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.     

Formulation and Copping Temperature Effects on Beef Frankfurters

Frankfurters were manufactured using four fat and added water (AW) formulations (10% fat/30% AW; 15%/25%; 20%/20%; 30%/10%) and processed at chopping temperatures 9, 12, or 15°C. The batters were stuffed into cellulose casings, thermally processed, chilled and vacuum-packaged. Frankfurters were analyzed for proximate composition, textural properties and purge. No differences occurred among treatments for processing yield (89.8%± 1.83). Frankfurters chopped to 12°C had the highest (P < 0.05) Kramer peak force values. As expected, purge increased in all treatments as storage time increased (P < 0.05). As AW increased, hardness and cohesiveness decreased and purge increased. Water level and fat reduction were the most critical factors affecting quality.     

Effects of High Pressure and Heat Treatments on Physicochemical and Gelation Properties of Rapeseed Protein Isolate

High pressure (HP, 200, 400, and 600 MPa)- and heat (60, 80, and 100 °C)-induced gelation, aggregation, and structural conformations of rapeseed protein isolate (RPI) were characterized using gel permeation–size-exclusion chromatography, differential scanning calorimetry, and circular dichroism (CD) techniques. HP treatments significantly (p?<?0.05) increased the content of soluble protein aggregates and surface hydrophobicity of RPI. In contrast, heat treatments at 80 and 100 °C led to significant (p?<?0.05) decreases in the amount of soluble protein aggregates. At pressure treatment of 200 MPa, there was a significant (p?<?0.05) increase in free sulfhydryl group content of RPI, whereas 400- and 600-MPa treatments as well as temperature treatments (60–100 °C) caused significant decreases. Protein denaturation temperature was increased by about 6 °C by HP and heat treatments. The far-UV CD spectra revealed increases in α-helix content of RPI after HP treatments with 400 MPa producing the most increase. Near-UV data showed that HP and heat treatments of RPI led to increasing interactions among the aromatic amino acids (evidence of protein aggregation), and between aromatic amino acids and the hydrophilic environment, which indicates protein unfolding. Least gelation concentration of RPI was significantly (p?<?0.05) reduced by HP and heat treatments, but HP-treated RPI produced gels with better textural properties (hardness increased from ~7.7 to 81.1 N, while springiness increased from ~0.37 to 0.99). Overall, pressure treatments (200–600 MPa) were better than heat treatments (60–100 °C) to modify the structure and improve gelation properties of RPI.     

Physicochemical characterization and stability of inulin gels

The ability of three commercial inulins (Raftilose ^®P95, Frutafit IQ^®, and Frutafit TEX^®) with different chemical composition (oligo-polysaccharides profile) to form gels (at 25 and 50 °C) was evaluated. Raftilose^®P95 (rich in mono-disaccharides) did not form gels, Frutafit IQ^® (mainly oligosaccharides) gelatinized in the 30–60% w/w concentration range and Frutafit TEX^® (mainly long-chain saccharides) in the 20–40% w/w range. Textural and thermal properties of the gels were studied and their stability was evaluated during storage at 4 °C. Frutafit TEX^® gels (both fresh and during storage) were harder, more adhesive, and less cohesive than Frutafit IQ^® gels (40% w/w). At 40% w/w, Frutafit TEX^® gels had a significantly higher amount of freezable water than Frutafit IQ^®, and the DSC thermogram line shapes indicated that ice melting was more uniform and occurred at higher temperatures in Frutafit TEX^® than in the Frutafit IQ^® gels. Ice melting profile was not significantly affected by both gelification temperature and storage time. Frutafit IQ^® gels were more stable than Frutafit TEX^® gels during storage.     

High pressure-induced tapioca starch gels: physico-chemical characterization and stability

Gelatinization of tapioca starch (25% dry basis) was induced by high hydrostatic pressure processing (HPP) at 600 MPa under different time and temperature regimes (30 °C for 10, 20 and 30 min; 50 °C for 10 min; 80 °C for 10 min). Textural, thermal and structural properties of the gels were studied and their stability was evaluated after 28 days of refrigerated (4 °C) and frozen (−18 °C) storage. Thermally induced gels (90 ± 1 °C, 20 min, gel-T) were used as controls. HPP resulted in the formation of harder gels than thermal processing (more significantly at lower processing temperatures) partially preserving the granular structure of the native starch. Longer HPP treatments caused only a slight decrease in hardness that was significant only at longer processing times (30 min). DSC thermograms of high pressure-induced samples showed a more asymmetrical ice-melting peak than that of thermally induced gels. Asymmetry of the peak of HP treated samples was more pronounced in samples processed at lower than at higher temperature. A different starch–water and/or starch/starch interaction may be hypothesized. During storage, all samples became stiffer and the amylopectin recrystallization increased, more extensively in thermally induced than in HPP samples where a stronger starch–starch and/or starch/water interactions may have hindered the recrystallization process.     

Low-fat, High Added Water Bologna from Massaged, Minced Batter

Bolognas were manufactured to produce a high-fat (30% fat), 10% added water (AW) formulation and three low-fat treatments which contained 10% fat/30% AW. Lean and fat trim for the low-fat treatments were blended and minced before massaging intermittently (10 min on/20 min off) for 0, 2.5 and 5.0 hr. Massaging did not affect pH or cook/chill losses but increased batter viscosity. Massaging generally increased purge accumulation, regardless of degree of vacuumization. Sensory and instrumental determinations indicated massaging up to 2.5 hr increased (P<0.05) cohesiveness. In addition, particle definition was decreased. There were no differences (P>0.05) in hardness among low-fat treatments. Massaging resulted in low-fat products that were less cohesive, softer, and more juicy than high-fat bologna.     

Effect of Hardness of Plastic Fat on Structure and Material Properties of Fish Protein Gels

Textural modification of fish protein gels by incorporation of plastic fat was investigated by examining the effect of the physical properties of fat on the structure and the material properties of protein gels. Material properties of fat-containing protein gels were influenced largely by fat distribution pattern which was, in turn, affected by fat hardness. Both compressive and shear forces reached their maximum when fat of 1.8 cm^–1 hardness index (HI) was added at a level of 15% (fat/muscle). Addition of medium hard fat (0.54–0.78 cm^–1 HI): (1) prevented a sponge-like texture development by improving freeze-thaw stability; (2) increased plastic deformation, thus making cooked gels less rubbery; (3) overcame the weakening of texture caused by cooking at the critical zone (60–70°C); and, (4) minimized the variations in textural strength resulting from cooking.     

Effect of high‐pressure treatments prior to cooking on gelling properties of unwashed protein from barramundi (Lates calcarifer) minced muscle

Heat‐induced gelling properties of barramundi minced muscle with 1.5% and 2% added salt were assessed after application of pressures at 300, 400 and 500 MPa at 4 °C (initial temperature) for 10 min and subsequent cooking at 90 °C for 30 min. Whiteness, gel‐forming ability, water‐holding capacity, hardness and springiness of the barramundi gels increased as applied pressure and salt concentration increased. At 2% salt concentration, high‐pressure treatment results in barramundi gels with higher gel strength, mechanical properties and smoother texture as compared to conventional heat‐induced gels (0.1 MPa, 90 °C for 30). At a reduced salt concentration (1.5%) and pressure ≥ 400 MPa, the quality (gel strength, water‐holding capacity, hardness and springiness) of pressurised cooked gels is comparable to those heat‐induced gels with 2% added salt, but the microstructure is smoother. Scanning electron microscope images of pressurised cooked gels showed dense and compact network with smoother surface than those of heat‐only‐induced gels. Thus, application of high‐pressure treatment prior to cooking could be an effective method to enable reduced salt concentration in barramundi gels.     

Structural and rheological properties of amaranth protein concentrate gels obtained by different processes

The heat-induced gelation of amaranth protein concentrates (APCs) by three processes was studied. The first was the conventional process for isolating protein (standard process-st), the second included an acid washing step prior to protein extraction (acid washing process-aw) and the third included heating (50 °C) during the alkaline extraction step (heat process-ht). The dispersions (12%, w/v) were heated to 55–90 °C and assessed by rheological measurements made under small deformations, whereas the gels obtained by heating at 70, 80 or 90 °C/30 min were subjected to uniaxial compression measurements (TPA and mechanical properties). The rheological parameters associated with the network structure, elasticity modulus (E) and storage modulus (G′), increased with increasing gelation temperature. For the APCst and APCht gels, protein aggregation occurred in two steps, whereas for APCaw, gelation occurred in a single step. The APCht gels showed the highest fracturability, hardness and adhesiveness, followed by the APCst and APCaw gels (p < 0.05). Similar results were obtained for the mechanical properties at fracture. Increasing the heat treatment temperature from 80 to 90 °C resulted in a more structured matrix with greater water-holding capacity as compared to gels obtained at 70 °C, and these properties were influenced by the extraction processes used to obtain the APCs. Heat extraction (APCht) improved the gelation and water-holding properties, whereas the acid treatment had the opposite effect.     

Enzymatic Production of Ribonucleotides from Autolysates of Kluyveromyces marxianus Grown on Whey

After 20h fermentation of medium containing 5% (w/v) dehydrated whey, at 30°C, pH 4.5, yeast cells were harvested, diluted in 0.1M KH₂PO₄, and autolyzed at different pHs (6.5–7.5) and temperatures (45–55°C). Phosphodiesterase (0.2–1.0% w/v, 65°C, pH 6.5, 6h) and adenyl deaminase (0.5-1.0% w/v, 60°C, pH 5.5, 4h) were added to the autolysates. After heat treatment (100°C, 15 min), samples were analyzed by RP-HPLC and LC/MS. Production of 5′-ribonucleotides was maximized at 50°C, pH 6.5. Yields of 5′-AMP (800 μg/g of biomass) and 5′-GMP (2000 μg/g) increased considerably after addition of 1.0% phosphodiesterase. 5′-IMP increased only after addition of 1.0% adenyl deaminase.     

Gel properties of silver carp (Hypophthalmichthys molitrix) and chicken mixture gels as affected by setting temperatures

This study aimed to evaluate the effect of setting temperatures (30°C, 35°C, 40°C, 45°C, and 50°C) on gel properties and protein profiles of paste gels derived from silver carp (Hypophthalmichthys molitrix) and chicken meat. The mixture composed of 50% (w/w) chicken meat and 50% (w/w) silver carp meat, and the three paste gels, were assessed based on color, gel strength, TPA, water distribution, chemical interactions, and SDS-PAGE. Chicken gels had better gel properties and a higher content of immobilized water than the mixture or fish gels, regardless of setting conditions. On the other hand, an appropriate setting temperature for the three paste gels promoted aggregation of the myosin heavy chain (MHC) and the formation of hydrophobic interactions and disulfide bonds, which resulted in superior gel properties. Pre-incubation at 40°C enhanced gel properties of fish meat, but pre-incubation at 45°C and 50°C were appropriate for achieving better gels for the mixture and chicken, respectively. These results indicated that there is the potential to obtain mixed products and new meat products by utilizing chicken and fish meat that have improved gel properties.     

Insolubilized Whey Protein Concentrate and/or Chicken Salt-Soluble Protein Gel Properties

Properties of gels prepared from five whey protein concentrates (WPC) with protein solubilities ranging from 27.5% to 98.1% in 0.1M NaCl, pH 7.0, chicken breast salt-soluble protein (SSP), or a combination of SSP and WPC at pH 6.0, 7.0 or 8.0 were compared. WPC did not form gels when heated to 65°C. SSP gels heated to 65°C were harder than those heated to 90°C at all pHs and hardness decreased as pH was increased. Hardness of combination gels heated to 65°C increased as WPC solubility decreased at all pHs; however, the opposite trend was observed at 90°C. Combination gels of the same WPC solubility at 65°C were more deformable than those heated to 90°C.     

Oxidative Stability of Restructured Beef Roasts As Affected by Cooking Temperature

Restructured beef roasts (2.5 kg) were cooked in a water bath at 70, 85, and l00°C to an internal temperature of 65°C, then stored at 4°C for 0 and 3 days. Storage increased (p ≤ 0.05) oxidation; after 3 days storage, roasts cooked at higher temperatures had higher (p ≤ 0.05) TBA values. Sensory panelists detected more (p ≤ 0.05) warmedover flavor (WOF) due to storage; however, after 3 days there was less (p ≤ 0.05) WOF in samples cooked at 70°C than in samples cooked at 85 or 100°C. Interaction (p ≤ 0.05) between cooking temperature and storage indicated oxidation proceeded more rapidly with higher cooking temperatures during refrigerated storage. Cook yield decreased as cooking temperature increased and expressible moisture was lower (p ≤ 0.05) at 100°C than at 70°C.     

Characterisation of heat-set milk protein gels

Milk protein solutions [10% protein, 40/60 whey protein/casein ratio containing whey protein concentrate (WPC) and low-heat or high-heat milk protein concentrate (MPC)] containing fat (4% or 14%) and 70–80% water, form gels with interesting textural and functional properties if heated at high temperatures (90 °C, 15 min; 110 °C, 20 min) without stirring. Adjustment of pH before heating (HCl or glucono-δ-lactone) produces soft, spoonable gels at pH 6.25–6.6, but very firm, cuttable gels at pH 5.25–6.0. Gels made with low-heat MPC, WPC and low fat gave some syneresis; high-fat gels were slightly firmer than low-fat gels. Citrate markedly reduced gel firmness; adding calcium had little effect on firmness, but increased syneresis of low-heat MPC/WPC gels. The gels showed resistance to melting, and could be boiled or fried without flowing. Microstructural analysis indicated a network structure of casein micelles and fat globules interlinked by denatured whey proteins.     

Influence of Gluten and Gum Additives and Cryogenic Treatment on Some Properties and Morphology of Wheat Starch Complex Gels

The influence of gums (guar and xanthan) and gluten additives on the physicochemical properties and structural features of wheat starch gels (8%, w/w) subjected to cryogenic treatment at various temperatures (−9°C, −20°C, −40°C) was studied. Shear modulus and breaking stress of the gels were measured, the gels' morphology was studied with optical microscopy and the local mobility of water in the gels was determined with ESR. The total concentration of polysaccharide additives did not exceed 1% (w/w), and a 65:35 (w/w) mixture of guar and xanthan gums proved to be the optimal additive, which caused a noticeable increase in rigidity and strength of the resulting complex gels. Shear modulus and breaking stress of the gels decreased with lowering the temperature of the cryogenic treatment. The heterogeneous morphology of thin sections of the gel samples was revealed via optical microscopy. ESR studies showed that the local mobility of water was much lower in the gels than in pure water.     

Modification of rheological properties of whey protein isolates by limited proteolysis

Whey protein isolate (WPI) was subjected to limited tryptic hydrolysis and the effect of the limited hydrolysis on the rheological properties of WPI was examined and compared with those of untreated WPI. At 10% concentration (w/v in 50 mM TES buffer, pH 7.0, containing 50 mM NaCl), both WPI and the enzyme-treated WPI (EWPI) formed heat-induced viscoelastic gels. However, EWPI formed weaker gels (lower storage modulus) than WPI gels. Moreover, a lower gelation point (77 °C) was obtained for EWPI as compared with that of WPI which gelled at 80 °C only after holding 1.4 min. Thermal analysis and aggregation studies indicated that limited proteolysis resulted in changes in the denaturation and aggregation properties. As a consequenece, EWPI formed particulated gels, while WPI formed fine-stranded gels. In keeping with the formation of a particulate gel, Texture Profile Analysis (TPA) of the heat-induced gels (at 80 °C for 30 min) revealed that EWPI gels possessed significantly higher (p < 0.05) cohesiveness, hardness, gumminess, and chewiness but did not fracture at 75% deformation. The results suggest that the domain peptides, especially β-lactoglobulin domains released by the limited proteolysis, were responsible for the altered gelation properties.     

Effect of different roasting methods on the proximate by composition,flow properties,amino acid compositions,colour, texture,and sensory profile of the chickpeas

Roasting is a common process for chickpeas to improve their texture, palatability, appearance, shelf-life, physical, and functional properties. This study aimed to determine the effect of different roasting methods (conventional, microwave, and microwave + conventional) on the proximate and amino acid compositions, powder properties, texture, and sensorial properties of the chickpeas. For this purpose three different roasting times (3, 5, and 7 min), microwave powers (100, 300, and 600 W), and microwave roasting + conventional roasting treatment (100 W + 250 °C, 300 W + 250 °C, and 600 W + 250 °C) were applied to raw chickpea samples. The moisture content and water activity values of roasted chickpeas were found to be lower than 7% (w.b.) and 0.50, respectively. The lower ash and protein contents, hygroscopicity value, wettability time and higher fat content and L* value were observed for control compared to roasted samples. The flowability behaviour of the samples was found at a fair level. Roasting methods significantly affected the amount of amino acids in chickpeas but do not reduce the nutritional quality of their proteins. The hardness value of chickpea samples from the suture and cheek angle was decreased parallel to the increase in the roasting temperature and time. The highest sensory scores in terms of general appeal were obtained from the combined group (300 W–250 °C) for 3 min.     

Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels

The mechanical properties and microstructure of 2.7% and 4.5% sodium caseinate gels chemically acidified by glucono-δ-lactone (GDL) and cross-linked by microbial transglutaminase (TG) were studied. The acidification was performed at different temperatures. According to SDS–PAGE TG clearly caused polymerisation of caseinate irrespective of the treatment temperature (4–50 °C), The cross-linking of the proteins was more extensive at temperatures 22–50 °C. Low amplitude viscoelastic measurements showed that 4.5% caseinate gels acidified at 50 °C were formed much faster than gels acidified at 22 °C. TG only slightly increased the time of gelling. Control gels prepared without TG at temperatures of 4, 22, 37 and 50 °C were mechanically weak. Examination of the control gels with a confocal laser scanning microscope showed that gels formed at 37 and 50 °C were coarse and porous with large cavities between particle aggregates, whereas those formed at 22 °C were much more homogeneous. The TG-treated and acidified sodium caseinate dispersions formed firm gels, indicating cross-linking of casein proteins. Interestingly, the strongest gels were formed at 22 and 37 °C. TG treatment improved the homogeneity of the gel structure at temperatures of 37 and 50 °C. The hardness of TG-treated gels acidified at 4 °C increased during 1 week of storage.     

Rheological and Water-Holding Properties of Gelled Meat Batters Containing Iota Carrageenan, Kappa Carrageenan or Xanthan gum

Meat batters containing either 0.5% or 1% iota carrageenan (IC, kappa carrageenan (KC) or xanthan gum (XG) were investigated. Rigidity changes during heating and Instron texture profile analysis indicated textural properties of batters. All treatments exhibited a decrease in water-holding ability (WHA) from 55–70°C. Addition of IC increased WHA, rigidity at 70°C, force-to-fracture and true shear strain. KC increased rigidity at 70°C and was most effective at increasing hardness. XC decreased all textural parameters measured. Gums were specific in affecting textural and WHA properties.     

Crystallization and Drying in Thin Sucrose Films During Panning

Sucrose crystallization in thin films (50–55 μm) was studied, using a videomicroscopy technique, at conditions encountered during hard panning processes. No nucleation occurred in unseeded films, while a linear increase in seeded crystals occurred during drying. Crystal growth rate increased with temperature (25–30°C) and with air velocity (2.4–12.5 m/sec), but did not change with varying sucrose concentrations (70–76% w/w) and relative humidities (0–66% at 30°C). FD & C Yellow No. 5 food coloring in the dye form (0.05–0.5 g/100 mL) showed no effects while similar concentrations in the lake form inhibited crystal growth rate.