改性方法对核桃浓缩蛋白凝胶性的影响

分别采用物理及化学方法对核桃浓缩蛋白进行改性,通过测定改性后蛋白中游离巯基、二硫键含量及表面疏水性指数等指标,研究不同的改性方法及条件对核桃浓缩蛋白质凝胶性的影响,以获得具有形成强凝胶潜力的蛋白质,确定适宜的改性条件,并对改性前后蛋白凝胶质构性进行分析。结果表明:物理改性(超声处理)的适宜条件为超声功率840 W,超声时间6min;化学改性(还原剂亚硫酸钠)的适宜条件为还原剂加入量0.625 mmol/L,处理时间60 min。经超声改性后的核桃浓缩蛋白,其凝胶性能最优。     

肌肉蛋白质的热诱导凝胶特性及其影响因素

肌肉蛋白质的热诱导凝胶作用及相关的脂肪和水的结合性质是肉制品最重要的加工特性（Smith,1988;Gordon and Barbut,1992）。热诱导凝胶作用是指变性的蛋白质分子经分子间的作用力（包括氢键、离子键、二硫键、疏水基作用力等）聚集并形成一种有序的三维网状结构,脂肪和水以物理和化学的方式包含在蛋白质基质中（Ferry,1948）。蛋白质的这种热诱导凝胶作用在很大程度上决定了肉糜制品的质地、外观和出品率,蛋白质凝胶特性受蛋白质结构特征和分子特性的影响（例如：疏水基作用力、表面电荷、巯基含量、分子量、构象稳定性和聚合／解聚行为）。另外,加工条件、环境因素（例如pH、离子强度）及其与基它成分间的相互作用也影响肉糜制品中蛋白质的凝胶特性。     

肌肉盐溶蛋白热诱导凝胶特性研究进展

综述肌肉中盐溶蛋白质的性质、成胶机制,以及影响其成胶的重要因素,并简述肉制品加工中广泛应用的亲水胶体和谷氨酰胺转氨酶对肌肉盐溶蛋白热诱导凝胶特性的影响的最新进展.     

高压处理对僵直前肌肉质量的影响

对所有食品及其组分来讲,肌肉和肌蛋白对压力的反应最为迅速。这是由于糖酵解过程对压力有较高的敏感性,以及肌原纤维蛋白之间的相互连接。应该指出,这里所讨论的压力处理是在排除自由空气的方式下进行包装的,这可避免因压力增加时由于气体溶解而引起样品成分的复杂变化。一、对嫩度的影响如果将所屠宰的牛或羊的热肉在大约100MPa压力下处理1分钟或更长时间,发现肌肉强烈收缩且手感坚硬。表1给出了僵直前肌肉经压力处理和未经压力处理的有关数据。压力处理的结果,肌肉收缩35％,而     

高压处理对花生分离蛋白凝胶特性和分子结构的影响

本文研究了质量浓度为5%的花生分离蛋白(PPI)在50-200 MPa压力范围处理5 min后的热凝胶硬度、弹性和粘结力的变化情况,并对处理前后的PPI进行了SDS-PAGE、圆二色谱(CD)、质谱和分子结构模拟分析。SDS-PAGE电泳结果表明,PPI中分子量为61.0 ku的亚基对压力最敏感,对此亚基进行质谱分析,结果表明压力处理后,此亚基的氨基酸序列未发生变化,含580个氨基酸,实际分子量为66.5 ku,为伴花生球蛋白Ⅱ的电泳条带,在此基础上进行分子模拟,发现其空间构象在100 MPa处理后发生了显著变化。CD结果表明,高压处理后,PPI的二级构象发生了显著变化。PPI热凝性结果表明,100 MPa处理后其形成的热凝胶硬度最大,为172 g,比未处理提高了49.6%,弹性和粘结力与未处理相当。以上结果说明压力处理使得PPI热凝胶特性得到了改善。     

热处理对大豆分离蛋白结构和凝胶性的影响

通过对大豆分离蛋白（soybean protein isolate,SPI）的亚基组成及结构、自由氨基浓度、游离巯基含量、 表面疏水性及凝胶强度的测定,研究热处理对SPI理化性质、结构特性及凝胶特性的影响。研究表明,随着热处理 温度的升高,SPI亚基解离加剧,SPI的β-折叠含量明显下降,无规卷曲含量显著增加。当热处理时间为10 min、温 度从70 ℃提高到95 ℃时,SPI中自由氨基浓度、自由巯基含量及表面疏水性呈上升趋势,SPI形成凝胶的强度先升 高后降低,凝胶失水率呈下降趋势。当热处理温度为90 ℃,随着时间从5 min延长到60 min时,SPI中自由氨基浓 度不断增加,自由巯基含量及表面疏水性则先增加后降低,SPI形成凝胶的强度呈上升趋势,凝胶失水率呈下降趋 势。随着凝胶保温时间的延长和温度的提高,SPI凝胶的强度均不断提高,失水率均不断下降。综合考虑,制备SPI 凝胶的最佳条件为：热处理90 ℃、15 min,保温90 ℃、30 min。     

改性对大豆分离蛋白凝胶性的影响

介绍了物理改性、化学改性、酶改性、基因工程改性等改性方法对大豆分离蛋白凝胶性的影响,并对此方面的研究趋势进行了预测.     

辐照对肌肉蛋白结构及其凝胶性能影响的研究进展

对肉类食品来说,辐照不仅能有效杀灭其中的微生物,而且能作用于蛋白质等生物大分子,影响蛋白间的相互作用力,从而改变蛋白质构象,导致蛋白变性、聚集或凝胶化,因此利用电子束辐照处理,有望成为改善肌肉蛋白凝胶品质的一种有效手段。本文列举了常用于表征蛋白质结构的光学仪器如拉曼光谱、红外光谱、圆二色谱等在肌肉蛋白构象研究中的应用,综述了辐照引起肌肉蛋白生化特性、化学作用力和构象的改变,以及这种改变对肌肉凝胶网络结构形成的作用,在分子水平上探讨了辐照对肌肉凝胶特性的影响机理,为利用辐照技术改善肌肉凝胶性能提供理论指导。      

超高压预处理对肌肉匀浆物凝胶保水特性的影响

采用均匀试验设计,研究不同压力和保压时间预处理对猪肉匀浆物凝胶保水特性的影响。结果表明:肌肉匀浆物中可溶性蛋白质浓度和凝胶的保水率均随着处理压力的降低和保压时间的缩短而逐渐升高;肌肉匀浆物凝胶的成胶脱水率变化趋势随处理条件的变化而不同,在保压时间较长时,随着压力的上升而增大;保压时间较短时,随着压力的升高而降低。相同压力下,凝胶的成胶脱水率随保压时间的延长呈先升后降的趋势。     

Cold-set gelation of high pressure-treated soybean proteins

The ability of soybean proteins to form cold-set gels, using high pressure (HP) processing as denaturing agent and calcium incorporation was evaluated. Different protein preparations were assayed: soybean protein isolate (SPI), a β-conglycinin enriched fraction (7SEF) and a glycinin enriched fraction (11SEF). 7SEF formed aggregated gels with low water holding capacity whereas 11SEF did not form self-standing gels. SPI formed the better gels: ordered and with high water holding capacity. SPI gels were relatively soft and their visual aspect, rheological and texture properties, and water holding capacity depended on HP level (400–600 MPa), CaCl₂ concentration (0.015–0.020 mol L⁻¹) and protein concentration (85–95 g L⁻¹), thus gels with different characteristics may be obtained. The gels comprised a three dimensional network stabilized by non-covalent interactions with spaces filled of proteins in aqueous solution. The results indicate that it is possible to use HP and subsequent calcium incorporation to form self-standing cold-set gels from soybean proteins. These gels may be of interest to incorporate heat-labile compounds or probiotics during the gelation step.     

Factors Affecting the Gelation Properties of Hydrolyzed Sunflower Proteins

The effects of temperature and several chemicals on gelation time and strength of gels formed by heating (pH 8) 5% solutions of trypsin hydrolyzed sunflower proteins were studied by dynamic rheological methods. The storage modulus reached a maximum at 80°C. Ca₂Cl (and NaCl at > 0.2M) accelerated gelation and weakened the gel. NaCOCH₃Na₂SO₄ and NaSCN decreased the storage modulus. Urea decreased gelstrength and at high concentrations slowed gelation. Time for gelation diminished and gel strength increased with increasing mercaptoethanol concentration up to 0.1M. Propylene glycol at 5–20% concentrations accelerated gelation and at 5% also increased gel strength. Trypsin hydrolyzed sunflower proteins could be useful in products requiring strong gels at high temperatures.     

Gelation of Proteins from Washed Muscle of Threadfin Bream (Nemipterus japonicus) under Mild Acidic Conditions

Gelation of proteins of washed mince of threadfin bream was induced by the organic acids: acetic, lactic, tartaric, and citric. Washing of mince was essential for gelation. The strength of acetic acid-induced gel was affected by setting conditions and heat treatment. Gelation was associated with degradation of myosin heavy chain and appearance of a new protein band of about 160 kDa. Solubility studies of the gel in various solvents suggested structural changes. Gelation was also associated with oxidation of sulfhydryl groups. Salts negatively influenced gelation.     

Protease-Induced Aggregation and Gelation of Whey Proteins

Aggregation and gelation of whey proteins induced by a specific protease from Bacillus licheniformis was revealed by turbidimetry, size exclusion chromatography, dynamic light scattering and rheology. The microstructure of the gel was examined by transmission electron microscopy. During incubation of 12% whey protein isolate solutions at 40°C and pH 7, the major whey proteins were partly hydrolyzed and the solution gradually became turbid due to formation of aggregates of increasing size. The viscosity of the hydrolysate simultaneously increased and eventually a gel formed. The gel had a particulate type of microstructure. We hypothesized that the aggregates forming the gel were held together by noncovalent interactions.     

Gelation mechanism of milk as influenced by temperature and pH; studied by the use of transglutaminase cross-linked casein micelles

Casein micelles in milk are colloidal particles consisting of four different caseins and calcium phosphate, each of which can be exchanged with the serum phase. The distribution of caseins and calcium between the serum and micellar phase is pH and temperature dependent. Furthermore, upon acidification casein micelles lose their colloidal stability and start to aggregate and gel. In this paper, we studied two methods of acid-induced gelation, i.e., 1) acidification of milk at temperatures of 20 to 50 degrees C and 2) decreasing the pH at 20 degrees C to just above the gelation pH and subsequently inducing gelation by increasing the temperature. These two routes are called T-pH and pH-T, respectively. The gelation kinetics and the properties of the final gels obtained are affected by the gelation route applied. The pH-T milks gel at higher pH and lower temperature and the gels formed are stronger and show less susceptibility to syneresis. By using intramicellar cross-linked casein micelles, in which release of serum caseins is prevented, we demonstrated that unheated milk serum caseins play a key role in gelation kinetics and characteristics of the final gels formed. This mechanism is presented in a model and is relevant for optimizing and controlling industrial processes in the dairy industry, such as pasteurization of acidified milk products.     

Thermal Gelation of Stretched and Cold-Shortened Bovine Sternomandibularis Muscle and Myofibrils

Muscle gels (10% protein) and myofibril gels (8% protein) were prepared at pH 6.0 with 2% NaCl and a heating rate of 0.7°C/min. No difference in gel strength occurred between stretched and cold-shortened muscles, but cooking loss was lower for stretched muscle. Stretched muscle sarcomeres were longer than those of cold-shortened muscle. The myofibril fraction from stretched muscle had higher gel strength, viscosity index, elasticity, and lower cooking loss than that from cold-shortened muscle. These results suggest that the contractile state of the muscle affects protein binding and water binding of the myofibrillar fraction.     

Partial purification of horse-specific soluble muscle proteins by immunoadsorption chromatography

Immunoadsorption chromatography has been used to isolate horse-specific soluble muscle proteins from crude horse protein extracts. Horse-specific polyclonal antibodies against soluble horse muscle proteins immobilised on a Protein A-Sepharose CL-4B matrix were used to adsorb the corresponding antigens. Analysis of the crude soluble horse muscle proteins by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) showed the existence of 20 protein subunits in the gel. SDS-PAGE of the proteins recovered by affinity chromatography showed nine protein subunits, three of which were enriched after the immunopurification step. These affinity-recovered horse-specific soluble muscle proteins may be used as antigens in the development of monoclonal antibodies to detect and quantify horse meat in raw, unheated meat mixtures.     

Heat-induced Gelation Properties of Salt-Soluble Muscle Proteins as Affected by Non-Meat Proteins

Addition of whey protein concentrate (WPC), whey protein isolate (WPI) or soy protein isolate (SPI) to salt-soluble muscle proteins (SSP) decreased the gel strength. WPI:SSP gels had higher water-holding capacity than SSP, SSP:WPC or SSP:SPI gels. Myosin heavy chain was a principal contributor to gel network formation in SSP, SSP:WPC, SSP:WPI and SSP:SPI systems. The characteristic fibrous network formed by SSP was the dominant feature of the microstructure of SSP:WPC and SSP:WPI gels. SSP:SPI gels had a more aggregated appearance due to the occurrence of clusters of SPI throughout the gel matrix.     

Gelation properties of previously cooked minced meat from Jonah crab (Cancer borealis) as affected by washing treatment and salt concentration

The influence of washing treatment (dewatered only, one wash, and three washes) and sodium chloride (NaCl) concentration (0%, 2%, and 4%) on the gelation properties of crab mince was investigated. This previously cooked muscle mince is a low-value by-product of the crab processing industry, considered to have little or no functional properties. Crab mince gels were produced and tested for water-holding capacity (WHC), gel strength, colour, and electrophoretic profile. Wash treatment and NaCl concentration significantly affected gelation. Washed samples exhibited significantly higher WHC than dewatered samples. The 4% NaCl treatment decreased WHC compared to lower NaCl levels. Multiple washing steps increased the force to gel deformation. Wash treatment and NaCl concentration also affected the colour of gels. Based on these results, cooked crab meat mince treated with three washes and 0% NaCl resulted in the strongest gels with the best water-holding capacity, which can be used in the development of value-added products.