3种淡水对虾在冻藏过程中蛋白质特性的变化

以目前市场上主要的3种养殖对虾为对象,以肌原纤维蛋白盐溶解度、Ca2+-ATPase活性与蛋白质表面的巯基含量为指标,探讨了不同温度冻藏过程(-10、-20、-30、-40℃)对虾虾肉蛋白质生物化学特性的变化,评价了不同冻藏温度对对虾品质的影响。结果表明,第一,3种蛋白质的冷冻变性指标应用于对虾时出现一定差异。Ca2+-ATPase活性比较灵敏,能较好反映-10～-40℃不同冻藏温度引起的蛋白质变性的程度。肌原纤维蛋白盐溶解度能够反映-20℃以上冻藏过程中蛋白质变性程度的差异,而-20～-40℃的差异难以区分。-10℃冻藏时,肌原纤维蛋白的盐溶解度下降明显,而-20℃冻藏时下降程度较小,-20、-30、-40℃冻藏时肌原纤维蛋白的盐溶解度没有明显区别。-10～-40℃冻藏对于巯基含量变化都不大。第二,冻藏过程中3种对虾蛋白质冷冻变性较轻度,比一般鱼类在冻藏过程中稳定,虾比大部分鱼类更耐冻。第三,冻藏温度越低Ca2+-ATPase活性下降程度越小,-10～-40℃冻藏时其差异性有比较明显区分,表明Ca2+-ATPase活性更适合于虾的质量评价。第四,-20℃冻藏对于虾类是比较经济合理的,实用冻藏温度可取-20℃...     

养殖花鳗鲡鱼皮胶原蛋白的特性分析

为了探究养殖花鳗鲡(Anguilla marmorata)鱼皮胶原蛋白的特性,利用胃蛋白酶结合酸抽提法提取花鳗鲡鱼皮胶原蛋白,SDS-PAGE电泳法展示胶原蛋白的电泳图谱,氨基酸分析仪测定胶原蛋白的氨基酸组成,分析胶原蛋白分子的紫外和红外光谱特征,用浊度实验和流变黏弹性实验探究胶原蛋白分子的体外自组装动力学特性。结果显示,花鳗鲡鱼皮胶原蛋白属于Ⅰ型胶原蛋白,氨基酸组成中甘氨酸、脯氨酸与羟脯氨酸三者的比值为8∶3∶2,胶原蛋白分子的最大紫外吸收峰出现在222.6 nm处,热变性温度28℃,红外光谱图和扫描电镜扫描结果图均表明经胃蛋白酶及酸溶得到的胶原蛋白保持了胶原原有的结构。胶原蛋白分子的体外自组装动力学曲线是含有迟滞期、成长期和稳定期的三阶段曲线。以上结果表明花鳗鲡鱼皮胶原具有接近淡水鱼皮胶原的特征。     

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。     

草鱼鱼鳞胶原蛋白的提取及其部分生物学性能

以草鱼鱼鳞为原料, 分别提取鱼鳞中的酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC), 着重开展了其包括热稳定性、体外酶降解性以及胶原海绵材料特性在内的相关研究, 并与哺乳动物来源的猪皮胶原(PC)相比较。实验结果表明, 制备所得的3种胶原蛋白均为典型的Ⅰ型胶原并具有完整的三螺旋结构; PC的热变性温度(41.6 ℃)明显高于ASC(34.8 ℃)和PSC(35.2 ℃); 3种胶原蛋白的体外酶降解性能受水解酶的种类、胶原蛋白提取方法、胶原蛋白来源、胶原蛋白受热历史以及蛋白的自组装程度影响。胶原蛋白酶、胰蛋白酶和木瓜蛋白酶对淡水鱼胶原均具有不同程度的降解能力, 但胶原蛋白酶的降解能力最强; 相同条件下, 3种胶原蛋白体外酶降解率依次为ASC>PSC>PC; 经热变性处理后胶原蛋白的体外酶降解率明显提高而经体外自组装处理后其体外酶降解率均出现不同程度的降低; 3种胶原样品冻干后得到的胶原海绵材料具有不同的机械性能和组织结构, ASC和PSC海绵是一种多孔但拉伸承受力较弱的海绵材料, 而PC则与之相反。     

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。     

缢蛏在-40℃冻藏过程中的质量变化

测定缢蛏可食用部分的挥发性盐基氮、游离脂肪酸、盐溶性蛋白、巯基及感官评定等指标,研究缢蛏在-40℃冻藏过程中的质量变化。试验结果表明,缢蛏各部位的挥发性盐基氮含量随着贮藏时间的延长而增加,缢蛏整体挥发性盐基氮含量在26周时达到17.7 mg/100 g,超过15 g/100 g的国家卫生标准;游离脂肪酸含量逐渐增加;感官评分逐渐下降,贮藏前5个月仍处于可接受阶段;缢蛏各部位的肌原纤维蛋白的溶出量和巯基含量均呈下降趋势,且在贮藏前14周下降较慢。缢蛏在-40℃冻藏条件下可贮藏5个月。     

南极磷虾冻藏温度下的品质变化及其货架期分析

以出肉率及化学变化(pH、TVB-N、TBARS、Ca² -ATPase活性)为指标,结合感官评价,探讨了南极磷虾冻藏温度下(-8、-18和-28 ℃)的品质变化及货架期。实验结果显示,南极磷虾感官评分与冻藏时间和冻藏温度均有显著的相关性(r=0.982和0.981),-8 ℃条件下20 d后南极磷虾感官不可接受,-18和-28 ℃条件下南极磷虾分别在75和120 d时感官不可接受;出肉率与冻藏时间有显著的相关性(r=0.953),在-8、-18和-28 ℃条件下南极磷虾出肉率在货架期终点分别达到31.62%、31.21%、34.52%;pH与冻藏时间和冻藏温度相关性不明显,不适宜用作反映南极磷虾冻藏条件下的品质指标,但随时间的延长pH仍呈增长趋势,在货架期终点3种冻藏温度下南极磷虾pH分别达到7.94、7.99、7.84;TVB-N和TBARS分别与冻藏时间有显著相关性(r=0.944和0.935),但TVB-N只与-8 ℃条件下的温度有显著相关性,TBARS只与-18和-28 ℃冻藏温度有显著相关性,在货架期终点时(感官不能接受)3种冻藏温度下南极磷虾TVB-N和TBARS分别为21.43、20.49、19.74 mg/100 g和0.88、0.78、0.66 mg MA/kg,均低于腐败水平阈值;Ca² -ATPase活性下降显著,与冻藏时间呈显著相关性(r=-0.929)。南极磷虾感官指标、出肉率、TVB-N、TBARS、Ca² -ATPase活性均在冻藏期间有明显变化,且与冻藏时间有明显的相关性,可以考虑用作反映冻藏条件下南极磷虾品质变化指标。因此,综合各项指标并结合感官评价,可以判断实验过程中3种冻藏温度下南极磷虾货架期终点分别为20、75、120 d。     

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。     

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。     

The effect of fish freshness on myosin denaturation in flounder Paralichthys olivaceus muscle during frozen storage

Fisheries Science - The effect of fish freshness on myosin denaturation during the frozen storage of flounder muscle was studied. The muscle of instantaneously killed flounder was immediately...     

不同加热温度下刺参肌肉组织与胶原纤维结构的变化

为研究鲜活和不同加热温度下刺参体壁组织构造及其胶原纤维结构的变化,采用VanGieson染色法观察组织构造、采用细胞分裂扫描电镜法(cell-maceration/SEM)观察胶原纤维结构,同时利用示差扫描量热仪(DSC)测定刺参肌肉蛋白质的热收缩温度。结果发现,在不同加热温度条件下,刺参体壁组织构造及其胶原纤维结构均发生显著变化。随着加热温度的升高,刺参肌肉组织中纤维逐渐聚集交联,形成多孔网状结构;蛋白质发生热变性、胶原纤维结构收缩,导致纤维排列紧密,纤维间孔隙度呈减小趋势。与刺参整体组织构造的变化相比,胶原纤维结构的变化尤其明显。鲜活刺参体壁肌肉蛋白质的热收缩温度为68.92℃,加热过程中蛋白质的热变性是引起其构造变化的主要原因。     

Preparation of Water-Soluble Chitosan and its Suppressive Effect on the Denaturation of Scallop Adductor Muscle Myofibrillar Protein During Frozen Storage

ABSTRACT

In the present study, investigated were the preparation of water-soluble chitosan (WSC) by hydrolysis of original chitosan with commercial α-amylase and the suppressive effect of WSC on denaturation of bay scallop adductor muscle myofibrillar protein (Mf) during frozen storage at ?18°C for 12 months. The WSC (2.5- to 10-g dry weight) was added to 100 g of the Mf, and the changes in the Ca-ATPase activity, solubility, and sulfhydryl content were examined during frozen storage. The addition of WSC significantly reduced the denaturation of the Mf Ca-ATPase. Moreover, a significant increase in Mf solubility and sulfhydryl content was observed in the WSC-treated bay scallop adductor muscles compared with the control (p < 0.05) during frozen storage at ?18°C.     

Physiochemical and Textural Alterations in Indian Squid (Loligo duvauceli) Mantle During Frozen Storage and Cooking

Textural variations in squid mantle and the role of proteins on texture during frozen storage and cooking were investigated. Myofibrillar protein (62.36%) and pepsin soluble collagen (10.70%) accounted for the major fraction of total protein (22.17%). The histochemistry of mantle tissue showed a mesh-like arrangement of myofibrillar proteins with a collagenous dermal layer and feebly passing collagen through myotome bundles. Texture profile analysis of unfrozen mantle suggested the first phase of hardening at 50°C with hardness 1 (H1) of 11.53 kgf and hardness 2 (H2) of 9.68 kgf; and the second phase of hardening with optimal texture and maximum juiciness at 70°C (H1, 8.11 kgf; H2, 7.13 kgf) that varied with extended frozen storage. Increased frozen storage and cooking led to protein denaturation and formation of new low molecular weight proteins as evidenced in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); these possibly influenced the functional and microstructural properties of the tissue.     

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。     

Comparison of Physical,Thermal and Chemical Methods to Measure Protein Denaturation in Frozen Pacific Whiting (Merluccius productus)

The potential of using the torsion test and differential scanning calorimetry (DSC) to determine the effect of frozen storage on protein denaturation in fish fillets was investigated. Pacific whiting fillets were stored for 12 weeks at three temperature conditions: -20¦C, -8¦C, and at a level varying between 0 and -8¦C. Salt soluble protein (SSP) extractability and Ca++-ATPase activity were used to evaluate the torsion test and DSC. The shear strain value of the torsion test provided a good correlation with SSP extractability, Ca++-ATPase activity, and myosin transition enthalpy as measured by DSC. Therefore, shear strain can be considered as a useful tool for the determination of protein denaturation in Pacific whiting during periods of frozen storage. Because Ca++-ATPase activity, shear stress and shear strain, and myosin transition enthalpy all decreased within one week, protein deterioration in frozen Pacific whiting appears to be rapid at the temperatures tested.     

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.