Effect of sodium caseinate and κ-carrageenan on binding and textural properties of pork muscle gels enhanced by microbial transglutaminase addition

Response surface methodology was used to investigate the main effects and interactions of sodium caseinate (SC, 0–2%), microbial transglutaminase (MTG, 0–0.6%) and carrageenan (CGN, 0–0.8%) on water binding, textural and colour characteristics of pork gels. Higher κ-carrageenan and sodium caseinate content favored hydration properties and thermal stability, yielding lower cooking loss and higher water holding capacity. Their addition also increased hardness of pork gels, but was unable to improve springiness or cohesiveness. Sodium caseinate either alone or in combination with MTG generally has been found to be inferior to κ-carrageenan for functionality in comminuted meat systems. Although MTG had no effect on binding properties it was found to increase strength of the gels at higher SC levels. Addition of SC and ic-carrageenan significantly altered colour, while no significant influence of MTG on gel colour parameters was observed.     

Microbial transglutaminase and caseinate as cold set binders: Influence of meat species and chilling storage

The effect of microbial transglutaminase/sodium caseinate (MTG/C) systems on meat batter characteristics (water binding and textural properties of raw and cooked products) was studied in the presence of NaCl (1.5 g/100 g) and sodium tripolyphosphate (0.5 g/100 g), and storage time (96 h at 3 °C) for three meat species (pork, chicken, lamb). Samples prepared from pork and lamb with only MTG/C (no salts) had the highest cooking loss (CL) values, about 23 and 29 g/100 g, respectively; for chicken, the CL was less than 13 g/100 g. Hardness (Hd) and chewiness (Cw) generally tended to be higher in cooked samples containing MTG/C than in samples containing only salts. Products combining salts and MTG/C had higher (P<0.05) Hd and Cw. The efficiency of the MTG/C system as a texture conditioner of cooked products varied with the meat source.     

Lipid and protein structure analysis of frankfurters formulated with olive oil-in-water emulsion as animal fat replacer

Lipid and protein structural characteristics of frankfurter formulated with olive oil-in-water emulsion stabilized with soy protein isolate (SPI) as pork backfat replacer were investigated using Fourier transform infrared spectroscopy (FT-IR). Proximate composition and textural properties were also evaluated. Different frankfurters were reformulated: F/PF with pork backfat, F/SPI with oil-in-water emulsion stabilized with SPI and F/SPI + SC + MTG with emulsion stabilized with a combination of SPI, sodium caseinate (SC) and microbial transglutaminase (MTG). Replacement of pork backfat with these emulsions produced an increase (P < 0.05) of hardness, springiness, cohesiveness and chewiness but a reduction (P < 0.05) of adhesiveness. F/SPI and F/SPI + SC + MTG frankfurters showed the lowest (P < 0.05) half-bandwidth in the 2922 cm⁻¹ band, which could be related to lipid chains were more ordered than in F/PF. Modifications in the amide I band profile revealed a higher concentration of aggregated intermolecular β-sheets in F/SPI + SC + MTG samples. Lipid and protein structural characteristics could be associated with specific textural properties of healthier frankfurters.     

Olive oil-in-water emulsions stabilized with caseinate: Elucidation of protein–lipid interactions by infrared spectroscopy

This paper reports a FT-IR study for probing lipid and protein structural changes and their interactions in various oil-in-water emulsions. Two different emulsions were prepared using sodium caseinate, as stabilizer system, without and with microbial transglutaminase (MTG), denominated E/SC and E/SC + MTG respectively. Proximate composition, fat and water binding properties and textural characteristics were also evaluated in the emulsions. Penetration force and gel strength values were used to distinguish different (P < 0.05) textural behaviours depending on the formulation of emulsifying system. E/SC + MTG emulsion showed gel textural behaviour while E/SC lack of this property. The spectral results showed frequency upshifting of the amide I band in going from protein stabilizer systems isolate (the solution used as reference) to their corresponding emulsions, what is attributable to greater protein structural order upon emulsion formation. Enzymatic action of MTG in the sodium caseinate stabilizing system induces structural changes, in terms of lipid chain disorder or lipid–protein interactions and protein secondary modifications, which may reflect the formation of a gel structure in the emulsion. These results could help to choose the stabilizing system that is most suitable and effective for its use in the formulation of food products.     

Transglutaminase treatment of pea proteins: Effect on physicochemical and rheological properties of heat-induced protein gels

Rheological properties of heat-induced pea protein isolate (PPI) gels with added microbial transglutaminase (MTGase) were studied under various reaction conditions. A positive linear relationship was observed between level of MTGase used (0 to 0.7% w/w) and shear stress and shear strain of heat-set commercial pea protein isolate (PPIc) gels at 92 °C following incubation at 50 °C. Use of MTGase allowed for preparation of PPIc gels of similar strength and elasticity as commercial soy protein isolate gels and commercial meat bologna. MTGase treatment did not alter thermal properties of PPI gels. The shear stress and strain of PPIc gels were also improved following low temperature (4 °C) incubation of PPI with MTGase. Enhancement of shear strain or gel elasticity of heat-induced PPI gels with MTGase has not been reported before and provides opportunities for extending the properties of pea proteins when developing new food products.     

Raman spectroscopic study of the effects of microbial transglutaminase on heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristics

The effects of microbial transglutaminase (MTG) on heat-induced gelation of pork myofibrillar proteins (PMP) structural changes, textural properties were studied by Raman spectroscopy and texture profile analysis (TPA), respectively. And the relationships between the structural changes and textural characteristics were estimated by principal component analysis (PCA). Changes in the Raman spectra were interpreted as the occurrence of secondary structural changes in myofibrillar proteins with MTG added. Modifications in the amide I (1600-1700 cm^− 1) regions indicated a significant (p < 0.05) decrease in ??-helix content, accompanied by a significant (p < 0.05) increase in ??-sheets, ??-turns and random coil content due to the addition of the enzyme. Obvious texture property changes were also determined by TPA. All these changes showed a strong, irreversible heat-induced gel formed due to the addition of MTG. The application of a dimensionality reducing technique such as PCA proved to be useful to determine the most influential properties of heat-induced gel. Significant (p < 0.05) correlations were found between these structural changes and the textural characteristics (hardness) in PMP system with the addition of MTG by PCA. The hardness was related positively to fraction of ??-sheet, ??-turns and random coil, and negatively to normalized intensity of 760 cm^− 1 and fraction of ??-helix. The samples are closely grouped in a cluster defined by level of MTG.     

Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

Gelation properties of chicken myofibrillar protein isolate (MPI) and the effect of microbial transglutaminase (MTG) were studied using a dynamic oscillatory rheometer and a texture analyzer. Final heating temperature had a great impact on gel stiffness and the maximum gel stiffness was obtained at 95 °C. pH and ionic strength also influenced gel stiffness and the maximum gel stiffness was achieved at pH 6, 0.9 M NaCl; however, less stiff gels were formed in 0.6 and 1.2 M NaCl. In the MPI concentration range of ∼0.5-5%, a positive correlation was observed between gel stiffness or gel peak force and MPI concentration. When MTG was included at levels of ∼0 to 12-15 U, positive linear relations were found between gel stiffness or peak force and MTG levels. However, negative correlations for these parameters were observed at higher MTG concentrations. When MTG level was greater than 15 U, gel stiffness or peak force tended to decrease. The improvement in gel strength or gel peak force for the MPI with inclusion of MTG suggested that some ε (γ-glutamyl) lysine (G-L) crosslinking occurred among myofibrillar molecules. Thus, MTG is useful in improving gelation properties of heat-induced MPI gel and provides new opportunities to expand the utilization of low value meat in muscle foods.     

Infrared spectroscopic analysis of structural features and interactions in olive oil-in-water emulsions stabilized with soy protein

Lipid and protein structural characteristics of olive oil-in-water emulsions formulated with various stabilizer systems were investigated using Fourier transform infrared spectroscopy (FT-IR). Proximate composition, water binding and textural properties were also evaluated in these emulsions. Two different olive oil-in-water emulsions were studied: E/SPI prepared with soy protein isolate as a stabilizing system, and E/SPI + SC + MTG prepared with a combination of soy protein isolate, sodium caseinate and microbial transglutaminase as a stabilizing system. Results showed that textural properties (P < 0.05) were dependent on the stabilizing system. E/SPI + SC + MTG emulsion presented greater (P < 0.05) lipid chain disorder, more lipid-protein interactions, and more (P < 0.05) ??-helix and ??-sheet structures. A relationship between textural and structural properties was also observed as a function of the stabilizing system employed in the formulation of emulsions. A more thorough understanding of this connection could help improve the development of food products with appropriate physical properties.     

Evaluation of red bean protein [Vigna angularis] isolate on rheological properties of pork myofibrillar protein gels induced by microbial transglutaminase

The effects of 1% red bean protein isolate (RBPI) on the gel properties of myofibrillar protein (MP) in various levels of microbial transglutaminase (MTG: 0%, 0.1%, 0.5%, & 1%) were evaluated. The cooking yield (CY) of the MP gels decreased with increasing MTG level, while the addition of RBPI improved the CY of the MP gels. Gel strength (GS) was also improved when RBPI was incorporated into the MP gels containing higher than 0.5% of MTG. The addition of MTG and RBPI was slightly changed the endothermic peak temperatures. Scanning electron microscopy (SEM) showed that the three‐dimensional structure of MP with RBPI alone or in combined with MTG was compacted as compared to the control. Based on the results, RBPI could be functioned as a substrate for MTG (0.5–1.0%) and a water binder of meat protein gel mediated by MTG.     

Binding and textural properties of beef gels processed with κ-carrageenan, egg albumin and microbial transglutaminase

The combined influence of κ-carrageenan (κ-CGN, 0.5%) and egg albumin (EA, 2%) on quality characteristics of beef gels processed without or with 0.5% microbial transglutaminase (MTG) was investigated. Beef gel properties were determined by measuring textural, hydration and colour characteristics. κ-Carrageenan favourably affected hydration properties and thermal stability, yielding lower cooking loss, purge and expressible moisture. It also increased hardness and fracturability of beef gels, but was unable to improve springiness or cohesiveness. Egg albumin either alone or in combination with MTG generally has been found to be inferior to κ-carrageenan for functionality in comminuted meat systems. Addition of EA produced an increase in lightness and yellowness, and a decrease in redness of beef gels, while the presence of κ-carrageenan resulted in lower L(?) and b(?), and higher a(?) values. No significant influence of MTG on gel colour parameters was observed.     

Gelation properties of myofibrillar/pea protein mixtures induced by transglutaminase crosslinking

Gelation properties of mixtures of myofibrillar protein isolate (MPI)/pea protein isolate (PPI) were studied using a dynamic oscillatory rheometer and a texture analyzer to evaluate PPI as a possible meat product additive. The inclusion of microbial transglutaminase (MTG) increased the gel strength of MPI/PPI mixture (3% + 1%) more than it did for MPI (3%), but less than a 3% MPI, 1% soy protein isolate combination. The direct evidence of interaction between muscle and pea proteins in the form of new sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) bands was not found; however, the improvement in gel strength or gel peak force for the MPI/PPI mixture (3% + 1%) with inclusion of MTG suggested that some ? (γ-glutamyl) lysine (G-L) crosslinking occurred between muscle and pea proteins. It likely that pea protein acted as a non-gelling component and interspersed throughout the primary MPI gel network and the addition of MTG promoted partial crosslinking of MPI. Consequently, MTG is useful in improving gelation properties of heat-induced MPI/PPI gel.     

Gelation properties of salt-extracted pea protein isolate catalyzed by microbial transglutaminase cross-linking

Gelation is a fundamental functional characteristic of plant proteins. In this paper, a salt-extracted pea protein isolate (PPI) was mixed with microbial transglutaminase (MTG) to produce gels and the gelation properties were studied. When the MTG level increased, the magnitude of both the G′ and G″ moduli also increased, which means the gel strength increased. A second order polynomial equation was used to describe the relationships between the G′, G″ modulus and TG level. It was found that with increased heating and cooling rate at the same MTG level, G′ and G″ tended to decrease, resulting in a weaker gel. This was attributed to the rearrangement time of pea protein molecules; slower heating and cooling rates enabled protein molecules to have more time to rearrange and therefore form a stronger gel. At the same MTG level, higher pea protein concentration resulted in higher G′ and G″ values and a power law relationship was found between G′ and pea protein concentration or G″ and pea protein concentration. Frequency sweep data of PPI show that the MTG treatment resulted in higher G′ values and lower tan delta values, indicative of a stronger more elastic gel. The minimum gelation concentration was found to be 3% (w/v) with 10 U MTG treatment, lower than 5.5% required when no MTG was present. When compared to PPI and soy protein isolate (SPI) with and without 10 U MTG treatment, the gel strength of PPI with MTG was stronger than that of SPI with MTG treatment, whereas the opposite was true without the MTG treatment. SDS-PAGE showed that at the same pea protein concentration, higher MTG level induced more cross-linking as fainter bands were seen on the gel and there was a shift in the relative intensities of the bands in the molecular weight range of 35–100 kDa.     

The use of microbial transglutaminase and soy protein isolate to enhance retention of capsaicin in capsaicin-enriched layered noodles

Specialty layered noodles (LN) were prepared by sandwiching a capsaicin-enriched dough (CED) between two gastro-resistant dough layers made up of wheat flour, soy protein isolate (SPI) and microbial transglutaminase (MTG) at 0.5 (0.5MTG LN), 1.0 (1.0MTG LN) and 1.5 (1.5MYG LN) g/100 g of wheat-SPI flour. The textural, tensile and structural breakdown properties, capsaicin retention, microstructures and the sensory characteristics of cooked LN were evaluated. Compared to other LN, 1.5MTG LN exhibited the highest textural and tensile parameters, highest capsaicin retention, densest structure and was the most difficult to breakdown. The sensory quality of all LN was acceptable, even though it was the Control LN (prepared without SPI and MTG) that scored the highest acceptability. In general, increasing the level of MTG in the sandwiching dough layers of MTG LN reduced the release of capsaicin in simulated mouth, gastric and intestinal conditions, and these results could be due to increased protein cross-linking.     

Dependence of microbial transglutaminase on meat type in myofibrillar proteins cross-linking

The objectives of this study were to determine the factors that cause differences in the improvements of gel strength and ε(γ-glutamyl)lysine (G-L) content in chicken and beef (Japanese black cattle) myofibrillar proteins after adding microbial transglutaminase (MTG). As the amount of MTG added increased, the breaking strength increased progressively (p < 0.01) in chicken and beef samples, with the exception of chicken samples treated at 40 °C. The values of elasticity in the chicken samples were lower than those of the beef samples (p < 0.01). Surprisingly, the elasticity level, ε(γ-glutamyl)lysine contents and myosin heavy chain (MHC) band sizes of chicken and beef at all levels of MTG were significantly different (p < 0.01). The results of this study suggest that MTG activity was affected by MTG inhibitors; that MTG develops the texture of myofibrils differently in different species. However, the activity is limited and inconstant among meat proteins, as suggested by the data collected from the chicken samples. As a result, when the transferable amino acid residues are depleted (cross-linked) by MTG activity, the function of MTG will be insignificant. The correlation between MTG and different sources of meat protein is quite unstable but it is strong, which was observed when chicken and beef responded differently to MTG because their chemical and physiological properties were different. The remarkable rate of formation of cross-linked proteins and the discrepancy between the expected and observed amount of dipeptide raises the possibility that there are enzymes capable of reversing the reaction induced by transglutaminase in chicken and beef myofibrils. In summary, our results suggest that access of MTG to chicken and beef myofibrils is different because it depends on physiological (muscles and their fibre types), biological (substrates) and biochemical (inhibitors and amino acids) variables.     

牛血浆蛋白对猪肉盐溶蛋白质凝胶特性的影响

以牛血浆和猪后腿肉为原料,研究牛血浆蛋白对猪肉盐溶蛋白质加工特性的影响。结果表明：牛血浆具有改善猪肉盐溶蛋白质凝胶特性的作用,当pH6.5时,添加牛血浆蛋白0.9g/100mL时效果最佳;添加0.9g/100mL牛血浆蛋白的猪肉盐溶蛋白凝胶煮制损失、凝胶保水性、凝胶强度与添加0.125g/100mL微生物转谷氨酰胺酶(MTG)的凝胶相当。     

固定化酶改性酸法大豆浓缩蛋白在猪肉肠中应用的研究

利用固定化谷氨酰胺转氨酶(MTG)对酸法大豆浓缩蛋白(SPC)进行改性,并将改性SPC应用于猪肉肠.试验表明:改性后SPC的持水性和吸油性分别比未改性SPC提高了24.8%和64.5%;与大豆分离蛋白(SPI)相比,其凝胶性和吸油性分别高出58.3%和27.0%,持水性则降低8.0%.改性后的SPC用于猪肉肠中,当添加量为6%时,猪肉肠的咀嚼性比未改性SPC和SPI分别提高了418.6%和187.1%;得率比未改性SPC和SPI分别提高了18.9%和4.8%,感官评分结果也与其相一致.     

Response surface methodology study on the effects of salt,microbial transglutaminase and heating temperature on pork batter gel properties

Response surface methodology was used to investigate the main effects and interactions of sodium chloride (0–2%), microbial transglutaminase preparate (MTG, 0–0.6%) and heating temperature (HT, 70–100°C) on water binding, textural and colour characteristics of pork batter gels cooked to an internal temperature of 70 °C. Lower salt gels showed decreases in hardness, chewiness and elastic properties, as well as significant reduction in the cooking yield and increase of expressible moisture. Salt levels also affected gel colour parameters, with Hunterlab a* and b* values being inversely correlated with salt concentration. MTG addition favourably reduced the cooking loss and increased hardness and chewiness of gels, but was not able to improve these parameters in low-salt products to the same levels as the high-salt products. Heating temperature was found to have relatively minor effect, primarily through its interaction with salt level and in a quadratic term affecting the elasticity and springiness of the gels.     

Impact of microbial transglutaminase on gelling properties of Indian mackerel fish protein isolates

Impacts of microbial transglutaminase (MTGase) (0–0.6 units/g sample) on gel properties of Indian mackerel unwashed mince, surimi and protein isolates with and without prewashing were studied. Generally, lower myoglobin and lipid contents were found in protein isolate with and without prewashing, compared to those of unwashed mince and surimi (P < 0.05). Protein isolate had the decreased Ca²⁺-ATPase and protein solubility, indicating protein denaturation. When MTGase was incorporated, breaking force and deformation of all gels markedly increased, especially as MTGase levels increased (P < 0.05). At the same MTGase level, gel from protein isolate with prewashing exhibited the highest breaking force and deformation (P < 0.05). The addition of MTGase could lower the expressible moisture content of most gels. No change in whiteness of gel was observed with the addition of MTGase (P > 0.05), but gel from protein isolate gels had decreased whiteness as MTGase at high level was added. The microstructure of protein isolate gels without prewashing showed a similar network to unwashed mince gels, whilst a similar network was observed between surimi gel and gel from protein isolate with prewashing. Nevertheless, a larger void was noticeable in gels from protein isolates. All gels incorporated with MTGase (0.6 units/g) showed a slightly denser network than those without MTGase. Thus, gel with improved properties could be obtained from protein isolate from Indian mackerel with added MTGase.     

Effect of microbial transglutaminase on NMR relaxometry and microstructure of pork myofibrillar protein gel

The effect of microbial transglutaminase (MTG) on nuclear magnetic resonance relaxation (NMR) behaviour, water holding capacity (WHC) and microstructure of pork myofibrillar protein (PMP) gel was studied. The enzymatic protein preparation had significantly lower values of spin–spin relaxation time (T ₂), higher WHC and more porous microstructure in comparison with the control system. T ₂ was reduced from 226 ms (peak value) of the PMP gel containing no MTG to 188 ms of the PMP gel containing 2 U/g protein. However, no further decrease was shown when the concentration of MTG increased. The reduction was attributed to reduced mobility of water protons in the system. Scanning electron micrographs (SEM) showed the mobility of water in the proteins gel network was related to gel microstructure.     

Effects of transglutaminase, tyrosinase and freeze-dried apple pomace powder on gel forming and structure of pork meat

Effects of microbial transglutaminase (mTG), mushroom tyrosinase and an apple powder containing transglutaminase (TG) and polyphenol oxidase (PPO) on the structure of industrial pork meat homogenate were studied. Apple powder and mTG both increased the value of storage modulus (G′). Mushroom tyrosinase was not able to affect gel forming with the used dosages and treatment conditions. All the enzymes studied were able to improve gel hardness of unheated meat homogenate at 4 °C to a certain extent. In gel hardness measurements added cysteine affected positively on the apple powder—treated pork meat and negatively on mTG—and tyrosinase-treated meat. Surprisingly cysteine addition nullified also the action of mTG. Hence powdered apple pulp, a recovered co-product of an industrial process, may contain suitable enzyme activities for food protein stabilization.