冷熏对高白鲑理化性质及肌球蛋白构象的影响

以新疆塞里木湖高白鲑为研究对象,研究冷烟熏过程对鱼肉理化性质及肌球蛋白构象的影响。冷熏温度为(20±2)℃,发烟温度140℃,冷熏时间分别为0、6、12、18、24 h,研究冷熏鱼肉理化性质(含水率、水分活度、色泽、质构特性、TVB-N)及肌球蛋白构象(蛋白浓度、总巯基含量、Ca^2+-ATPase、表面疏水性)变化。研究结果表明,冷熏0~24h,鱼肉含水率由75.75%下降至53.03%,水分活度(Aw)由0.988下降至0.952;鱼肉亮度值(L^*)显著降低(P<0.05),红度值(a^*)缓慢增加,黄度值(b^*)显著增加(P<0.05);表征鱼肉质构特性的剪切力与韧性均呈明显上升趋势(P<0.05);鱼肉挥发性盐基氮(TVB-N)由9.81上升至14.23 mg/100g;肌球蛋白浓度、总巯基含量、Ca^2+-ATPase活性均显著降低(P<0.05),表面疏水性增加(P<0.05);综上,控制冷熏时间12~18 h有利于提高冷熏鱼肉品质,降低鱼肉肌球蛋白变性与氧化程度。该研究为特色淡水鱼冷熏制品开发与烟熏过程中蛋白氧化调控提供理论依据与技术参考。     

琥珀酰化修饰改善牦牛乳酪蛋白胶束结构及疏水性

琥珀酰化是改善食品蛋白质功能性质的常用手段,牦牛乳是青藏高原特色乳资源.为了揭示琥珀酰化对牦牛乳酪蛋白胶束结构的修饰作用,以牦牛乳酪蛋白为原料,研究了琥珀酰化修饰对其结构及疏水性的影响.分别通过傅里叶变换红外光谱分析了修饰前后酪蛋白胶束二级结构变化,采用动态光散射技术分析了修饰前后酪蛋白胶束粒径变化,采用扫描电镜技术观察了酰化反应对酪蛋白的表面形貌的影响.结果显示,牦牛乳酪蛋白胶束二级结构为33.1%β-转角、23.2%无规卷曲,32.0%β-折叠和11.7%大环结构,α-螺旋结构未检出.琥珀酰化修饰后,α-螺旋结构形成,含量为12.4%,其他二级结构含量变化不大.琥珀酰化修饰使酪蛋白胶束粒径减小,由不规则的球形转变为规则的球形,疏水性显著降低.研究结果可为牦牛乳酪蛋白的改性提供参考依据.     

玉米秸秆生物炭对Cd（Ⅱ）的吸附机理研究

以玉米秸秆为原料,在350℃和700℃热解温度下分别制备了两种生物炭（BC350和BC700）,并对其理化性质进行了表征。在700℃下制备的生物炭芳构化程度更高,疏水性更强,比表面积更大,孔结构发育更加完全。研究Cd（Ⅱ）在两种生物炭上的吸附发现,Two-site Langmuir吸附等温模型比One-site Langmuir吸附等温模型能更好描述Cd（Ⅱ）在生物炭表面的吸附。BC700对Cd（Ⅱ）的吸附容量大于BC350,解吸率远小于BC350,吸附效果更好;离子交换和阳离子-π作用两种吸附机理同时存在并共同作用,前者分别占BC350和BC700总吸附容量的13.7%和1.1%,后者分别占86.3%和98.9%,阳离子-π作用是最主要的吸附机理。红外光谱FTIR分析表明,生物炭表面的含氧官能团和π共轭芳香结构分别提供不同机理的吸附位点。由于具有更多的离子交换位点,BC350对Cd（Ⅱ）吸附受pH影响较BC700更大。     

用低场核磁共振研究盐溶液漂洗对带鱼鱼糜凝胶品质的影响

为了比较单一成分盐溶液(质量分数为0.30%Na Cl、0.06%Ca Cl2或0.50%柠檬酸钠)和复合盐溶液(0.15%Na Cl、0.04%Ca Cl2、0.35%柠檬酸钠)漂洗对带鱼鱼糜凝胶水分分布及其凝胶特性的影响,该文运用低场核磁技术测定鱼糜凝胶的水分弛豫时间和水分质子密度,并结合鱼糜凝胶含水率、持水性、凝胶强度及其电镜扫描图,对盐溶液漂洗效果进行探究。鱼肉经单一成分0.30%Na Cl、0.06%Ca Cl2或0.50%柠檬酸钠溶液漂洗,柠檬酸钠组鱼糜凝胶中的氢质子束缚力最大,水分难以迁移,自由水的相对含量最低;与单一成分漂洗相比,经过复合盐溶液漂洗后,鱼糜凝胶水分迁移力相对较低,自由水含量较少,而水分质子密度较高,水分分布均匀;盐溶液漂洗后鱼糜凝胶的持水性、含水率、凝胶强度、凝胶显微结构与鱼糜凝胶中的水分分布相关,利用复合盐溶液漂洗带鱼鱼肉,能更好地改善带鱼鱼糜凝胶品质。研究结果为改善鱼肉漂洗工艺、提高鱼糜品质提供参考。     

热处理强度对猪肉肌球蛋白结构及风味成分吸附特性的影响

为了探究热处理强度对肌球蛋白结构及风味吸附特性的影响,该文选取猪肉中肌球蛋白,采用拉曼光谱等技术,分析了不同温度(45、55、65、75、85℃)对肌球蛋白巯基总量、二级结构和表面疏水性的影响;然后选取8种典型肉品风味成分,建立肌球蛋白-风味化合物作用体系,以同一顶空内不同风味化合物浓度自由比例为指标,采用固相微萃取气质联用技术探究不同热处理强度对肌球蛋白风味吸附作用的影响。结果表明:整个热处理强度增加的过程中肌球蛋白巯基基团含量显著降低(P0.01);温度升至55℃蛋白分子展开,α-螺旋和β-折叠转换成β-转角及无规则卷曲结构;温度升至75℃蛋白分子变性,β-转角及无规则卷曲转换成α-螺旋和β-折叠结构;在温度升高至65℃的过程中蛋白表面疏水性持续增加,温度继续升高略有降低;蛋白对4种醛(3-甲基丁醛、戊醛、庚醛、辛醛)的吸附性在展开过程中增强,聚合过程中减弱;蛋白对2-戊酮的吸附性先降低后升高,45℃处理组最低,85℃处理组最高,对3种酮(2-庚酮、2-辛酮、2-壬酮)的吸附性呈先增加后降低再增加的趋势,蛋白变性时(75℃)显著低于其余温度条件(P0.01),85℃处理时显著高于其余温度条件(P0.01);研究结果为今后关于肉品风味形成机理的研究提供参考。     

热处理过程中肌肉蛋白与萜类化合物相互作用机制

为明确热处理过程中肌肉蛋白与萜类化合物的相互作用规律及机制,以肌原纤维蛋白（myofibrillar protein,MP）和肌浆蛋白（sarcoplasmic protein,SP）为研究对象,测定不同加热时间下表面疏水性、总巯基含量、粒径、二级结构含量等理化特性。选取炖煮猪肉中3种关键萜类化合物（3-蒈烯、柠檬烯、芳樟醇）,结合气相色谱-质谱联用,探究热处理过程中MP和SP对萜类化合物吸附能力与蛋白构象变化的相关性,并通过分子对接揭示肌肉蛋白与萜类化合物结合机制。结果表明：随加热时间延长,MP和SP的表面疏水性和总巯基含量先上升后下降,粒径持续上升,α-螺旋结构转化为β-折叠和无规则卷曲结构。加热5 min内,MP和SP二级结构展开,结合位点暴露,对萜类化合物吸附能力增强;继续加热后,MP和SP聚集使结合位点被掩埋,对萜类化合物吸附能力降低,且由于SP更高的聚集程度,加热10～60 min内吸附能力弱于MP。分子对接结果证明,疏水相互作用为3-蒈烯和柠檬烯与肌肉蛋白结合的主要驱动力,而芳樟醇通过疏水相互作用和氢键与肌肉蛋白结合。结果表明热处理可以通过改变肌肉蛋白构象控制风味结合位点暴露或掩埋,从而影响肌肉蛋白与萜类化合物的相互作用,研究结果可为热加工肉制品的风味调控提供理论指导。     

羟基自由基氧化对乌贼蛋白分子间作用力及结构的影响

为研究贮藏过程中蛋白质氧化对蛋白质分子间作用力的影响机理,通过建立羟基自由基(·OH)氧化体系体外模拟乌贼肉在冻藏过程中蛋白质氧化的过程,从而探究蛋白质分子间作用力与结构的变化情况。结果表明,随着·OH氧化体系中H₂O₂浓度的增加,乌贼肌原纤维蛋白分子间作用力平衡被打破,离子键和氢键含量逐渐降低,疏水作用力逐渐增强,二硫键和非二硫共价键含量逐渐增加;肌原纤维蛋白表面疏水性逐渐增加;巯基与活性巯基含量逐渐降低。应用红外光谱(FTIR)分析氧化过程中蛋白质二级结构的变化规律,结果表明,自由基对氨基酸侧链和蛋白肽链进行了攻击,随着H₂O₂浓度的增加,光谱带向不同波数方向有规律地移动,蛋白质二级结构发生变化,α-螺旋和β-折叠含量降低,β-转角和无规则卷曲含量增加。石蜡切片显示,随着H₂O₂浓度的增加,肌纤维蛋白结构趋于疏松、间隙持续增大、肌丝变细且断裂卷曲量增多。本研究为探究乌贼肉蛋白质氧化的机理提供了理论依据,为延长乌贼贮藏期、提高经济效益与食用品质等相关研究奠定了理论基础。     

超高压前处理对虾仁冻藏期品质的影响

为研究超高压辅助脱壳所得到的中华管鞭虾虾仁在冻藏期的品质变化,以虾仁色泽、质构、肌原纤维蛋白相对含量、表面疏水性、总巯基相对含量和Ca²⁺-ATPase活性为指标,探讨超高压前处理对虾仁品质的影响。结果表明,冻藏6个月后虾仁L^*值、a^*值和b^*值均有所变化,与对照组相比,超高压前处理对虾仁L^*值的影响不显著,但能延缓冻藏后期a^*值的增加,对保持虾肉色泽的稳定有一定作用;超高压前处理对虾仁的咀嚼性和弹性影响不显著,但能增加虾仁的硬度。超高压前处理使冻藏初期虾仁肌原纤维蛋白的表面疏水性增加,而对其溶解性、巯基含量及Ca²⁺-ATPase活性的影响不显著;冻藏后期由于虾仁蛋白冷冻变性,致使肌原纤维蛋白溶解性、巯基含量及Ca²⁺-ATPase活性下降。综上所述,超高压辅助脱壳在一定程度上有利于保持冻虾仁的色泽和硬度。本研究结果为利用超高压技术辅助脱除中华管鞭虾虾壳,生产冷冻虾仁提供了新思路。     

羟自由基氧化对牦牛肉肌原纤维蛋白生化特性的影响

为探究羟自由基(·OH)氧化处理对宰后牦牛肉成熟过程中肌原纤维蛋白氧化特性的影响,以经不同浓度(0、0.5、1、5、10、20 mmol·L^-1)羟自由基氧化体系氧化不同时间(0、0.5、1、12、24、48 h)的牦牛肉为研究对象,以未经处理的牦牛肉为空白对照,测定不同浓度不同氧化时间下肉样肌原纤维蛋白的羰基含量、巯基含量、二硫键含量、表面疏水性、Ca/K-ATPase活性等指标的变化规律。结果表明,随着H₂O₂浓度的增加及氧化时间的延长,不同处理组间牦牛肉肌原纤维蛋白均表现出不同程度的氧化水平,其中羰基含量、二硫键含量和Ca-ATPase活性均呈显著增加趋势(P<0.01),而表面疏水性呈先上升后下降的趋势,巯基含量和K-ATPase活性则显著降低(P<0.01)。H₂O₂浓度增加至20 mmol·L^-1时,与空白对照组相比,羟自由基处理组羰基含量升高46.03%,而巯基含量下降79.79%。综上,羟自由基促使宰后牦牛肉成熟过程中肌原纤维蛋白发生了显著氧化,增加了蛋白的氧化程度。本研究结果为牦牛肉生产加工过程中蛋白氧化控制提供了一定的参考。     

超高压微射流对花生蛋白结构的影响（简报）

为了探讨超高压微射流对花生蛋白理化性质和结构的影响,该文研究了花生蛋白溶液经超高压微射流处理后的颗粒大小、游离巯基基团、疏水基团和紫外吸收基团的变化规律。结果表明：花生蛋白的颗粒尺寸和游离巯基基团含量随着超高压微射流均质压力的增大而显著减小;疏水基团和紫外吸收基团的含量则随着均质压力的增大而显著增大,说明超高压微射流处理可破坏花生蛋白的内部基团,使蛋白的结构发生变化。     

红外光谱法研究铬对酵母细胞内蛋白二级结构的影响

利用氨水、Sephadex G-75对富铬酵母、空白酵母进行蛋白提取,采用红外光谱测定及数学方法对比分析铬作用前后蛋白质二级结构的变化,探讨铬对蛋白结构的影响。结果显示,铬与蛋白的键合导致大分子蛋白中的α-螺旋结构和无规则卷曲结构被破坏,α-螺旋结构由11.35%降至1.63%,无规则卷曲结构略有下降,β-转角结构增加,由33.88%升至52.72%,β-折叠结构几乎无变化;小分子蛋白的β-折叠结构被破坏,由61.41%降至48.54%,无规则卷曲和α-螺旋结构比例增加,由1.41%增加至13.30%,α-螺旋结构略有增加,β-转角结构几乎无变化。与铬结合的大分子蛋白中,β-转角结构占优势;与铬结合的小分子蛋白中,β-折叠结构占优势。     

Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin

Physicochemical changes of myosin during heating were investigated to elucidate the mechanism of heat-induced gelation of arrowtooth flounder (ATF) myosin at high ionic strength. Changes in dynamic properties indicated ATF myosin formed a gel in three different stages as shown by the first increase in G' (storage modulus) at 28 degrees C, followed by the decrease at 35 degrees C and the second increase at 42 degrees C. DSC thermogram showed the onset of myosin denaturation at 25 degrees C with two maximum transition temperatures at 30 and 36 degrees C. The decrease in alpha-helical content indicated ATF myosin began to unfold at 15 degrees C and the unfolding continued until it reached 65 degrees C. Turbidity measurement showed myosin began to aggregate at 23 degrees C and the aggregation was complete at 40 degrees C. Surface hydrophobicity increased consistently in the temperature range studied, 20-65 degrees C. Sulfhydryl contents decreased significantly at 20-30 degrees C due to the formation of disulfide linkages but remained constant at temperatures >30 degrees C. ATF myosin was shown to be extremely sensitive to heat, resulting in denaturation at lower temperature than other fish myosin. Denaturation was initiated by unfolding of the alpha-helical region in myosin followed by exposure of hydrophobic and sulfhydryl residues, which are subsequently involved in aggregation and gelation processes.     

Effect of moisture content during dry-heating on selected physicochemical and functional properties of dried egg white

This article addresses the effect of moisture content (0.8-9.9%) during dry-heating (80 degrees C) on selected physicochemical (solubility, turbidity, residual denaturation enthalpy, aggregation, surface hydrophobicity, and sulfhydryl content) and functional (foaming ability, foam density, and stability) properties of freeze-dried egg white (FDEW). Moisture content during dry-heating proved to be a parameter determining the functionality of the resulting egg white powder. The degree of conformational changes induced in the egg white proteins by dry-heating was strongly dependent on the amount of water present. Preferentially, dry-heating at 80 degrees C should be performed on egg white powder with a moisture content below 6.8%, as the loss of protein solubility above this value is extensive. In addition to insoluble aggregates, soluble, strongly stabilized aggregates were also formed, especially at higher moisture contents. The decrease in denaturation enthalpy, increase in surface hydrophobicity, and exposure of SH groups previously hidden in the protein core and their subsequent oxidation were more pronounced at prolonged dry-heating times and at higher moisture contents. These conformational changes resulted in improved foaming ability and foams with lower density. No effect of dry-heating on the foam stability was observed.     

高密度CO2处理虾肌球蛋白形成凝胶的临界浓度与凝胶强度

为了探讨高密度CO_2(dense phase carbon dioxide,DPCD)诱导蛋白质形成凝胶的机制,以凡纳滨对虾肌球蛋白为研究对象,研究了DPCD处理压强、温度和时间对虾肌球蛋白形成凝胶的临界浓度和对虾肉糜凝胶强度的影响。研究结果表明:DPCD处理压强和温度对虾肌球蛋白溶液形成凝胶的临界浓度有显著影响,处理时间对肌球蛋白溶液形成凝胶的临界浓度无显著影响,但增加处理时间,可以形成更加紧实的凝胶。在40℃和5~30 MPa时虾肌球蛋白溶液形成凝胶的临界质量浓度为14 mg/mL,在50℃和5、10 MPa时虾肌球蛋白溶液形成凝胶的临界质量浓度为12 mg/mL,在50℃和15~30 MPa时虾肌球蛋白溶液形成凝胶的临界质量浓度为11 mg/mL,在60℃和5~30 MPa时虾肌球蛋白溶液形成凝胶的临界质量浓度为10 mg/mL。DPCD处理压强和温度对虾肉糜的凝胶强度也具有显著影响(P0.05),且随着压强增加和温度升高,虾肉糜凝胶强度呈增加趋势(P0.05);在50℃和25 MPa下处理虾肉糜20 min,形成的凝胶强度较好,达到了(14.28±0.57)N·mm。DPCD处理温度越高,虾肌球蛋白形成凝胶的临界浓度就越低,而虾肉糜形成凝胶的强度越高;DPCD处理压强越高,虽然对虾肌球蛋白形成凝胶的临界浓度影响较小,但能使虾肌球蛋白和虾肉糜形成凝胶的强度增加。从分析中还可以推断,DPCD低压(5~10 MPa)诱导虾肉糜形成凝胶主要是热效应的作用,DPCD较高压强(10 MPa)诱导虾肉糜形成凝胶是热和CO_2分子效应的共同作用。研究结果为进一步阐明DPCD诱导蛋白质形成凝胶的机制提供了基础数据。     

Heat-induced gels of egg white/ovalbumins from five avian species: thermal aggregation, molecular forces involved, and rheological properties

Product processing (heating, pH change, etc.) usually alters protein structure, improves rheological properties, and gives a unique texture to foods. The thermal aggregation and structural properties of ovalbumins from five avian species were studied at different pH values by polyacrylamide gel electrophoresis (PAGE) and determinations of sulfhydryl group content and surface hydrophobicity. The results showed that sulfhydryl group content changed insignificantly in heat-denatured ovalbumins other than hen ovalbumin (pH-independent), and surface hydrophobicity markedly increased (pH-dependent) after heating, with a significant difference among species. Furthermore, it was demonstrated that the hydrophobic interaction and sulfhydryl-disulfide interchange reaction were necessary in the aggregation and cross-linking of gel networks. Creep tests were also used to characterize the gel network structures of various egg white/ovalbumins upon heating. The viscoelastic behavior of the ovalbumins of all species was dependent on pH values, and changed significantly with the phylogeny of these species. With increases in pH value (7.0-8.5), the heat-induced gels of ovalbumins gradually changed from turbid to translucent, the instantaneous modulus (E(0)) increased slightly and reached a nearly constant value, and the Newtonian modulus (etaN) increased significantly in each sample. The heated egg white from these five avian species also formed highly viscoelastic gels, with a good correlation of viscoelastic behavior between ovalbumin and egg white in corresponding species.     

Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles

Thermal denaturation and aggregation abilities of salmon myofibrils and myosin were studied measuring turbidity, intrinsic fluorescence, 8-anilino-1-naphthalene sulfonic acid binding, and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide cross-linking. The thermal behaviors of protein preparation from white and red muscles were compared, and the relationship with thermal gelation properties is discussed. The low gelation ability of salmon muscle proteins was related to a limited extent of protein denaturation and aggregation upon heating. These properties seemed to be carried by myosin molecules as a similar behavior was observed for both myofibrils and myosin preparations. The higher thermal stability observed for red muscle proteins with higher transition temperatures in rheological profiles was related to a shift to higher temperature in denaturation and aggregation processes. The extent of denaturation and aggregation was very similar for both muscle types as was the final rigidity of the gels formed.     

Interaction between β-casein and whey proteins as a function of pH and salt concentration

The effectiveness of β-casein as a chaperone in the aggregation of whey proteins was investigated. β-Casein altered heat-induced aggregation as shown by a reduction in turbidity of β-lactoglobulin, α-lactalbumin, and bovine serum albumin (BSA) solutions. The pH of the mixtures greatly affected how much β-casein reduced the turbidity of the solutions; the maximum reductions in turbidity were observed at pH 6.0. Reducing the pH decreased the effectiveness of β-casein as a chaperone. An increase in ionic strength by the addition of NaCl or CaCl(2) also decreased the effectiveness of the chaperone. The addition of CaCl(2) had a larger effect than the addition of NaCl. The chaperone effect was seen at temperatures up to 145 °C. Differential scanning calorimetry (DSC) showed that β-casein did not alter the denaturation temperature of β-lactoglobulin. The kinetics curves for loss of native protein and turbidity development showed that β-casein did not function by slowing the aggregation process. It was concluded that β-casein competes with whey protein in the aggregate process and the aggregates formed in the presence of β-casein are smaller in size than those formed during whey protein self-aggregation. The formation of smaller aggregates gives rise to less turbid, more soluble protein solutions.