Enzymatic modification of selected functional properties of myofibril preparation obtained from mechanically recovered poultry meat

The effect of addition of 3 g/L of commercially available transglutaminase preparation to protein extracts obtained from mechanically recovered poultry meat was studied. The content of free thiol groups (–SH), thermal drip and gel texture were determined. After pre-incubation at 7–8 °C for 1, 3, 5 and 24 h, the samples were subjected to one-step heating at 50, 60, 70 and 80 °C and two-step heating at 50/80, 55/80 and 60/80 °C. The addition of preparation and the extension of pre-incubation time led to decrease of free -SH groups content. After heating, the number of thiol groups decreased, the texture was improved, but thermal drip from gels increased. The amount of –SH groups in gel extracts subjected to one-step heating decreased with simultaneous increase of mechanical strength of gels. Protein gels subjected to two-step heating exhibited higher firmness than gels subjected to one-step heating. Thus, the 3 g/L addition of transglutaminase preparation in combination with one-step thermal processing at 70 °C and pre-incubation for 3 h contributed to improvement of texture properties of model gels and low thermal drip.     

微生物转谷氨酰胺酶(MTGase)的蛋白质底物催化特性及其催化机理研究 (I)MTGase催化单底物蛋白质的聚合特性

采用SDS-PAGE结合凝胶成像技术比较了MTGase在还原状态下对酪蛋白酸钠(SC)、牛血清蛋白(BSA)、大豆球蛋白(glycinin)和β-伴豆球蛋白(β-conglycinin)、β-乳球蛋白(β-LG)和α-乳白蛋白(α-LA)等单底物蛋白的聚合效率。结果表明MTGase较易催化SC和BSA聚合,其次为大豆球蛋白,而β-伴豆球蛋白、β-LG和α-LA最不易。根据MTGase催化不同单底物蛋白质的聚合速率的差异,对MTGase催化单底物蛋白质的聚合特性进行了探讨,指出:①底物蛋白的分子结构对MTGase催化活性的重要性;②蛋白质表面疏水度对MTGase催化活性的重要性;③对蛋白质进行一定的预处理可增强MTGase对蛋白质(特别是球蛋白)的催化活性。     

转谷氨酰胺酶对蛋白质凝胶性能的影响

本文研究了转谷氨酰胺酶浓度、反应温度、pH、时间对非肉蛋白质凝胶硬度的影响。结果表明转谷氨酰胺酶添加浓度在10-40U／g蛋白质，反应温度4-60℃，pH6-7，反应时间50-300min范围内，对于大豆分离蛋白、酪蛋白、乳清浓缩蛋白、卵清蛋白、明胶蛋白5种非肉蛋白质作用，均可以获得蛋白质凝胶能力以及凝胶性能的提高，表现在形成凝胶蛋白质极限浓度的降低以及凝胶硬度的提高。     

转谷氨酰胺酶及其在食品工业中的研究进展

本文论述了转谷氨酰胺酶的来源、制备、理化性质、功能特性和作用原理,并介绍了转谷氨酰胺酶在肉制品加工、乳制品加工、水产品加工、植物蛋白制品以及可食性保鲜膜等方面的应用情况。     

赖氨酸与谷氨酰胺在谷氨酰胺转胺酶作用下的交联反应

本文研究了赖氨酸与谷氨酰胺在谷氨酰胺转胺酶催化下的交联反应。探讨了底物比、加酶量、pH值、反应温度和反应时间对聚合度的影响。利用Design-Expert6.0.3软件优化得出交联反应的最佳工艺条件为底物比2.15、加酶量14.39U/g、pH值8.0、温度42℃和反应时间94min。同时,分析了各因素之间的交互效应。     

Physical properties of yoghurt manufactured with milk whey and transglutaminase

The effect of milk protein polymerization prior to the yoghurt fermentation process was evaluated by enzymatic reaction with microbial transglutaminase (Streptoverticillium mobaraense). Yoghurt samples were manufactured with 100% milk or by substituting milk with 20 or 30% of liquid milk whey, aimed at determining the use of natural milk whey in dairy products. Transglutaminase was added at a protein ratio of 0.5 U g⁻¹ to all samples and evaluated regarding rheological behavior, syneresis index and texture profile. The addition of enzyme transglutaminase contributed to syneresis prevention and increased the consistency index in yoghurt samples manufactured with milk whey. Yoghurt manufactured from 70% milk plus 20% milk whey, followed by enzymatic treatment, presented similar characteristics to traditionally manufactured yoghurt (C 100), with no alteration in the syneresis of the samples (p > 0.05) and presented texture parameters similar to the control yoghurt (C 100).     

Impact of microbial transglutaminase on the viscoelastic profile of formulated bread doughs

The effects of microbial transglutaminase (TGM) on the viscoelastic profile of wheat flour doughs when added singly and in combination with hydrocolloids—hydroxypropylmethylcellulose (HPMC) and a high ester pectin (GENU pectin type BIG, or BIG)—, amylolytic (-amylase) and non amylolytic enzymes (xylanase) and an emulsifier [diacetyl tartaric acid ester of mono-diglycerides (DATEM)] have been investigated by applying response surface analysis to a Draper-Lin small composite design of formulated dough samples. In spite of the major effects on mixing, textural, extensional and viscometric parameters, which were provided by hydrocolloid/surfactant combinations, incorporation of TGM into dough formulas improved some viscoelastic properties. TGM, when added to DATEM and/or HPMC-containing doughs, induced synergistic effects on mixing parameters, resulting in increased water absorption, development time and stability. Highly cohesive doughs with improved water holding capacity and gluten strength during mixing and fermentation, and suitable pasting behaviour during cooking were achieved using TGM/BIG/DATEM mixtures, mainly associated with suitable interactions of the pairs TGM/DATEM and DATEM/BIG.     

Effect of chymotrypsin digestion followed by polysaccharide conjugation or transglutaminase treatment on functional properties of millet proteins

Millet protein was solubilized by chymotrypsin; the soluble protein was conjugated to galactomannan under controlled conditions (60 °C, 76% RH) or polymerised by transglutaminase (TGase). SDS–PAGE patterns showed that the conjugated and polymerised proteins had higher molecular mass bands above the stacking gel. SDS–PAGE patterns also indicated that the digest was conjugated to galactomannan and polymerised by TGase. The free amino groups (OD₃₄₀) of the conjugated and polymerised digest were greatly reduced. Although the chymotrypsin digest was considerably insoluble between pH 2.0 and 5.0, galactomannan conjugate was completely soluble at all levels of pH. TGase polymer was slightly insoluble at pH 4.0. Galactomannan conjugate resisted heat-induced aggregation, even after heating at 90 °C for 20 min, while TGase polymer resisted heat-induced aggregation up to 70 °C, after which its solubility started to decline. The emulsifying properties of the conjugate and the polymerized proteins were greatly improved, compared to the native and chymotrypsin digests.     

Effect of selected substances on the properties of frozen myofibril preparation obtained from mechanically recovered poultry meat

The experimental material was a myofibrillar preparation obtained from mechanically recovered poultry meat by the washing and separation of fat and connective tissues. Changes occurring during frozen storage were investigated in the preparation without and with the addition of the following substances: 2 g/kg carrageen, 2.5 g/kg sodium tripolyphosphate (TPP) mixture and 80 g/kg polydextrose, and 3 g/kg enzymatic preparation (ACTIVA WM) containing microbial transglutaminase (MTG). Samples with the addition of MTG were pre-incubated at the temperature of 7 ± 1 °C for 1, 3, 5, 24 h. All samples were stored at the temperature of approx. −23 °C for 2, 30, 60, 90 days. The smallest change in protein solubility was observed in samples with added TPP and polydextrose. Along with the extension of pre-incubation time of samples containing the enzyme a gradual decrease was found in the amount of soluble protein. Also the results of the investigations obtained using the DSC technique showed the most advantageous protective effect, i.e., causing the smallest decrease in enthalpy values of samples during freezer storage, in case of the addition of TPP and polydextrose mixture. Analysis of thermal drip volume from gels showed that carrageen was the most advantageous addition to the myofibrillar preparation. Moreover, a gradual increase was observed in the volume of thermal drip along with the extension of pre-incubation time of the protein isolate with enzymatic preparation. Results of gel texture testing indicated that the most advantageous effect on gel quality was found for ACTIVA applied in 3 and 5 h pre-incubation with the myofibrils. Assuming that among the analyzed properties the most important were thermal drip and gel texture, 3 g/kg MTG at pre-incubation time of 3 h was considered the most advantageous additive.     

Transglutaminase effects on gelation capacity of thermally induced beef protein gels

Transglutaminase (TG) is an enzyme that catalyzes an acyl-transfer reaction between the γ-carboxyamide group of peptide or protein-bound glutaminyl residues, and primary amines. TG action on protein molecules, causes a cross-linking and polymerizing effect of these latter, through ε-(γ-glutamyl)lysine bonds. This TG-mediated protein cross-linking creates drastic physical changes in protein-rich foods.