鳙肌肉蛋白质生化特性在冻藏过程中的变化

以肌动球蛋白的盐溶性、肌原纤维蛋白ATPase活性以及肌原纤维蛋白的巯基含量为指标,研究了鳙肌原纤维蛋白在-10℃,-20℃,-30℃和-40℃下冻藏时的变性情况。结果表明,在不同温度下冻藏时,鳙肌动球蛋白的盐溶性、肌原纤维蛋白的ATPase活性以及巯基含量随着冻藏时间的延长,均呈下降趋势。但是,鳙蛋白质的变性速度在不同冻藏温度下的差异是极其显著的(P<0.01)。冻藏温度越低,变性越缓慢。     

日本枪乌贼(Loligo japonica)不同温度冻藏过程中的品质变化

选取-20℃、-30℃和-50℃3个冻藏温度,以TVB-N值、肌原纤维蛋白含量、Ca2+-ATPase活性、巯基含量、TBARS值及肌肉组织微观结构为指标,结合感官评分,对比分析90 d内日本枪乌贼(Loligo japonica)的品质变化规律。结果显示,在不同冻藏温度下,随着时间的延长,Ca2+-ATPase活性和感官评分不断下降;肌原纤维蛋白和巯基含量,则先略微上升而后快速下降;TVB-N值和TBARS值呈不断上升的趋势,且温度越高上升速率越快;肌肉组织微观结构分析表明,枪乌贼肌纤维结构在冻藏过程中逐渐变得松散。相比-20℃,-30℃和-50℃冻藏温度条件下更能长久地保持枪乌贼品质,且品质无显著差异。综合分析认为,冻藏温度低于-30℃时,可较好地保持枪乌贼品质。     

海藻糖对冻藏过程中鳙肌原纤维蛋白冷冻变性的影响

从鳙（Aristicktkys nobilis）肌肉中提取肌原纤维蛋白，在蛋白溶液中加入10％（W／V）蔗糖、山梨醇混合物（质量比1：1）或10％（W／V）海藻糖。蛋白溶液在-18℃下冻藏30d，测定冻藏过程中肌原纤维蛋白盐溶性、Ca^2＋-ATPase活性、活性巯基含量、总巯基含量、表面疏水性变化和冻藏结束时的SDS-PAGE。测定结果表明，蔗糖、山梨醇混合物和海藻糖都抑制了冻藏过程中肌原纤维蛋白盐溶性、Ca^2＋-ATPase活性、巯基含量的降低和表面疏水性的升高，延缓了鳙肌原纤维蛋白的冷冻变性。海藻糖比蔗糖、山梨醇混合物有更好的抗冷冻变性效果。[中国水产科学，2006，13（4）：637—641]     

复合鱼肉肌原纤维蛋白加热过程中理化特性变化的研究

考察了鲢(Hypophthalmichthys molitrix)、小黄鱼(Pseudosciaena polyactis)及其以质量比1∶1复合的肌原纤维蛋白的浊度、Ca2+-ATPase活性和巯基含量在加热过程中的变化规律。结果显示:随着加热温度的升高,三种蛋白溶液的浊度呈S型曲线增加。复合肌原纤维蛋白的增加模式与小黄鱼肌原纤维蛋白的增加模式相似,不同于鲢肌原纤维蛋白的增加模式。鲢肌原纤维蛋白和小黄鱼肌原纤维蛋白的Ca2+-ATPase活性随温度的升高逐渐下降。复合肌原纤维蛋白的Ca2+-ATPase活性在20～35℃略有上升,而后剧烈下降,55℃时活性完全丧失。复合肌原纤维蛋白的总巯基含量随着加热温度的升高呈下降趋势。当温度在30～60℃时下降缓慢,高于65℃时剧烈下降。     

浸渍冻结对调理草鱼冻藏过程中肌原纤维蛋白特性的影响

为了探讨浸渍冻结对草鱼(Ctenopharyngodon idellus)冻藏过程蛋白质变性的影响,对蛋白质溶解性、巯基、Ca~(2+)-ATPase活性、肌原纤维的降解及二级结构进行了研究。结果发现浸渍冻结的肌原纤维蛋白的溶解度、总巯基含量、活性巯基总量和Ca~(2+)-ATPase的活性均比空气冻结的高,冻藏150 d后分别比空气冻结的高17.51%、14.20%、4.86%和28.73%。初步表明浸渍冻结更有利于减缓蛋白质变性。电泳结果表明,冻藏过程中浸渍冻结的肌球蛋白重链的电泳条带颜色比空气冻结的深,原肌球蛋白的电泳条带颜色比空气冻结的浅,说明浸渍冻结可减缓调理草鱼块蛋白质的降解。红外光谱的结果进一步发现浸渍冻结的肌原纤维蛋白的α-螺旋含量的下降程度较空气冻结的小,β-折叠、无规卷曲和β-转角含量的增加程度无空气冻结的明显。结果揭示了浸渍冻结更有利于维持冻藏过程中肌原纤维蛋白的二级结构。总的来说,浸渍冻结更有利于减轻蛋白质变性而引起调理草鱼块品质下降的问题。     

臭氧减菌化处理罗非鱼片冰温贮藏过程中蛋白质生化特性的变化

为研究臭氧减菌化处理罗非鱼片冰温贮藏过程中蛋白质生化特性变化规律,本研究对冰温贮藏过程中经臭氧处理罗非鱼片肌原纤维蛋白盐溶性、Ca2+-ATPase活性、表面疏水性、巯基及羰基含量变化进行了评价。结果显示：在冰温贮藏过程中,臭氧处理组和对照组罗非鱼片蛋白质均发生了不同程度的变性,表现为：随贮藏时间的延长,肌原纤维蛋白盐溶性、Ca2 -ATPase活性及巯基含量均呈下降趋势,而肌动球蛋白表面疏水性和羰基含量则呈上升趋势;冰温贮藏20 d后,臭氧处理组罗非鱼片肌原纤维蛋白盐溶性、Ca2 -ATPase活性和巯基含量分别下降了76.57%、89.76%和66.72%,而对照组则分别下降了69.05%、86.45%和62.29%;另一方面,臭氧处理组罗非鱼片肌动球蛋白表面疏水性和羰基含量分别上升了111.75%和76.46%,对照组则分别上升了104.77%和58.23%。在同一贮藏时间臭氧处理组罗非鱼片肌原纤维蛋白盐溶性、Ca2 -ATPase活性及巯基含量较对照组低,而肌动球蛋白表面疏水性和羰基含量较对照组高。研究表明：臭氧水的氧化性及处理过程中产生的ROS加速了冰温贮藏过程中罗非鱼肌肉蛋白质的变性。     

日本枪乌贼(Loligo japonica)不同温度冻藏过程中的品质变化

选取-20℃、-30℃和-50℃3个冻藏温度,以TVB-N值、肌原纤维蛋白含量、Ca~(2+)-ATPase活性、巯基含量、TBARS值及肌肉组织微观结构为指标,结合感官评分,对比分析90 d内日本枪乌贼(Loligo japonica)的品质变化规律。结果显示,在不同冻藏温度下,随着时间的延长,Ca~(2+)-ATPase活性和感官评分不断下降;肌原纤维蛋白和巯基含量,则先略微上升而后快速下降;TVB-N值和TBARS值呈不断上升的趋势,且温度越高上升速率越快;肌肉组织微观结构分析表明,枪乌贼肌纤维结构在冻藏过程中逐渐变得松散。相比-20℃,-30℃和-50℃冻藏温度条件下更能长久地保持枪乌贼品质,且品质无显著差异。综合分析认为,冻藏温度低于-30℃时,可较好地保持枪乌贼品质。     

低温速冻处理对美国红鱼-20℃冻藏生化特性的影响

以盐溶性蛋白质含量、巯基含量、ATPase活性、pH值、感观评定等为指标,研究美国红鱼在-20℃冻藏中肌肉蛋白质生化特性的变化情况。结果表明,无论是-20℃直接冻结还是-80℃低温速冻,在冻藏过程中随着时间的延长,美国红鱼的肌动球蛋白盐溶性、巯基含量以及ATPase活性均呈下降趋势;除冻藏后期外,低温速冻处理能降低美国红鱼蛋白质冷冻变性的程度。     

鲫肌原纤维蛋白加热过程中理化特性变化规律和控制技术的研究

通过对鲫肌原纤维蛋白加热过程中浊度、粘度、Ca²⁺-ATPase活性以及总巯基含量的测定,结合SDS一聚丙烯酰胺凝胶电泳分析了鲫肌原纤维蛋白在加热过程中理化特性的变化。结果表明:鲫肌原纤维蛋白在加热过程中浊度随着溶液温度的升高而上升,在36 ℃、42 ℃和48 ℃条件下变化显著;粘度在20~47 ℃期间下降,在35 ℃和47 ℃出现显著的变化。Ca²⁺-ATPase活性28~40 ℃间显著下降,并且在36 ℃条件下变化显著。总巯基含量结合SDSPAGE电泳显示,当溶液温度在40 ℃以上时,蛋白质分子间通过二硫键产生了肌球蛋白重链聚合物以及其它大分子物质。     

冻结和冻藏对中华绒螯蟹蟹肉品质的影响

为了研究冻结和冻藏对中华绒螯蟹蟹肉品质的影响,本研究对冻结和冻藏中华绒螯蟹的蛋白质特性、游离氨基酸、核苷酸关联成分、Ca2+-ATPase活性以及解冻汁液流失率进行了全面的评价。中华绒螯蟹较耐冻结但不耐冻藏,冻藏2周后蟹肉弹性程度开始下降。中华绒螯蟹在冻藏过程中,蟹肉中游离氨基酸、呈味核苷酸、Ca2+-ATPase活性以及解冻汁液流失率都发生明显变化。冻藏12周后相对于新鲜蟹,游离氨基酸、呈味核苷酸、Ca2+-ATPase活性以及解冻汁液流失率分别下降了25.3%、100%、41.6%和增加了9.2%。普通冻藏(-20℃)条件下,中华绒螯蟹蟹肉发生快速蛋白质分解和ATP降解,表现为游离氨基酸成分与ATP关联物成分都发生很大变化,蛋白质变性显著、汁液流失现象严重等。推测中华绒螯蟹蟹肉不耐冻藏可能与其自身的自溶酶和ATP酶类有关。     

凡纳滨对虾虾仁在冻藏过程中品质变化研究

以凡纳滨对虾（Penaeus vannamei）为研究对象,经过去头和去壳处理后,于-35℃冷冻过夜,然后置于-18℃条件下进行保藏试验。通过测定解冻损失率和肉色变化,明确冻藏期间虾肉的质量变化规律,结合腺苷三磷酸（ATP）及其降解产物、总挥发性盐基氮（TVB-N）和酸碱度（pH）等鲜度指标的测定结果,分析对虾在冻藏条件下鲜度的变化规律,旨在为其生产加工提供理论依据。研究结果表明,冷冻保藏至第18天时解冻损失率达到最大,同时表面色差（L^＊）也达到最大值41.56。而虾肌肉中的ATP质量摩尔浓度冻藏第1天就降低了71.78%,次黄嘌呤（Hx）和次黄嘌呤核苷（HxR）则一直维持在较低水平。第10天鲜度指标（K值）达到最大值7.18%,并能比较稳定地保持这一水平,结合TVB-N测定结果,发现冻藏至第30天时,虾肌肉中的TVB-N仍未超过腐败临界值。因此,冻藏处理可以保持凡纳滨对虾的鲜度,使各项理化指标维持在较低水平,但会加重解冻损失现象。     

Astaxanthin profiles and corresponding colour properties in Australian farmed black tiger prawn (Penaeus monodon) during frozen storage

The colour of commercial cooked black tiger prawns (Penaeus monodon) is a key quality requirement to ensure product is not rejected in wholesale markets. The colour, due to the carotenoid astaxanthin, can be impacted by frozen storage, but changes in colour or astaxanthin profile, during frozen storage, have not been studied in detail. Subsequently in this study, the aims were to define the astaxanthin (as cis, trans, mono‐ester and di‐ester forms) content, together with the colour properties, in both pleopods (legs) and abdominal segments. Changes in astaxanthin content and colour properties were further determined during frozen storage (?20°C). Total astaxanthin content was seen to decrease in all samples over time, with the rate of degradation being significantly greater (P < 0.05) in pleopods than abdomen. In both pleopods and abdomen, rate of degradation of esterified forms was significantly greater (P < 0.05) than non‐esterified forms. Hue angle (increase), a* value (decrease) and L value (increase) were all seen to significantly change (P < 0.05) during storage, with changes being more prevalent in the pleopods. The pleopods are the key indicator of astaxanthin and colour loss in cooked black tiger prawns and preservation strategies are required to preserve astaxanthin and colour during frozen storage.     

冷冻贮藏对凡纳滨对虾肌肉质构特性的影响

采用质构仪TPA模式对冷冻贮藏条件下凡纳滨对虾（Litopenaeus vannamei）肌肉的硬度、黏附性、弹性、咀嚼性、胶黏性和凝聚性等进行了测试。结果显示，在-18℃和-50℃的贮藏条件下，随着贮藏期的延长，凡纳滨对虾肌肉的硬度、咀嚼性、胶黏性和凝聚性均呈现缓慢下降的趋势，弹性的变化不明显，而黏附性则有所上升。这表明冷冻贮藏凡纳滨对虾虽然能保证其较长的货架期，但其口感特征总体上持续下降，而温度越低越有利于保持其肌肉的质构特性。     

Effects of Bicarbonate,Xanthan Gum,and Preparation Methods on Biochemical,Physicochemical, and Gel Properties of Nile Tilapia (Oreochomis niloticus Linn) Mince

This study was aimed to determine the effects of phosphate compound substitutions (sodium bicarbonate and xanthan gum) and preparation methods—headed, gutted whole fish, and mince; fresh and after frozen storage (?20°C for 3 months)—on Nile tilapia mince qualities. Results showed that bicarbonate (0.3% with 8% sucrose/sorbitol) is an efficient phosphate compound replacement as evidenced by the comparative values of salt extractable protein, Ca²⁺-ATPase activity, total sulfhydryl content, and textural properties to those of the phosphate-added—0.3% sodium tripolyphosphate (STPP) with 8% sucrose-sorbitol—sample after 3-month frozen storage (p > 0.05). Both cryoprotected samples containing STPP or bicarbonate exhibited higher denaturation temperatures of myosin than others. Xanthan gum (0.5%) could neither stabilize the biochemical and physicochemical properties of mince during 3-month frozen storage nor improve textural properties of gel from frozen whole fish.     

Postmortem Changes in the Adductor Muscle of Scallop (Chlamys tehuelchus) in Chilled and Frozen Storage

Abstract

The effects of freezing and frozen storage on the biochemical properties of scallop adductor muscles stored at 2-4EC were investigated. Glycogen content fell 40% in the first 12 hr of chilled storage and decreased slowly thereafter. ATP content increased for a short time after death and then decreased slowly. Glycogen and ATP degradation was accompanied by a decrease in both pH and 260/250 absorbance ratio of scallop muscle extracts. A significant increase (p < 0.05) in the hypoxanthine (Hx) content was also observed in chilled stored adductor muscles. Adductor muscles showed a significant decrease (p < 0.05) in the 260/250 absorbance ratio of extracts and an increase in the Hx level after freezing. An increase in Hx content was observed during frozen storage of adductor muscles frozen immediately after processing. Expressible juice increased with freezing and frozen storage of the muscles. The results shown in this paper indicate a rapid loss of quality in scallop adductor muscles during storage at 2-4. Freezing and frozen storage enhanced the quality deterioration of the muscles.     

Antioxidant Properties of Chitosan Coatings on Frozen Atlantic Salmon Fillet Portions

Atlantic salmon contain omega-3 fatty acids, which play important roles in promoting human health but are highly susceptible to oxidation. Chitosan has been shown to have antioxidant properties which could be beneficial in extending the shelf life of Atlantic salmon; however, the effects of chitosan molecular size on oxidation of salmon fillets have not been reported. The primary objective of this study was to evaluate the effects of chitosan coatings on lipid oxidation of Atlantic salmon fillet portions during 5 months frozen storage. The effects of chitosan molecular weight (high molecular weight, low molecular weight, and enzymatically degraded chitosan), concentration (0.5 and 1.0%), and the addition of 1% ascorbic acid to the chitosan coating were evaluated. Chitosan molecular weight significantly affected oxidation as evaluated by propanal levels and changes in L* values of the fillet portions. The chitosan treatment with added ascorbic acid resulted in the lowest propanal levels during 5 months of frozen storage. Manipulation of chitosan molecular weight and incorporation of natural antioxidants into chitosan coatings can provide an effective method of reducing lipid oxidation during extended frozen storage of seafood products.     

无磷品质改良剂对阿根廷鱿鱼冷冻变性的影响

通过考察阿根廷鱿鱼（Sepiaiuex argentinus）在冻藏过程的浸泡增重率、自由液滴损失率、蒸煮损失率、盐溶性蛋白、肌原纤维蛋白钙ATP酶（Ca^2＋-ATP酶）活性、pH、总挥发性盐基氮（TVB—N）以及色泽的变化,试验分别比较了蒸馏水、常用的含磷保水剂及无磷品质改良剂对阿根廷鱿鱼冷冻质量的影响。结果表明,鱿鱼经无磷品质改良剂或含磷保水剂处理后,在冻藏过程中较用蒸馏水处理的具有更好的保水性,浸泡增重率达到26％～35％,但无磷品质改良剂较含磷保水剂能更好地减少鱿鱼自由液滴损失率和蒸煮损失率,且盐溶性蛋白减少率和Ca^2＋-ATP酶活性损失率分别比含磷保水剂组少6％和5％,TVB—N变化缓慢且小于0．30mg·g^-1,而对鱿鱼pH和色差值影响不大。因此,无磷品质改良剂能有效防止冻藏鱿鱼冷冻变性,且效果优于含磷保水剂,值得在鱿鱼冷冻加工中推广应用。     

Effects of Freezing and Frozen Storage on Protein Functionality and Texture of Some Cephalopod Muscles

The aim of this study was to investigate the effects of freezing and frozen storage on protein functionality and texture of squid (Loligo vulgaris), octopus (Octopus vulgaris), and cuttlefish (Sepia officinalis) muscles. Squid, octopus, and cuttlefish samples were cut into pieces of 4 × 4 cm. These pieces were packed in polyethylene bags. The bags were frozen in a blast freezer at ?45°C until the thermal center reached ?18°C. Frozen samples were stored in a deep freezer at ?18°C for 30 days. After freezing and during frozen storage, total soluble protein and water holding capacity decreased and total free amino acid and cooking loss increased in all cephalopod muscles. According to instrumental texture analysis results, freezing and frozen storage affected textural characteristics of squid and cuttlefish but not of octopus. Sensory hardness and chewiness values of all cephalopods increased after freezing, but elasticity values did not change. There were no significant differences between storage days in hardness values of squid and octopus. However, significant differences in hardness values of cuttlefish were observed between the 1st day of storage and the last day.     

Myosin and actin denaturation in frozen stored kuruma prawn Marsupenaeus japonicus myofibrils

Myosin and actin denaturation in kuruma prawn myofibrils stored frozen (0.1 M NaCl, pH 7.5) at ?20 °C was investigated. The inactivation profile of Ca²⁺-ATPase in the myofibrils was identical to that for myosin, indicating that myosin in myofibrils was not protected by actin. The presence of myosin detached from actin in the soluble fraction was proven by ammonium sulfate fractionation in the absence and presence of Mg-ATP. Actin denaturation in myofibrils was further confirmed by its increased susceptibility to chymotryptic degradation. In the frozen myofibrils, actin denatured more rapidly quicker than myosin: actin had completely denatured by storage day 1, followed by a gradual denaturation of myosin. Both myosin and actin in the frozen stored myofibrils retained their high salt-solubility, which decreased slowly during the frozen storage period. The presence of aggregated inactivated myosin in the salt-soluble fraction was proven by precipitation at 40 % saturation of ammonium sulfate in the presence of Mg-ATP, leaving active monomeric myosin in the soluble fraction. Almost no actin denaturation was observed with heated myofibrils.