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.     

Rheology and microstructure of κ-carrageenan under different conformations induced by several concentrations of potassium ion

Rheology, micro-DSC and confocal microscopy were used to study the effect of potassium ion on the viscoelastic behavior, disorder–order transition and microstructure, respectively, of κ-carrageenan in solution under different conformations at 60, 25 and 9 °C. At 60 and 25 °C the rheological behavior of 0.5% κ-carrageenan with 0–80 mmol/dm³ and 0–5 mmol/dm³ KCl, respectively, was typical of viscoelastic solutions of random coiled polymers. At 9 °C and below a critical ionic concentration of about 7.0 mmol/dm³, κ-carrageenan adopted an ordered conformation in which helical structures did not aggregate and hence did not form self-supporting gels. Changes in polysaccharide stiffness were estimated from intrinsic viscosity variations as a function of ionic content. In the ordered state, the stiffness was higher than in the disordered state, whereas a liquid-like viscoelastic behavior was still exhibited. In 0.5% κ-carrageenan at 25 °C, increasing KCl from 0 to 300 mmol/dm³ produced gels of increasing rigidity. However, above 100 mmol/dm³ such increase was marginal. Confocal images evidenced a three-dimensional network whose continuity depends on polysaccharide and salt concentrations. These observations are consistent with the rheological behavior of the self-supporting gels obtained with κ-carrageenan concentrations in the range of 0.05–1%.     

Acid induced gelation of soymilk,comparison between gels prepared with lactic acid bacteria and glucono-δ-lactone

The objective of this work was to compare the gelation of soymilk particles induced by the acidification of a commercial starter culture with that resulting by addition of glucono-δ-lactone (GDL). Structure formation was followed using rheology, and the microstructure was observed by confocal microscopy. Acidification of lactic acid bacteria resulted in a higher gelation pH (pH 6.29 ± 0.05) compared to that of a gel induced by GDL (pH 5.9 ± 0.04). This difference was attributed to the longer time available for rearrangements of the soymilk particles in soymilk with starter cultures compared to the fast acidification by GDL. In spite of the earlier gelation pH, there were no observed differences in the final gel stiffness measured at pH 5.1, the value of tan δ, the frequency dependence and the linear viscoelastic range of the gels measured at the final pH. Microstructural observations also showed a similar protein network structure.     

Rumen ciliated protozoa decrease generation time and adjust 18S ribosomal DNA copies to adapt to decreased transfer interval, starvation, and monensin

Defaunation studies have documented decreased ammonia concentrations associated with reduced microbial protein recycling and wastage of dietary protein, whereas many methods to suppress protozoa can reduce feed intake or depress ruminal organic matter or fiber digestibility. Therefore, more research is needed to optimize dietary conditions that improve protozoal growth and ruminal outflow relative to autolysis and recycling. Response in growth rate to ruminal outflow was simulated by abrupt changes in transfer interval of batch cultures, and substrate availability was evaluated by feeding without or with abrupt addition of monensin, which was postulated to inhibit digestive vacuole function. In experiment 1, Entodinium caudatum, a mix of Entodinium species, Epidinium caudatum, or Ophryoscolex caudatus cultures rapidly adjusted their generation times to approach respective changes in transfer interval from 3 to 2 or 1 d (cultures were always fed at 24-h intervals). Monensin (0.25 μM) consistently delayed this response. To evaluate a metabolic upshift associated with feeding or a downshift associated with substrate depletion, experiment 2 used real-time PCR to quantify protozoal 18S rRNA gene (rDNA) copies that were expressed relative to cell numbers or to the cellular constituents N and nucleic acids after feeding without or with monensin (0.5 μM). The 18S rDNA copies per milligram of nucleic acids were least for Ophryoscolex compared with the other cultures. When averaged over cultures (no culture × treatment interaction), 18S rDNA copies per unit of nucleic acids decreased at 16 h when cultures were starved but increased with feeding unless monensin uncoupled availability of consumed substrate. Rumen protozoal growth increased in response to decreased transfer interval in experiment 1. Substrate availability appeared to initiate metabolic responses preparing for cell growth, explaining how cultures could rapidly adjust to decreasing transfer interval in experiment 2. Because feeding was not coupled with transfer in experiment 2, however, a metabolic control probably arrested cell division to prevent overgrowth relative to substrate availability.     

The role of peroxidase on the antioxidant potential of fresh-cut ‘Piel de Sapo’ melon packaged under different modified atmospheres

The effects of different initial in-package O₂ and CO₂ concentrations (2.5 kPa O₂ + 7 kPa CO₂, 10 kPa O₂ + 7 kPa CO₂, 21 kPa O₂, 30 kPa O₂ and 70 kPa O₂) on peroxidase activity, vitamin C content, total phenolics and antioxidant capacity of fresh-cut ‘Piel de Sapo’ melon have been investigated for 14 days at 4 °C. The radical scavenging activity of fresh-cut melon strongly increased after 9 days storage related to a synthesis of phenolic compounds, especially under 2.5 kPa O₂ + 7 kPa CO₂ atmospheres. Low O₂ levels best maintained vitamin C and phenolic content during the storage. However, stressful too-low O₂ and high CO₂ levels induced an important increase of peroxidase activity under 2.5 kPa O₂ + 7 kPa CO₂ atmosphere, which was directly related to changes of vitamin C throughout storage. Therefore, 70 kPa O₂ atmospheres are proposed to prevent anaerobic conditions during storage of fresh-cut melon and thus, reduce wounding stress and deteriorative changes related to high peroxidase activity in tissue.     

Konjac flour improved textural and water retention properties of transglutaminase-mediated,heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation

Functional properties of heat-induced gels prepared from microbial transglutaminase (TG)-treated porcine myofibrillar protein (MP) containing sodium caseinate with or without konjac flour (KF) under various salt concentrations (0.1, 0.3 and 0.6 M NaCl) were evaluated. The mixed MP gels with KF exhibited improved cooking yields at all salt concentrations. TG treatment greatly enhanced gel strength and elasticity (storage modulus, G′) at 0.6 M NaCl, but not at lower salt concentrations. The combination of KF and TG improved the gel strength at 0.1 and 0.3 M NaCl and G′ at all salt concentrations, when compared with non-TG controls. Incubation of MP suspensions (sols) with TG promoted the disappearance of myosin heavy chain and the production of polymers. The TG-treated MP mixed gels had a compact structure, compared to those without TG, and the KF incorporation modified the gel matrix and increased its water-holding capacity. Results from differential scanning calorimetry suggested possible interactions of MP with KF, which may explain the changes in the microstructure of the heat-induced gels.     

Microstructure and rheology of phase-separated gels of gelatin + oxidized starch

We report on small-deformation rheology and confocal microscopy at 24 °C of high-sugar gel samples based on an aqueous mixture of gelatin + oxidized (non-gelling) starch exhibiting thermodynamic incompatibility. Using a standard protocol involving the heating of previously rapidly quenched samples at a fixed holding temperature (24–60 °C) for a fixed time (from 20 s to 30 min), gel samples of different storage modulus and degrees of spinodal-type phase separation were systematically generated. The developing time-dependent modulus of the gelatin gel was found to be sensitive to the extent of gelatin crosslinking as influenced by the nature of the thermal processing conditions. Under identical processing conditions, a gradual increase in starch content gave gels of lower elastic modulus and increased degree of microscopic phase separation. Taken all together, our results indicate that the gel rheology is determined by a subtle combination of overall system composition and temperature/time processing history. We conclude that the mechanical properties of this mixed biopolymer system are not directly deducible from the extent of phase separation observed microscopically without detailed additional information concerning sample preparation and treatment conditions.     

Rheological and sensory properties of fish gelatin gels as influenced by agar from Gracilaria tenuistipitata

Agar extracted from Gracilaria tenuistipitata and commercial agars were incorporated into fish gelatin at various levels (0, 5, 10, 15 and 20% gelatin substitution). G. tenuistipitata agar (GA) had lower failure stress (~16 kPa) than commercial agar (CA) (~20 kPa). However, the former showed higher failure strain (~30%) with lower melting temperature (65.9 °C). The critical linear stress and failure stress of agar/gelatin mixed gels increased with increasing agar levels (P < 0.05). At 15 and 20% of agar used, the mixed gels containing CA exhibited higher failure stress than those with added GA (P < 0.05). Two melting points of agar/gelatin mixed gels were observed, corresponding to the melting temperatures of gelatin and agar gels. Nevertheless, the incorporation of agar lowered the likeness score of gelatin gel. Thus, both GA and CA had the impact on rheological property and the selected sensory characteristics of fish gelatin, depending on the level of substitution.     

Cold storage conditions affect the persistence of diphenylamine, folpet and imazalil residues in ‘Pink Lady’ apples

‘Pink Lady^®’ apples (Malus domestica) fruit were harvested at commercial maturity treated with three different agrochemical products, and stored at 1 °C under either air or controlled atmosphere conditions (2.5 kPa O₂ + 3 kPa CO₂ and 1 kPa O₂ + 2 kPa CO₂) for 15 and 28 weeks. Diphenylamine, folpet and imazalil contents in both skin and flesh were simultaneously determined after cold storage plus a simulated marketing period of 1 or 7 days at 20 °C. Results showed that apples stored in 2.5 kPa O₂ + 3 kPa CO₂ retained higher contents of diphenylamine residues in comparison with those stored in 1 kPa O₂ + 2 kPa CO₂ or refrigerated air. Significant differences in imazalil skin contents were found throughout the simulated marketing period at 20 °C after storage for 28 weeks in controlled atmospheres.     

Short communication: Interrelationship between butyrate and glucose supply on butyrate and glucose oxidation by ruminal epithelial preparations

The aim of this study was to determine whether dietary Na-butyrate supplementation affects butyrate and glucose oxidation by ruminal epithelial preparations and whether this effect can be acutely modulated by substrate (glucose and butyrate) supply. Eighteen Suffolk wether lambs (6 lambs/treatment) were blocked by body weight and, within block, randomly assigned to the control treatment (CON) or to diets containing differing Na-butyrate inclusion rates (1.58 or 3.16%) equating to 1.25 (B1.25), and 2.50% (B2.50) butyrate on a dry matter basis, respectively. All lambs received their diet for a period of 14 d. After dietary adaptation, lambs were killed and the ruminal epithelium was harvested from the ventral sac, minced finely, and used for in vitro incubations. Incubation medium contained either a constant concentration of glucose (4 mM) with increasing butyrate concentrations (0, 5, 15, 25, or 40 mM) or a constant butyrate concentration (15 mM) with increasing glucose concentrations (0, 1, 2, 4, or 8 mM) to allow for the evaluation of whether acute changes in the concentration of metabolic substrates affect the oxidation of glucose and butyrate. We observed no interactions between the in vivo and in vitro treatments. Increasing dietary butyrate supplementation linearly decreased glucose oxidation by ruminal epithelial preparations, but had no effect on butyrate oxidation. Increasing butyrate concentration in vitro decreased (cubic effect) glucose oxidation when butyrate concentration ranged between 5 and 15 mM; however, glucose oxidation was increased with a butyrate concentration of 40 mM. Butyrate oxidation decreased (cubic effect) as glucose concentration increased from 1 to 4 mM; however, butyrate oxidation increased when glucose was included at 8 mM. The results of this study demonstrate that dietary butyrate supplementation can decrease glucose oxidation by the ruminal epithelium, but the relative supply of glucose and butyrate has a pronounced effect on substrate oxidation.     

Rheological and textural studies of fresh and freeze-thawed native sago starch–sugar gels. I. Optimisation using response surface methodology

A three-factor–three-level Box–Behnken design was adopted to study the simultaneous effects of two compositional variables (6–8% sago starch and 25–35% sugar) and one processing variable (shearing speed of mixer at 20–50 rpm) on textural and rheological properties of gels. Analysis of variance (ANOVA) was performed to evaluate the potential interactive and quadratic effects between these variables. Sago starch and sugar levels both increased gel stiffness and viscoelasticity. Shearing, on the other hand, reduced gel stiffness and viscoelasticity. Ridge analysis was performed to estimate the values of these variables which maximised and minimised the textural parameters of hardness, gumminess, resilience, cohesiveness, and springiness. Pearson correlations among various rheological and textural properties of gels were studied. The processing conditions that contributed to an optimum gel setting were found at sago starch of level of 7.69%, sugar of 30.29%, and shearing speed of 45.86 rpm.     

Effects of xylooligosaccharides and sugars on the functionality of porcine myofibrillar proteins during heating and frozen storage

The gel properties of mixed gels of salt-soluble proteins (SSP) and xylooligosaccharides (XOS) or other sugars were investigated. Furthermore, the water-holding capacity, synaeresis, and protein surface hydrophobicity of heated SSP/sugar mixed gels under frozen storage were evaluated. Addition of XOS and sugars lowered expressible moisture and thus elevated the water-holding capacity of mixed gels. The protein surface hydrophobicity (RSo) of heated (71.1 °C) XOS-added gels was lower than that of other treatments, indicating possible lower exposure of protein hydrophobic groups. Results from freeze/thaw stability and protein solubility showed a descending pattern of SSP/sugar mixed gels during frozen storage, with XOS-added gels being better in both test items than other treatments. Increasing saccharide levels improved freeze/thaw stability and protein solubility of frozen mixed gels. Addition of xylooligosaccharides resulted in the lowest RSo among treatments and appears to impact better cryoprotective function to meat proteins than other sugars.     

Surface enhanced Raman scattering (SERS) with biopolymer encapsulated silver nanosubstrates for rapid detection of foodborne pathogens

A biopolymer encapsulated with silver nanoparticles was prepared using silver nitrate, polyvinyl alcohol (PVA) solution, and trisodium citrate. It was deposited on a mica sheet to use as SERS substrate. Fresh cultures of Salmonella Typhimurium, Escherichia coli, Staphylococcus aureus and Listeria innocua were washed from chicken rinse and suspended in 10 ml of sterile deionized water. Approximately 5 μl of the bacterial suspensions was placed on the substrate individually and exposed to 785 nm HeNe laser excitation. SERS spectral data were recorded over the Raman shift between 400 and 1800 cm^− 1 from 15 different spots on the substrate for each sample; and three replicates were done on each bacteria type. Principal component analysis (PCA) model was developed to classify foodborne bacteria types. PC1 identified 96% of the variation among the given bacteria specimen, and PC2 identified 3%, resulted in a total of 99% classification accuracy. Soft Independent Modeling of Class Analogies (SIMCA) of validation set gave an overall correct classification of 97%. Comparison of the SERS spectra of different types of gram-negative and gram-positive bacteria indicated that all of them have similar cell walls and cell membrane structures. Conversely, major differences were noted around the nucleic acid and amino acid structure information between 1200 cm^− 1 and 1700 cm^− 1 and at the finger print region between 400 cm^− 1 and 700 cm^− 1. Silver biopolymer nanoparticle substrate could be a promising SERS tool for pathogen detection. Also this study indicates that SERS technology could be used for reliable and rapid detection and classification of food borne pathogens.     

UNIAXIAL COMPRESSION OF GELS MADE FROM PROTEIN AND K-CARRAGEENAN

Investigations of gels (18% total solids) made from pea protein isolates (PPI) or soy protein isolate (SPI) with differing amounts of _K-carrageenan added showed that the gel strength increased with the concentration of _K-carrageenan. When the concentration of_K-carrageenan exceeded 0.4%, gels made with PPI were stronger and more stiff than equivalent gels made with SPI. Addition of _K-carrageenan stabilized gels made with PPI towards variations in brittleness (indicated by strain at fracture) with pH. This was not the case when SPI was used. Preheating (75C, 2 min) suspensions containing protein isolates and _K-carrageenan before gel formation increased the strength and stiffness of the final gels, most pronounced when SPI was used. Addition of NaCl (0.5–2%) reduced strength and stiffness of gels, whereas CaCl₂ had no influence on gel properties. Mixtures of PPI and SPI proved to be weaker and more brittle than gels made from only SPI of PPI. Results indicate that using proteins of different origin can cause differences in gel structure.     

Synergistic action of transglutaminase and high pressure on chicken meat and egg gels in absence of phosphates

The effects of simultaneous application of microbial transglutaminase (MTGase) and high pressure (HP) (500, 700 and 900 MPa/40 °C/30 min), only pressure under the same conditions or heat (75 °C/30 min) were investigated on chicken batters with the addition of egg components and without phosphates. MTGase gels (700 and 900 MPa) showed marked increases in textural parameters compared to gels without enzyme (NE) or those obtained by heat. The addition of enzyme did not show differences between gels obtained at 700–900 MPa; however, gels obtained at 500 MPa were darker and more reddish than those obtained by heat. MTGase gels were more homogeneous and compact. Thermal analysis revealed that pressure levels above 700 MPa caused as much denaturing as did heat. The microstructure and texture of MTGase gels suggest that a higher amount and heterogeneity of crosslinks was produced when meat and egg proteins were treated in the presence of MTGase under specific conditions of pressure.     

Production of potentially probiotic beverages using single and mixed cereal substrates fermented with lactic acid bacteria cultures

In the present work, single and mixed cereal substrates were fermented with lactic acid bacteria to study and compare the effect of the media formulation on fermentation parameters. Three cereal flours namely malt, barley and barley mixed with malt (barley–malt) were selected and fermented with two probiotic strains: Lactobacillus plantarum (NCIMB 8826) and Lactobacillus acidophilus (NCIMB 8821). The effect of the single and mixed cereal flour suspensions on the fermentation of these two strains of lactic acid bacteria (LAB) was studied at an incubation temperature of 30 °C for 28 h. It was found that the LAB growth was enhanced in media containing malt and significant amounts of lactic acid were produced (0.5–3.5 g/L). A cell concentration between 7.9 and 8.5 Log₁₀ CFU/mL and a pH below 4.0 was achieved within 6 h of fermentation. Though the cell populations in the mixed culture fermentations of mixed substrates were similar to the ones obtained with single cereal flours, significant differences in the production of lactic acid were observed. These results suggest that the functional and organoleptic properties of these cereal-based probiotic drinks could be considerably modified through changes in the substrate or inocula composition.     

Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine

Binding properties are important for meat products and are substantially derived from the heat-induced gelation of myosin. We have shown that myosin is solubilized in a low ionic strength solution containing l-histidine. To clarify its processing characteristics, we investigated properties and structures of heat-induced gels of myosin solubilized in a low ionic strength solution containing l-histidine. Myosin in a low ionic strength solution formed transparent gels at 40-50 °C, while myosin in a high ionic strength solution formed opaque gels at 60-70 °C. The gel of myosin in a low ionic strength solution with l-histidine showed a fine network consisting of thin strands and its viscosity was lower than that of myosin in a high ionic strength solution at 40-50 °C. The rheological properties of heat-induced gels of myosin at low ionic strength are different from those at high ionic strength. This difference might be caused by structural changes in the rod region of myosin in a low ionic strength solution containing l-histidine.     

Isolation and viscometric characterization of hydrocolloids from mulberry (Morus alba L.) leaves

Hydrocolloid in mulberry leaves was extracted with water or sodium bicarbonate, and characterized rheologically in a highly dilute to a semi-dilute regime. Mulberry leaf hydrocolloid was composed of mainly carbohydrate with high levels of uronic acid. The hydrodynamic behavior of mulberry leaf hydrocolloid in deionized water demonstrated a typical polyelectrolyte behavior in the dilute domain, as indicated by a nonlinear Huggins' plot. Intrinsic viscosity value for alkaline-extracted (Alk) and water-extracted (Hw) hydrocolloid was around 7.25 dL/g and 3.61 dL/g, respectively. The specific viscosity versus concentration plot for both Alk and Hw exhibited a power-law dependence on concentration, with an onset of molecular entanglement occurring at a concentration of around 0.6 g/dL and 1.8 g/dL, respectively. Coil-overlap parameter for Alk and Hw was in the range of 4.35–6.61. The relative chain stiffness parameter (B) for Alk and Hw was in the range of 0.004–0.013, indicating a stiff backbone.     

Thermodynamic incompatibility between denatured whey protein and konjac glucomannan

The current study investigated the effect of a neutral polysaccharide, konjac glucomannan, on the heat-induced gelation of whey protein isolate (WPI) at pH 7. Oscillatory rheology (1 rad/s; 0.5% strain), differential scanning calorimetry and confocal laser scanning microscopy were used to investigate the effect of addition of konjac in the range 0-0.5% w/w, on the thermal gelation properties of WPI. The minimum gelling concentration for WPI samples was 11% w/w; the concentration was therefore held constant at this value. Gelation of WPI was induced by heating the samples from 20 to 80 °C, holding at 80 °C for 30 min, cooling to 20 °C, and holding at 20 °C for a further 30 min. On incorporation of increasing concentrations of konjac the gelation time decreased, while the storage modulus (G′) of the mixed gel systems increased to ∼1450 Pa for 11% w/w WPI containing 0.5% w/w konjac gels, compared to 15 Pa for 11% w/w WPI gels (no konjac). This increase in gel strength was attributed to segregative interactions between denatured whey proteins and konjac glucomannan.     

Influence of the process parameters and sugar granulometry on cocoa beverage powder steam agglomeration

The objective of this research was to evaluate the effects of the steam agglomeration process variables on the characteristics of cocoa beverage powders. A pilot scale agglomerator was used in the tests. For the cocoa beverage powder formulated with granulated sugar, most common commercial product, the increase in solids feed rate (400–700 g/min) led to a decrease in the mean particle diameter (400 g/min – 564.70 μm, 700 g/min – 438.40 μm) and an increase in the dryer rotation (12–52 rpm) led to an increase in the product moisture (12 rpm – 1.52% w.b., 52 rpm – 1.88% w.b.). The changing from 1.0 × 10² to 1.8 × 10² kPa of the vapor pressure resulted in an increase in moisture of the cocoa beverage powder (1.0 × 10² kPa – 1.46% w.b., 1.8 × 10² kPa – 1.94% w.b.) and the intensification of the yellow color of the product (1.0 × 10² kPa – 14.51, 1.8 × 10² kPa – 15.17).