,4℃冷藏牛肉肌原纤维蛋白的Ca2+-ATPase活性下降了72.9%,而冰温保鲜的牛肉下降46.9%;冷藏牛肉肌原纤维蛋白的总巯基和活性巯基含量分别下降50.12%和93.68%,而冰温保鲜牛肉降至35.08%和71.15%;冷藏牛肉蛋白质溶解度下降41.18%,而冰温保鲜牛肉下降15.52%。SDS-PAGE表明冷藏牛肉的肌原纤维蛋白降解程度比冰温保鲜的大,冷藏条件下的牛肉肌原纤维蛋白热稳定性亦不如冰温保鲜的高。冰温保鲜是一种有效牛肉保鲜方法。     

不同冻融次数下牦牛肉蛋白质氧化与保水性的关系

探讨不同冻融次数下牦牛肉中的蛋白质氧化对其保水性的影响。选取3?岁左右的甘南牦牛背最长肌,经过7?次冻融循环,分别测定样品的pH值、解冻损失率、蒸煮损失率、加压失水率、羰基含量、巯基含量以及蛋白质溶解度。结果表明,随着冻融次数的增加,pH值显著降低（P＜0.05）,解冻损失率、加压失水率和蒸煮损失率反映的保水性也显著降低（P＜0.05）,羰基、巯基含量反映的蛋白质氧化程度显著增加（P＜0.05）,蛋白质溶解度中全蛋白、肌原纤维蛋白以及肌浆蛋白均呈现显著下降（P＜0.05）。pH值、保水性和蛋白质氧化之间相关性显著（P＜0.05）,在7?次冻融过程中,pH值下降速率趋势与保水性下降速率趋势一致,并且后期保水性下降速率减缓的同时蛋白质氧化速率上升。表明多次冻融循环会引起牦牛肉蛋白质氧化程度显著升高,造成保水性显著下降,贮运体系中通过有效地控制蛋白质氧化可以更好地提高牦牛肉品质。     

不同包装方式和贮藏温度对牛肉保水性的影响

以牛背最长肌为原材料,分别经托盘包装(AP)或气调包装(MAP)后贮藏于2℃及-1.5℃条件下,于贮藏第0、5、10、15天测定p H、蒸煮损失、汁液流失率等指标,并利用低场核磁共振技术(LF-NMR)考查水分分布状态及迁移规律,旨在探索不同包装方式及贮藏温度对牛肉保水性的影响。结果表明:随贮藏时间的延长,牛肉保水性下降,表现为蒸煮损失和汁液流失率增加,弛豫时间(T23)延长和不易流动水含量(P22)的减少。皮尔逊相关系数分析结果显示P22、T23与贮藏时间、蒸煮损失及汁液流失显著相关(P0.05或P0.01),表明弛豫时间的延长及不宜流动水的损失是导致保水性下降的直接原因。试验表明包装方式及贮藏温度对牛肉保水性影响显著(P0.05),冰温贮藏及气调包装可较好的维持牛肉保水性。     

Superchilled,chilled and frozen storage of Atlantic mackerel (Scomber scombrus) fillets – changes in texture,drip loss,protein solubility and oxidation

Changes in quality characteristics in relation to protease activity and protein oxidation in chilled, superchilled and frozen mackerel fillets during storage were studied. The solubility of sarcoplasmic proteins was quite stable in mackerel samples for all storage experiments, whereas the solubility of myofibrillar proteins decreased in both superchilled and frozen samples. A significant correlation (r = 0.983, P < 0.05) between the increased activity of cathepsin B+L in chilled fillets and softening of the fish flesh during storage was revealed. Contrary with chilled samples, the texture of superchilled mackerel fillets became tougher along the storage period, which can be explained by a higher rate of myofibrillar oxidation (r = 0.940, P < 0.05). The hardness and drip loss decreased slightly at the end of frozen storage. Superchilling preserved the quality of mackerel fillets with the least side effects in relation to protein solubility, drip loss and softening of the fish tissue as compared to chilled and frozen storage.     

Effects of kojic acid on changes in the microstructure and myofibrillar protein of duck meat during superchilled storage

This study investigated the effect of 0.8% (m/v) kojic acid treatment on changes in the microstructure and myofibrillar protein of duck meat covered with oxygen-permeable polyvinylchloride (PVC) film (9 ± 0.5 µM) during superchilled storage (−1.65 ± 0.5°C). The superchilled samples exhibited wider gaps between muscle fibers at 5 weeks storage compared with kojic acid–treated groups. Based on the variation of water status, the water-holding capacity decreased significantly (p < 0.05), and bound water and immobilized water were gradually converted into free water during superchilled storage. For kojic acid–treated samples, however, no major changes were observed with respect to muscle structure, water status, and protein degradation at 6 weeks. The 0.8% (m/v) kojic acid treatment increased the water-holding capacity, reduced carbonyl content and protein degradation, and decreased the α-helix contents loss of myofibrillar proteins. Kojic acid treatment effectively protected myofibrillar protein structure from being destroyed during superchilled storage, suggesting that this method was a good way to reduce protein oxidation and prolonged its shelf life.     

静电场辅助冻结-解冻对肌肉保水性及蛋白理化特性的影响

以牛背最长肌（Longissmus dorsi）为研究对象,探讨静电场辅助冻结-解冻、自然冻结-解冻（对照组）、 自然冻结-静电场辅助解冻、静电场辅助冻结-自然解冻4 个处理对肌肉保水性及蛋白理化特性的影响,为冷冻肉 品质控制技术开发提供理论依据。采用差示扫描量热、核磁共振质子成像等技术,对比分析了冻结-解冻速率、解 冻汁液流失、蛋白表面疏水性、热稳定性、水分迁移等指标。结果表明：静电场辅助冻结-解冻实验组牛肉冻结、 解冻时间较对照组分别缩短16.290、8.920 h;通过最大冰晶生成带用时较对照组缩短3.41 h;解冻汁液流失率显著 低于对照组（P＜0.05）,为4.19%;冻结蛋白质表面疏水性显著降低,为16.16 μg,解冻后显著升高,为9.45 μg （P＜0.05）;蛋白质变性程度显著低于对照组（P＜0.05）,变性温度分别为55.130、63.940、78.350 ℃。静电场 辅助冻结-解冻可有效提高牛肉冻结-解冻速率,降低肌原纤维蛋白变性程度,减少解冻汁液损失。     

Investigation of the activity of cathepsin B in red shrimp (Solenocera crassicornis) and its relation to the quality of muscle proteins during chilled and frozen storage

Cathepsin B is a cysteine protease that has important effects on the quality of muscle products. In this study, the changes of cathepsin B activity and its relation to muscle proteins were investigated in intact and beheaded shrimp during chilled and frozen storage. The obtained results indicated that the water holding capacity (WHC), shear force, hardness, and myofibrillar protein (MP) content all significantly decreased in both the intact and beheaded shrimp samples with increasing storage period (p < 0.05). Specifically, beheading shrimp exhibited much more stable characteristics than intact shrimp samples during both chilled and frozen storage. The enzyme activity results suggested that cold temperature and storage induced the release of cathepsin B from the lysosomes to the mitochondria, sarcoplasm, and myofibrils in the muscle tissues. Furthermore, SDS-PAGE and transmission electron microscopy (TEM) analysis revealed that beheading the shrimp greatly inhibited the dissociation of shrimp muscle proteins during storage. The current findings suggest that cathepsin B located in the head of shrimp was likely transferred to the muscle through the first abdominal segment during storage, accelerating the dissociation of the muscle proteins. Therefore, beheading the shrimp was conducive to prolonging the shelf-life of stored shrimp products.     

Quality changes during superchilled storage of cod (Gadus morhua) fillets

Superchilling is a method with potential for extending the shelf life of food products by partial freezing. For centuries, Atlantic cod (Gadus morhua) has been the most important commercial species in the North Atlantic fisheries and is now regarded as a very promising species in cold water fish farming. In the present work, superchilled storage at −2.2 °C of fillet portions of farmed cod was investigated. Superchilled cod showed increased shelf life with respect to reduced growth of sulphide producing bacteria compared to ice chilled. Drip loss was lower in superchilled cod. However, liquid loss by low-speed centrifugation was higher in superchilled cod fillets compared to ice chilled. This can be explained by freeze denaturation of muscle proteins, which is supported by the lower extractability of salt soluble proteins. There is a need for process optimization to minimize protein denaturation.     

Quality changes during superchilled storage of pork roast

Quality parameters (sensory, physical, biochemical and microbiological) of superchilled vacuum packed boneless pork roasts were studied during storage for 16 weeks. Superchilling of vacuum packed pork roast at a temperature of −2.0 °C improved shelf life significantly compared to traditional chilled storage at +3.5 °C. Superchilled pork roasts maintained good sensory quality and low microbiological counts during the whole storage period. The drip loss in superchilled samples was lower and showed less variation than in the references and the temperature abused roasts. The consequences of an interrupted cold chain during storage were also investigated. Superchilled samples with temperature abuse resembled chilled samples with respect to drip loss and microbial levels. To take advantage of all the benefits of superchilling and successfully implement the process in the food industry a stable, controlled temperature during storage is critical.     

Effect of Modified Atmosphere Packaging and Superchilled Storage on the Microbial and Sensory Quality of Atlantic Salmon (Salmo salar) Fillets

ABSTRACT: Fresh Atlantic salmon fillets packaged under modified atmosphere (MA) (CO²:N² 60:40) and air was stored at superchilled (-2 °C) and chilled (+4 °C) temperatures. Changes in sensory scores, microbial growth, headspace gas composition, water loss, and pH were monitored during 24 d of storage. The superchilled MA packaged salmon maintained a good quality, with negligible microbial growth (<1000 colony-forming units [CFU]/g) for more than 24 d based on both sensory and microbial analyses (aerobic plate count, H2S-producing, and psychrotrophic bacteria). Superchilled salmon in air had a 21-d sensory shelf life, whereas MA and air-stored fillets at chilled conditions was spoiled after 10 d and 7 d, respectively.