转谷氨酰胺酶的性质、制备及在食品加工中的应用

转谷氨酰胺酶是催化蛋白质分子之间交联的一种酶，对蛋白质的成胶能力、热稳定性、持水能力等功能特性有独特的改善作用。目前从微生物Streptoverticillium spp．中分离转谷氨酰胺酶和在食品工业中的实际应用都已经实现，因为从微生物制备可以实现大规模的工业化生产，成本低廉，为转谷氨酰胺酶在工业上的应用奠定了基础。现在转谷氨酰胺酶广泛地应用于海洋食品、面条／面团、奶制品、烘焙食品等食品加工领域，通过温和的酶反应可以明显地改善食品的硬度、弹性、热稳定性和持水能力。主要讨论了转谷氨酰胺酶的性质、分离和在食品加工中的应用。     

转谷氨酰胺酶和超高压技术在重组肉制品中的应用

介绍重组肉制品的定义、分类及加工原理,并对转谷氨酰胺酶和超高压技术在重组肉制品中的应用和研究进展进行综述,以期为转谷氨酰胺酶和超高压技术在重组肉制品加工中的应用提供参考。     

转谷氨酰胺酶对乳蛋白质的改性作用

转谷氨酰胺酶是催化酰基转移反应的一种酶,可使蛋白质或多肽之间发生共价交联反应。本文介绍了转谷氨酰胺酶对牛乳蛋白质凝胶特性、乳化性、热稳定性、成膜性等特性的改性作用及其在乳品加工中的应用。     

转谷氨酰胺酶及其在鱼糜制品加工中的应用

通过比较分析鱼内源性转谷氨酰胺酶(Fish endogenous transglutaminase,FTGase)和微生物来源的转谷氨酰胺酶(Microbial transglutaminase,MTGase)的性质和作用机理的异同。在此基础上探讨影响转谷氨酰胺酶(Transglutaminase,TGase)作用的因素(热处理方式、酶活促进剂、酶活抑制剂)及在鱼糜制品加工中的应用(改善凝胶特性、提高营养价值、提高持水性),并对TGase在今后的研究方向进行了展望,以期为TGase在鱼糜制品加工中的开发利用提供参考。     

酶法交联对食物蛋白的改性作用研究进展

食物蛋白通过分子间或分子内的交联作用,可有效地改善功能特性,有利于在食品加工中的应用。可用于蛋白交联的酶主要有转谷氨酰胺酶、多酚氧化酶、过氧化物酶等。主要阐述了转谷氨酰胺酶、多酚氧化酶、过氧化物酶交联蛋白的作用机理及最新研究进展。     

浅谈几种酶在食品加工中的应用

主要介绍了超氧化物岐化酶、脂肪酶、转谷氨酰胺酶、纤维素酶、溶菌酶、葡萄糖氧化酶等六种酶在食品加工中的应用。     

转谷氨酰胺酶在食品中的应用

本文论述了转谷氨酰胺酶的作用机理、测定方法、来源及其生产工艺，以及在食品加工中的应用。     

转谷氨酰胺酶酶原在大肠杆菌中的重组优化表达

茂原链霉菌(Streptomyces mobaraensis)转谷氨酰胺酶酶原(pro-transglutaminase,pro-TG)在重组大肠杆菌中的表达量低,限制了其在食品、化妆品、纺织行业中的应用。通过对转谷氨酰胺酶酶原的基因序列进行密码子优化,降低其GC含量,提高了它在大肠杆菌中的表达水平,结果表明经优化后转谷氨酰胺酶原的表达量达到了优化前的4.4倍。为提高转谷氨酰胺酶的比活力,通过基于融合PCR的定点突变技术将转谷氨酰胺酶第二位的丝氨酸突变为脯氨酸,突变后转谷氨酰胺酶的比活力达到了突变前的1.26倍。上述研究结果表明,密码子优化及定点突变技术可以应用于优化转谷氨酰胺酶酶原在大肠杆菌中的表达。     

转谷氨酰胺酶及其在肉制品加工中的应用

本文论述微生物来源转谷氨酰胺酶反应机理与特性及其在肉制品加工中的应用。     

转谷氨酰胺酶在肉制品中的应用

从转谷氨酰胺酶所催化的生化反应入手,依据此酶对肌肉蛋白质作用的特点,阐述了转谷氨酰胺酶对改善肉制品质构、提高产品率、拓宽原料来源及开发新产品的重要作用,并且对转谷氨酰胺酶作用产物的生物利用性进行了探讨。     

转谷氨酰胺酶在食品加工中的应用

简要介绍了转谷氨酰胺酶的分类和性质,并从畜肉制品、乳制品、水产品、大豆蛋白制品、小麦粉制品和食品包装与保藏6个方面较为详细地介绍了其在食品加工中的应用情况。     

酪蛋白的转谷氨酰胺酶酶促糖基化交联条件及产物性质

在氨基葡萄糖存在的条件下,利用转谷氨酰胺酶(EC2.3.2.13)对酪蛋白进行糖基化交联修饰。以修饰酪蛋白产物中氨基葡萄糖的导入量为指标,采用单因素试验分别考察反应体系pH值、酶添加量、反应温度和时间对修饰反应的影响。优化后的适宜修饰条件为:酪蛋白底物质量浓度为30g/L,氨基葡萄糖添加量为3mol(每kg酪蛋白中)、pH值为7.5、酶添加量为10kU(每kg酪蛋白中)、反应温度为37℃、时间4h。与酪蛋白和转谷氨酰胺酶促交联的酪蛋白相比,修饰酪蛋白产物的乳化性质和胶凝性质得到显著改善,并且体外消化性能未受到影响,表明转谷氨酰胺酶催化的糖基化交联修饰可以用于改善酪蛋白的这些功能性质。     

Cross-Linking and Glucosamine Conjugation of Casein by Transglutaminase and the Emulsifying Property and Digestibility In Vitro of the Modified Product

Microbial transglutaminase was applied as a biocatalyst and glucosamine as an acyl acceptor to modify casein by cross-linking and glucosamine conjugation. Electrophoretic analysis revealed that transglutaminase-induced cross-linking and glucosamine conjugation occurred simultaneously during reaction, and some polymers of glycoproteins with higher molecular weights were formed in the modified casein product prepared. HPLC analysis demonstrated that about 1.2 mol of glucosamine was conjugated to 1 mol of casein, under the preparation conditions as follows: casein concentration of 3% (w/v), molar ratio of acyl donor in casein to glucosamine acceptor of 1:3, transglutaminase addition level of 10 U/g casein, reaction temperature of 37°C, and reaction time of 4 h. The evaluation results also showed that the surface hydrophobicity of the modified casein product decreased. The emulsifying activity index and emulsifying stability index of the modified casein product were 100.9 m²/g and 84.3%, about 12 and 20% higher than that of original casein. The digestibility in vitro of the modified casein product was the same as that of original casein or had an increase of 9.8%. Meanwhile, cross-linking of casein by transglutaminase in the absence of glucosamine showed adverse impact on the emulsifying properties of the cross-linked casein prepared. The new modification method developed might have the potential as an effective approach to improve the functional properties of food proteins.     

Study on the Functional Properties of Soybean Protein Isolate Cross-Linked with Gelatin by Microbial Transglutaminase

A microbial transglutaminase was used to cross-link soybean protein isolates in the presence of gelatin to prepare a cross-linked composite soybean protein-gelatin. Cross-linking conditions, such as total proteins, the ratio of soybean protein isolates to gelatin, and original pH, were fixed at 5% (w/v), 4:1 (w/w), and 7.5, respectively. The 4-hydroxyproline content in the modified product was measured and used as an index to select suitable transglutaminase addition, reaction temperature, and time by single factor experiments, which were found to be 20 U/g proteins, 40°C, and 2 h, respectively. Under the identified conditions, a modified product with 4-hydroxyproline content of about 36 mg/g proteins was prepared, and its functional properties were evaluated. SDS-PAGE analysis showed that several protein polymers existed in the modified product. Compared to the original soybean protein isolates or a cross-linked soybean protein isolates, the modified product had a better emulsifying stability and water holding capacity but a poor enzymatic digestibility in vitro, emulsifying activity and oil binding capacity; meanwhile, the dispersions formed by the modified product exhibited the highest apparent viscosity, storage modulus, and viscous modulus.     

高纤维酸浆豆干制作配方优化及品质分析

本文以提高豆干副产物利用及生产高品质豆干为目的,在酸浆豆干制作工艺的基础上,添加豆渣和谷氨酰胺转氨酶(TG酶),选择豆水比例、豆渣添加量、酸浆添加量和TG酶添加量为考察因素,以感官评分为评价指标,优化高纤维酸浆豆干的制备工艺,并将其与传统酸浆豆干进行比对,分析二者的膳食纤维含量、感官评价、质构特性、蛋白质结构和微观结构...     

Determination of microbial transglutaminase in meat and meat products

Transglutaminase is an enzyme that can be used to cross-link pieces of meat, fish or meat products. The resulting product gives the optical impression of an intact chunk of meat. The usage of transglutaminase as a food additive is permitted in some countries. However, its utilisation has to be declared to ensure transparency for consumers. This paper describes two orthogonal analytical methods suited for the detection of technological relevant transglutaminase concentrations (around 25?mg pure enzyme in 1?kg of product) in meat and meat products. The mass spectrometry-based approach relies on a previous digestion with Achromobacter lyticus protease and LC-MS/MS separation and detection. Sufficient selectivity was obtained by monitoring four different peptides. The orthogonal (complementary and independent), ELISA-based approach relies on two commercially available bacterial transglutaminase-specific antibodies, combined to a sandwich ELISA. The two methods were tested by analysing some 60 samples obtained from the market.     

Determination of microbial transglutaminase in meat and meat products

Transglutaminase is an enzyme that can be used to cross-link pieces of meat, fish or meat products. The resulting product gives the optical impression of an intact chunk of meat. The usage of transglutaminase as a food additive is permitted in some countries. However, its utilisation has to be declared to ensure transparency for consumers. This paper describes two orthogonal analytical methods suited for the detection of technological relevant transglutaminase concentrations (around 25?mg pure enzyme in 1?kg of product) in meat and meat products. The mass spectrometry-based approach relies on a previous digestion with Achromobacter lyticus protease and LC-MS/MS separation and detection. Sufficient selectivity was obtained by monitoring four different peptides. The orthogonal (complementary and independent), ELISA-based approach relies on two commercially available bacterial transglutaminase-specific antibodies, combined to a sandwich ELISA. The two methods were tested by analysing some 60 samples obtained from the market.     

Transglutaminase-mediated incorporation of whey protein as fat replacer into the formulation of reduced-fat Iranian white cheese: physicochemical,rheological and microstructural characterization

The effects of transglutaminase treatment (0–2 units/g milk protein) on the chemical composition, textural characteristics, proteolysis and yield of reduced-fat Iranian white cheese (milk fat: 0.4–1.4% w/w) incorporated with whey proteins (0–6 g/L milk) were investigated. Enzyme-mediated inclusion of whey proteins in the reduced-fat cheese caused a noticeable increase in moisture to protein (M:P) ratio with concomitant decease in the hardness rheological parameters of fracture stress and Young’s and storage (G’) moduli. However, increase in concentrations of whey proteins or/and transglutaminase enzyme above a critical level led to formation of a cheese matrix with lower moisture content and greater values of hardness indices. Whey protein addition and transglutaminase treatment resulted in the same trends of changes in proteolysis rate and cheese yield as in cheese softness. Response surface method (RSM) suggested that the enzymatic incorporation of 4.2 g deliberately added whey proteins to 1 L of milk (1.04% w/w fat) into the cheese matrix using 0.833 unit transglutaminase per gram milk protein would provide a reduced-fat product with the softest texture and the highest yield. The scanning electron micrographs showed formation of honeycomb structures in the protein matrix of the reduced-fat sample with optimum formulation.     

Effect of heat and transglutaminase on solubility of goat milk protein‐based films

The effect of heat, transglutaminase and combination of heat and transglutaminase treatments on the solubility of films prepared from goat milk casein, goat milk whey proteins and whole goat milk proteins was investigated. Goat milk casein films were less soluble when treated with transglutaminase and combination of heat with transglutaminase compare with heat‐treated caseins alone. Heat treatment was more effective at decreasing the solubility of whey protein films. SDS‐PAGE patterns demonstrated that goat milk caseins were better cross‐linked by transglutaminase, whereas whey proteins were better cross‐linked by heat. The extent of cross‐linking was further enhanced when a combination of heat and transglutaminase was used.