Salt-soluble Meat Proteins Research Articles

Aggregation behavior of solubilized meat - Potato protein mixtures

Knowledge on the mixing behavior of meat and plant proteins is of importance for the manufacture of so-called hybrid products, a product category that is becoming of interest to food manufacturers. The aim of this study was to assess the pH-dependent miscibility and aggregation behavior in combinations of solubilized pork meat and potato tuber proteins. Analysis on their individual pH-dependent surface charge and size were followed by a visual and microscopic evaluation of their mixtures. Image analysis was used to obtain separation indices, aggregate areas, and aggregate aspect ratios and FTIR spectra were recorded to obtain insights into secondary structural elements. Net zero charge transition points differed, with a higher value for potato (pH 6.8) compared to meat proteins (pH 5.7). In mixtures, homogeneous solutions (pH 5.8 and 7.0) abruptly changed to phase-separated ones at low (pH 3) to medium (pH 5.5) pH. Here, anisotropic, clustered aggregates at high meat protein contents were exchanged for smaller, irregularly-shaped and sized microstructures at low ones and image analysis suggested a perturbing effect of potato on meat proteins to associate and form fibrous aggregates. The isoelectric point of salt-soluble meat proteins (pH ~ 5.5) was described as defining boundary value for co-solubility or interaction in between individual meat and meat and potato proteins. FTIR results confirmed alterations as a function of mixing ratio and pH. Results indicate that significant textural changes can be expected to occur in hybrid matrices, with plant proteins impeding the structural-self-association of meat proteins.

Effects of basic amino acid on the tenderness, water binding capacity and texture of cooked marinated chicken breast

This work investigated the effects of basic amino acids such as l-arginine (Arg)/l-lysine (Lys) on the physicochemical properties of cooked marinated chicken breast (CMCB) as well as the possible mechanism underlying these effects. The results indicated that shearing force decreased from 13.3 N to 10.0 N and cooking loss decreased from 38.3 g/100 g–26 g/100 g when Lys increased from 0 g/100 g–0.4 g/100 g, while shearing force decreased to 8.8 N and cooking loss decreased to 28 g/100 g at 0.4 g Arg/100 g. Furthermore, Arg/Lys improved the textural parameters and increased pH value. Low field-nuclear magnetic resonance showed that Arg shortened the relaxation times of T21 from 50 ms to 38 ms and Arg/Lys increased the peak area percentage (P21) for T21 from 93.6 to 97. Arg/Lys promoted the extraction of salt-soluble meat proteins from 54 mg/g to 78.6 mg/g. Scanning electron microscopy illustrated that Arg and Lys narrowed the gaps between muscle fibers at 0.6 g/100 g and at 0.4 g/100 g, respectively. The results disclosed that Arg/Lys could improve the physicochemical properties of CMCB, and thus showing a potential for the manufacture of cooked marinated meat products.

L–Arginine/l–lysine improves emulsion stability of chicken sausage by increasing electrostatic repulsion of emulsion droplet and decreasing the interfacial tension of soybean oil-water

The effects of l–arginine (Arg) and l–lysine (Lys) on the emulsifying properties of the salt-soluble meat proteins (SSMPs)–soybean oil emulsion (SSOE) and soybean oil–water emulsion (SWE) were evaluated to ascertain their roles in improving the emulsion stability of sausage. The results indicated that Arg/Lys addition or increasing pH increased the emulsifying activity/stability index and the absolute ζ–potential of emulsion droplets but decreased the creaming index, apparent viscosity, and mean particle size of SSOE. Amino acid analysis showed that Arg/Lys accumulated at the interface of the emulsion droplets. Arg/Lys also decreased the surface tension of SWE at 0.002% but increased the stability of SWE at 0.1%–0.3%. In summary, Arg/Lys improved the stability of emulsified sausage by increasing the electrostatic repulsion of emulsion droplets and decreasing the interfacial tension of soybean oil-water.

Effects of nanofiber cellulose on functional properties of heat-induced chicken salt-soluble meat protein gel enhanced with microbial transglutaminase

The effects of carboxylated nanofiber cellulose (cNFC) on chicken breast muscle salt-soluble protein (SSP) in model systems in the presence or absence of transglutaminase (TG) were investigated. cNFC at concentrations of 0%, 2.5%, 5%, 7.5%, and 10% was introduced into salt-soluble protein. The results indicated that cNFC contributed to the improvement of water-holding capacity of gels, but this effect was insignificant when TG was added into the composite gel. This was attributed to steric hindrances of the pre-formed TG cross-linked network. The presence of cNFC enhanced gel strength in the model system with TG. Based on scanning electron micrographs (SEM) and confocal laser scanning micrographs (CLSM), the addition of cNFC to SSP produced a hydrogel in the form of a semi-IPN (Interpenetrating Polymer Network). In the presence of TG, this structure was more compact. No strong intermolecular interaction between SSP and nanocellulose was evident from FTIR spectra, suggesting the occurrence of physical entanglement of cNFC in the composite gel. In summary, the presence of cNFC can improve gel properties of salt-soluble protein, depending on its concentration and the gel structure, thereby providing potential applications in restructured meat products.

Applications of high pressure to pre-rigor rabbit muscles affect the functional properties associated with heat-induced gelation

High pressure (HP) was applied to pre-rigor rabbit muscles (PRRMs) for the manufacture of value-added gel-type products. A 2×3 factorial design was adopted for HP-treatment (100, 200 and 300MPa for 15 or 180s) to PRRMs. The HP-treated meat was used for gel preparation and determination of water mobility properties and textural profiles. Salt-soluble meat proteins (SSMP) were then extracted from meat for estimating the tertiary conformational changes (hydrophobic and sulfhydryl groups). The water-holding capacity of treated samples increased significantly (P<0.05) except for those treated at 300–180 (MPa-s). The hardness, cohesiveness and chewiness were significantly improved (P<0.05) by moderate HP-treatments (100–200MPa for 15 or 180s). HP-induced the de-polymerization of some protein components, together with unfolding and refolding of protein tertiary conformations, partly explaining the observed functionality changes. In conclusion, application of moderate HP to PRRM modified the protein conformation in a manner that improved the functional properties of gels.

Interaction between carrageenan/soy protein isolates and salt-soluble meat protein

The effects of combined κ-carrageenan (CAR) and soy protein isolate (SPI) on gel strength, water loss, the rheological properties, particle size, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and Raman spectroscopy of salt soluble meat protein were evaluated. Combination of CAR/SPI increased gel strength and water retention of SSMP (salt-soluble meat protein), suggesting that molecular interaction may have occurred. However, no indications of specific molecular interactions were observed upon addition of stabilizing/destabilizing reagents. The results showed that hydrophobic force affected the water retention of salt soluble protein gel, and hydrogen bond significantly affected the formation of gel. The analysis of the Raman spectra showed that adding of combined CAR/SPI in SSMP decreased the content of α-helix and increased the content of β-sheet. SDS-PAGE did not show significant interactions between SSMP and CAR/SPI indicating that the property improvement of combined SSMP/SPI/CAR gel was not related to chemical reaction. Instead, physical rearrangement process and electrostatic attraction resulted from SPI, CAR and SSMP molecule could contribute to the gel quality improvement.

Effects of l-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

The paper focused on the effects of l-Arginine (l-Arg) on the water holding capacity (WHC) and texture of salt-soluble meat proteins (SSMP) gel and the thermal gelling mechanism were investigated. The addition of 0–0.25 g l-Arg/100 g increased the WHC, hardness, springiness cohesiveness and chewiness of SSMP gel. Rheology indicated the addition of l-Arg increased storage modulus (G′), but decreased phase angle (tan δ). Differential scanning calorimeter (DSC) disclosed that l-Arg-treatment caused the disappearance of the first and third transition peaks, but the increase of the enthalpy of the second denaturation (ΔH2). Low field nuclear magnetic resonance (LF-NMR) showed l-Arg at 0.25 g/100 g increased the fraction of spin–spin relaxation times distribution for immobile water (T21). Scanning electron microscopy (SEM) revealed that l-Arg promoted to form a dense, uniform SSMP gel. The results suggested that the thermal stability and gelation of SSMP were affected by l-Arg, which changed the microstructure of SSMP gel, and ultimately improving the corresponding WHC and texture, as well as changing the distribution of T2.

Effects of gamma irradiation on physicochemical properties of heat-induced gel prepared with chicken salt-soluble proteins

The technological effects of gamma irradiation (0, 3, 7, and 10kGy) on chicken salt-soluble meat proteins in a model system were investigated. There were no significant differences in protein, fat, and ash content, and sarcoplasmic protein solubility among all samples. The samples with increasing gamma irradiation levels had higher pH, lightness, yellowness, and apparent viscosity, whereas moisture content, water holding capacity, redness, myofibrillar protein solubility, total protein solubility, hardness, springiness, cohesiveness, gumminess, and chewiness were the highest in the unirradiated control. The result from meat products using gamma irradiation was intended to provide a basic resource processing technology.

Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl2 and κ-carrageenan

The effects of high pressure processing (HPP) on the water-binding capacity and texture profile (TPA) of salt-soluble meat protein (SSMP) containing 0.2% CaCl2 and 0.6% κ-carrageenan (SSMP-CK) gels were investigated. The results showed that 300–400MPa improved water-binding capacity and decreased TPA parameters of SSMP-CK gels (P<0.05), while 100MPa could increase hardness and chewiness of the gels. The thermal transition temperature peak for the myosin head (Tpeak1) of SSMP disappeared on addition of CaCl2 and κ-carrageenan. 300MPa produced a new peak, and caused a shift of the NH-stretching left peak and amide I and the disappearance of NH-stretching right peak. The destruction of network structure and the weakening of molecular interaction within the pressurized gels could result in the decrease of TPA parameters. Thus gelling properties could be modified by HPP, κ-carrageenan and Ca2+. It is of interest to develop low-fat and sodium-reduced meat products.

Interactions between Chicken Salt-soluble Meat Proteins and Makgeolli Lees Fiber in Heat-induced Gels

The technological effects of Makgeolli lees fiber (0, 0.5, 1.0, 2.0, and 4.0%) on chicken salt-soluble breast meat proteins in a model system on proximate composition, physicochemical properties, and textural properties were investigated. Makgeolli lees fiber was obtained from Makgeolli brew processing, and the by-products showed good dietary fiber. The moisture and ash contents, water holding capacity, redness, yellowness, hardness, and apparent viscosity of chicken salt-soluble meat protein heat-induced gel systems with Makgeolli lees fiber were all higher than the control without Makgeolli lees fiber. However, protein solubility and electrophoretic patterns did not differ among the control and treatments with Makgeolli lees fiber samples. The chicken salt-soluble protein heat-induced gel systems incorporating Makgeolli lees fiber had improved water holding capacity, textural properties, and viscosity due to Makgeolli lees fiber addition. These results suggest that the addition of 4.0% Makgeolli lees fiber to gel is helpful to improve the physical properties of heat-induced gels.

Effects of high pressure and CaCl2 on properties of salt-soluble meat protein gels containing locust bean gum

Abstract The effects of high pressure processing (HPP) (0–400 MPa) and CaCl2 (0–0.8%) on cooking loss (CL), water holding capacity (WHC) and textual properties of salt-soluble meat protein (SSMP) gels with the addition of 3% sodium-salt and 0.2% locust bean gum (LBG) (SSMP-SL) were investigated. Results showed that 100–200 MPa could significantly increase WHC of SSMP-SL gels, while 300–400 MPa could decrease CL, hardness and chewiness of that (P Industrial relevance To develop low-fat and sodium-reduced meat products, the application of HPP and the addition of CaCl2 (0–0.8%) might be of great interest for industrial manufacture and can yield the products bearing high water binding capacity and good textural properties.

Effects of rice bran fiber on heat-induced gel prepared with pork salt-soluble meat proteins in model system

The technological effects of rice bran fiber on pork salt-soluble meat proteins in a model system were investigated. Rice bran fiber at levels of 0% (control), 0.1%, 0.5%, 1%, and 2% was added at the same time as salt-soluble meat protein to maintain similar moisture levels in all samples. Samples with increasing amounts of added rice bran fiber had higher pH, yellowness, sarcoplasmic and total protein solubilities. The moisture content, myofibrillar protein solubility and water holding capacity were the highest in the treatments containing with 1% rice bran fiber. However, the lightness and redness, textural properties decreased with increasing rice bran fiber levels. SDS gel electrophoresis did not reveal any changes in proteins regardless different rice bran fiber levels. The apparent viscosity indicated that improvements in water holding capacity and decreased texture due to added rice bran fiber.

Phase behaviour, rheology and microstructure of mixture of meat proteins and kappa and iota carrageenans

The phase behaviour of mixtures of salt soluble meat proteins, kappa (κ) and iota ( ι) carrageenan in non-gelling conditions (45 °C) were determined at pH 5.6, 6.2 and 7.1. The concentration of meat proteins ranged from 0.1 to 1.0 percent and that of κ-carrageenan and ι-carrageenan from 0.02 to 0.3 percent in the mixtures. Mixtures separated under gravity to form soluble/liquid and gelled/complex phases. For meat proteins- κ-carrageenan mixtures, phase separations at all meat protein/carrageenan ratios were observed. For meat protein- ι-carrageenan mixtures, soluble complexes were formed at low meat protein to ι-carrageenan ratios and gels at higher ratios. The yield of the complex/gels increased with the increase in the concentration of the meat proteins and carrageenans and decreased with increase in the pH of the initial mix. The complex/gels formed became stronger with the increase in carrageenan in the mix and with κ-carrageenan compared to ι-carrageenan. Chemical analyses and scanning electron and phase contrast microscopy indicated that in phase separated mixtures, the bulk of the meat proteins and carrageenan were found in the gel compared to the liquid phase; and that meat protein interacted with carrageenan in the gel and formed soluble complexes with carrageenan in the liquid phase. SDS-PAGE showed that the meat proteins that interacted to form the complex/gels with carrageenan included myosin heavy chain, α-actinin, actin, myosin light chains and proteins with molecular weights around 150 and 50 kD. The outcomes of the present study could be used in the formulation of multi-component foods with a range of consistencies containing meat proteins.

Effects of chitosan on the gel properties of salt-soluble meat proteins from silver carp

Chitosans (CHI) with different degree of deacetylation (DD) (60.5%, 65.4%, 70.8%, 77.3%, 86.1%) and different molecular weight (MW) (299, 410, 600, 706, 880 kDa) were obtained. Heat-induced composite gels were prepared from 4% salt-soluble meat proteins (SSMP) with chitosans at 0.6 mol/L NaCl, pH 7.0. Penetration forces and storage modulus of SSMP–CHI composite gels increased proportionally with increasing amount of molecular weight. Gel containing chitosan with DD 77.3% exhibited the highest penetration force and storage modulus. The SEM observations showed that SSMP–CHI incorporated gels were compact and fine compared with that of SSMP. Chemical forces involved in SSMP–CHI composite gels were investigated by determining the effects of NaCl, urea, propylene glycol, and 2-MeSH on penetration forces. Results of these studies demonstrated that interaction between CHI and SSMP contributed to the enhancement of texture of the SSMP–CHI composite gels by electrostatic interactions and hydrogen bonds.

Interaction between flaxseed gum and meat protein

Thermal properties, dynamic rheological properties, texture and microstructure of salt-soluble meat protein and flaxseed gum (SSMP-FG) mixtures were investigated. Two transitions, 57.0 °C ( T SSMP1) and 63.2 °C ( T SSMP2), were observed for SSMP without FG with differential scanning calorimetry (DSC). Addition of 2% FG to SSMP increased T SSMP1 and T SSMP2 by 1.9 °C and 5.9 °C, respectively. Two transitions, 53 °C ( T SSMP1′) and 75 °C ( T SSMP2′), were also observed for SSMP without FG with dynamic rheological measurement. Addition of 2% FG to SSMP increased T SSMP1 ′ and T SSMP2 ′ by 9 °C and 14 °C. These results indicated that addition of FG increased thermal stability of SSMP. Addition of FG also increased the storage modulus G′, gel strength, decreased syneresis, and changed the microstructure of SSMP gels with texture analyser and scanning electron microscope (SEM), respectively, suggesting that an interaction between FG and SSMP may have occurred. The results of addition of destabilizer to SSMP gels indicated that electrostatic forces seemed to be the main force involved in the formation and stability of protein–polysaccharide gel.

Influence of κ-carrageenan on the thermal gelation of salt-soluble meat proteins

Cooked ham-based model systems were prepared using salt-soluble meat protein isolate, κ-carrageenan and sodium and potassium chloride. The pH was set to 6.2 using a 50 mM PIPES-buffer. An experimental mixture design was used to study the effect of carrageenan on the structure build-up of the gelled meat products. In situ gelation experiments were carried out on a controlled-stress rheometer, while a texture analyzer was used to determine the large deformation behaviour. The water holding capacity was measured by a centrifugal technique and confocal scanning laser microscopy was used to visualize the microstructure of the gelled meat products. κ-Carrageenan was found to increase the complex modulus, the gel strength and the water holding capacity, although these properties were mainly governed by the concentration of meat protein isolate.

Functional properties of soy protein hydrolysates obtained by selective proteolysis

Soy protein hydrolysates were produced from a soy protein isolate (SPI) in which either the glycinin or β-conglycinin fractions had been selectively hydrolysed. The solubility, apparent viscosity, emulsifying activity, whippability and gel-forming ability of each hydrolysate were determined. Both hydrolysates had minimum solubility at around the same level of pH 4.5 as that of SPI. The reduced-β-conglycinin hydrolysate (RCH) showed lower apparent viscosity than the reduced-glycinin hydrolysate (RGH). Increased whippability was observed with both hydrolysates in comparison with SPI, whereas lower emulsifying activity was found, except at acidic pH 4. RCH retained more gel-forming ability than RGH when determined by mixing with salt-soluble meat protein. This result was supported by observation of the microstructure of the gels.

Protein interactions in comminuted meat gels containing emulsified corn oil

Model comminuted meat gels incorporating corn oil droplets, emulsified either with salt-soluble meat proteins (SSMP) or with soy protein isolate (SPI), were prepared by heat treatment of meat paste at 90 °C, and their strength was evaluated by applying a uniaxial compression test. The presence of emulsified oil droplets resulted in a significant reduction of the gel network strength, the extent of decrease being independent of the type of protein emulsifier used. Gels prepared with SSMP, on the other hand, suffered a less pronounced structure disruption by oil droplet incorporation and the extent of disruption depended on the type of protein used for oil emulsification. Competitive adsorption studies in emulsions between SSMP and SPI indicated that the former may partly displace the latter from oil droplet surface, thus, offering binding sites to which the SSMP molecules of the gel network may become attached during the development of system structure.

Gelation properties of salt soluble meat protein and soluble wheat protein mixtures

Salt soluble meat proteins (SSMP) and commercially available soluble wheat proteins (SWP) were characterised by SDS-polyacrylamide gel electrophoresis, differential scanning calorimetry (DSC) and small and large deformation testing. DSC scans indicated transitions similar to those of native actomyosin for the salt soluble meat extract whereas SWP did not indicate any transitions between 20 and 120 °C. Small deformation tests on SWP indicated a G′/ G″ crossover gelation temperature of 90 °C and weak gels as judged by frequency sweeps. In contrast, SSMP gelled at 40 °C and formed strong gels on heating to 90 °C. However, on autoclaving at 120 °C, 20% SWP in distilled water produced strong elastic gels with little syneresis, compared with the more brittle gels produced with 20% (w/w) SSMP as indicated by large deformation testing. Mixtures of the two proteins in the ratio SSMP/SWP (15:5) gave strong elastic gels similar to the SWP gels. Even the presence of very small amounts of SWP in the mixture, e.g. SSMP/SWP 20:1 trebled the elastic modulus compared with a SSMP gel and reduced syneresis. This was probably due to the close association of SWP with actomyosin strands as viewed by transmission electron microscopy. However, increased levels of SWP in the mixture, for example SSMP/SWP 10:10 ratio, resulted in the separation of the two protein phases as shown by phase contrast microscopy, and consequently led to lower G′ values in the mixed gels. The addition of 20 mM chloride salts showed that potassium reduced the shear modulus, sodium had no effect and calcium enhanced the shear modulus for SWP gels formed at 120 °C. In contrast, SSMP gels were stronger in the presence of potassium, followed by sodium and calcium.

Carrageenan Effects on Salt‐Soluble Meat Proteins in Model Systems

ABSTRACTThe effects of κ‐, ι‐, and λ‐carrageenans (CGNs) on the rheological properties, water loss, and ultrastructure of salt‐soluble meat protein (SSMP) gels were evaluated. κ‐CGN increased gel strength and water retention of SSMP, suggesting that a molecular interaction may have occurred. However, no indications of specific molecular interactions were observed upon addition of stabilizing/destabilizing reagents. Electron microscopy indicated that improvement of water retention and texture of SSMP/κ‐CGN gels may be due to physical rearrangement of the κ‐CGN and SSMP molecules.