Lipolysis in reduced sodium Feta cheese made by partial substitution of NaCl by KCl

Feta cheese (five trials) of different sodium content was made from split lots of curd by varying the salting procedure, i.e. dry salting with NaCl (control) or mixtures of NaCl/KCl (3 : 1 or 1 : 1, w/w basis) and filling the cans with brine made with NaCl or the above NaCl/KCl mixtures, respectively. Lipolysis in cheese was monitored during aging by using the acid degree value (ADV) method and gas chromatography (GC). It was found that the ADVs of control and experimental cheeses were similar (P>0.05) at all sampling ages (3, 20, 40, 60, 120 and 240 d). Moreover, the results of GC showed that there were neither qualitative nor significant (P>0.05) quantitative differences in the individual free fatty acids (FFA) of the control and experimental cheeses at the ages of 40 and 120 d. These findings indicated that the partial substitution of NaCl by KCl in the manufacture of Feta cheese had no effect on lipolysis during cheese aging.     

Generation of volatile compounds in Brazilian low-sodium dry fermented sausages containing blends of NaC1, KC1, and CaC12 during processing and storage

Brazilian dry fermented sausages with different salt contents were manufactured: control (2.5% NaCl), 50% salt reduced (1.25% NaCl, F1), 50% replaced by KCl (1.25% NaCl and 1.25% KCl, F2), 50% replaced by CaCl₂ (1.25% NaCl and 1.25% CaCl₂, F3), and 50% replaced by KCl and CaCl₂ (1.25% NaCl, 0.625% KCl and 0.625% CaCl₂, F4). Changes in the composition of volatile compounds were studied during processing (0, 7, and 19 days) and storage (30, 60, and 90 days). Neither reduction nor replacement of NaCl by KCI affected the volatile compounds produced during the manufacturing process, and both increased the volatile compounds from carbohydrate fermentation and amino acid degradation during storage. The addition of CaCl₂ improved the generation of hexanal and (E)-hept-2-enal and other volatiles from lipid oxidation during processing and storage. After 90 days of storage, the control sample showed an increase in the generation of volatile compounds from lipid oxidation.     

Effect of soy protein substitution for sodium caseinate on the transglutaminate-induced cold and thermal gelation of myofibrillar protein

The influence of soy protein isolate (SPI) substitution for sodium caseinate (SC) on the properties of cold-set (4 °C) and heat-induced gels of pork myofibrillar protein (MP) incubated with microbial transglutaminase (TG) was investigated. The strength of cold-set MP–SC gels (formed in 0.45 M, NaCl, 50 mM phosphate buffer, pH 6.25) increased with time of TG incubation, but those gels with more than 66% SPI substituted for SC had a >26% reduced strength (P < 0.05). Upon cooking, both incubated and non-incubated protein sols were quickly transformed into highly elastic gels, showing up to 6000 Pa in storage modulus (G′) at the final temperature (72 °C). However, no differences (P < 0.05) in G′ were observed between heated samples with SPI and SC. Myosin heavy chain, casein and soy proteins gradually disappeared with TG incubation, contributing to MP gel network formation. Both cold-set and heat-induced gels had a compact protein matrix, attributable to protein cross-linking by TG.     

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.     

Gelation properties of salt-extracted pea protein induced by heat treatment

Gelation is one of the most important properties of plant proteins. In this paper, a low denaturation salt extraction method was used to extract pea (Pisum sativum L.) protein isolate from commercial pea flour. The gelation properties of this isolate were examined and compared to commercial products. The pea protein isolate followed the three-step process of gelation that is generally accepted for heat-induced gelation of globular proteins. The minimum gelation concentration of salt-extracted pea protein isolate (PPIs) was 5.5% while that of commercial pea protein isolate (PPIc) was 14.5%. The gelling point was in the range of 82–86 °C for 14.5% PPIs, 0.3 M NaCl at natural pH (5.65). With increasing heating rate, the gelling point tended to increase. Higher heating and cooling rates resulted in decreased final G′ (storage modulus) and G″ (loss modulus) values, indicative of decreased gel strength. A higher protein concentration resulted in higher G′ and G″ values and it was found that there was a power law relationship between protein concentration and G′ and G″. Tan delta (δ) values decreased with increasing protein concentration and at concentrations of 5.5% and above, tan δ remained constant which means the critical concentration for gel formation was 5.5%. The values of G′ and G″ for PPIs were greater than those of PPIc, and tan δ of PPIs was smaller, indicative of a stronger gel network. DSC data showed that PPIc had undergone denaturation whereas PPIs had not (ΔH = 15.81 J/g protein). Although rheometer data showed that the final G′ value of commercial soy protein isolate (SPIc) was smaller than that of PPIs, the gel prepared with SPIc was visually stronger than that of PPIs. The rheological data obtained with small amplitude oscillatory testing was not consistent with the actual observations. Overall, the low degree of denaturation of the PPIs resulted in a stronger gel than that of PPIc making the PPIs a more attractive food ingredient.     

Suppressive effect of Tetragenococcus halophilus,isolated from fish-nukazuke,on histamine accumulation in salted and fermented fish

Occasionally, quantities higher than 1000 mg/kg of histamine (Hm) accumulate in salted and fermented fish products by the histidine decarboxylase of halophilic lactococci Tetragenococcus sp. In a total of 200 isolates from fish nukazuke (salted and fermented fish with rice bran), 13 strains produced Hm more than 200 μg/ml in 0.5% histidine containing broth, whereas 130 isolates produced absolutely no Hm. Among the strains, 22 strains suppressed the Hm production of the Hm-forming (HmF) strains. Both the HmF and Hm-suppressing (HmS) strains were identified as Tetragenococcus halophilus. To observe the Hm-suppressing effect, a specified quantity of live cells was needed. In the case of 10% NaCl salted sardine, inoculation with 3 log cells/g of a strain HmF-131 resulted in a significant Hm accumulation, 2800 μg/g in 30 days at 20 °C. The increase in Hm was clearly suppressed by 9 log live cells/g of strain HmS-129. These results suggest that HmS-129 can be used as a starter for salted and fermented fish products, enhancing food safety.     

The cooling rate effect on the microstructure and rheological properties of blends of cocoa butter with vegetable oils

The elasticity (G′) and yield stress (σ¹) of blends of cocoa butter (CB) in vegetable oils (i.e., 30% CB/canola and 30% CB/soybean oil) crystallized at temperatures (T_Cr) between 9.5 °C and 13.5 °C and two cooling rates (1 °C/min and 5 °C/min) were determined, evaluating their relationship with parameters associated with the formation and structural organization of the crystal network [i.e., solid fat content (SFC), Avrami index, crystallization rate, fractal dimension (D)]. The results showed that T_Cr and cooling rate had a different effect for each blend on the three-dimensional organization of the crystal network, and on the proportion and size of β′ and β crystals. Thus, under low supercooling conditions at both cooling rates, the crystallized CB/canola oil blend was formed by a mixture of small β′ and large β crystals that provided high G′ and σ¹ at low SFC (i.e., 20.5–20.9%) and D (i.e., 1.66–1.72) values. The CB/soybean oil blend achieved similar G′ and σ¹ independent of cooling rate only at high supercooling. In this case, the crystal network was formed mainly by small β′ crystals with SFC (i.e., 25.4–26.3%) and D (i.e., 2.86–2.79) values higher (P < 0.05) than in the CB/canola oil blend at low supercooling.     

Gelling properties of protein fractions and protein isolate extracted from Australian canola meal

Gelling properties of canola albumin and globulin fractions, and canola protein isolate (CPI) were examined in this study. The effects of pH and salt concentration on canola protein gelling properties were studied primarily by means of dynamic oscillatory rheology and gel texture analysis. The findings were supported by confocal laser scanning microscopy (CLSM) images of the gels, isoelectric point, and solubility measurement data. All canola proteins showed typical heat-set gel protein profiles. Gels formed at higher pH had better gelling properties including higher overall resistance to deformation (G*), higher gel elasticity (low tan δ ), higher fracture stress and firmness, and denser gel microstructure. Isoelectric points of canola proteins used in this study were in the range of pH 3.0–4.7 where low protein solubility was observed. The albumin fraction was able to form a very weak gel at pH 4, whereas the globulin fraction and CPI precipitated due to loss of protein surface charge. The effects of NaCl on gelling were protein sample dependent. The presence of NaCl negatively affected gelling properties of albumin and globulin fractions, with decreases in overall resistance to deformation (G*), and fracture stress and firmness, but positively affected CPI gels in the same aspects. The elasticity (tan δ) of all canola protein gels remained constant in the presence of NaCl. Frequency sweep analysis revealed that the albumin fraction and CPI formed weak gels, whereas the globulin fraction formed a strong gel. Strain sweep analysis further confirmed that the globulin fraction formed a stronger gel with a critical strain of at least 10%. This study demonstrates the high potential of canola proteins, particularly the globulin fraction, as a prospective gelling agent.     

Modelling the effect of pH,sodium chloride and sodium pyrophosphate on the thermal resistance of Escherichia coli O157:H7 in ground beef

The objective of this study was to assess the combined effects of temperature, pH, sodium chloride (NaCl), and sodium pyrophosphate (SPP) on the heat resistance of Escherichia coli O157:H7 in minced beef meat. A fractional factorial design consisted of four internal temperatures (55.0, 57.5, 60.0 and 62.5 °C), five concentrations of NaCl (0.0, 1.5, 3.0, 4.5 and 6.0 wt/wt.%) and SPP (0.0, 0.1, 0.15, 0.2 and 0.3 wt/wt.%), and five levels of pH (4.0, 5.0, 6.0, 7.0 and 8.0). The 38 variable combinations were replicated twice to provide a total of 76 survivor curves, which were modelled by a modified three-parameter Weibull function as primary model. The polynomial secondary models, developed to estimate the time to achieve a 3-log and a 5-log reduction, enabled the estimation of critical pH, NaCl and SPP concentrations, which are values at which the thermo-tolerance of E. coli O157:H7 reaches it maximum. The addition up to a certain critical concentration of NaCl (~ 2.7–4.7%) or SPP (~ 0.16%) acts independently to increase the heat resistance of E. coli O157:H7. Beyond such critical concentrations, the thermo-resistance of E. coli O157:H7 will progressively diminish. A similar pattern was found for pH with a critical value between 6.0 and 6.7, depending upon temperature and NaCl concentration. A mixed-effects omnibus regression model further revealed that the acidity of the matrix and NaCl concentration had a greater impact on the inactivation kinetics of E. coli O157:H7 in minced beef than SPP, and both are responsible for the concavity/convexity of the curves. When pH, SPP or NaCl concentration is far above or below from its critical value, the temperatures needed to reduce E. coli O157:H7 up to a certain log level are much lower than those required when any other environmental condition is at its critical value. Meat processors can use the model to design lethality treatments in order to achieve specific log reductions of E. coli O157:H7 in ready-to-eat beef products.     

Characterization of gellan/gelatin mixed solutions and gels

The physico-chemical properties of gellan/gelatin mixed solutions and gels were examined at five different ratios of gellan to gelatin (100:0 (I), 80:20 (II), 60:40 (III), 40:60 (IV), 20:80 (V)) and four different NaCl levels (0–300 mmol/l). All mixed solutions exhibited the shear-thinning behavior, which decreased with increasing gelatin proportion, temperature, and NaCl level. Synergism on G′ was observed in mixed solution III and IV depending on NaCl level. Hardness of mixed gel decreased with increasing gelatin proportion and cohesiveness increased up to the gellan to gelatin ratio of 40–60 and then decreased. For gellan dominant gels, maximum hardness and cohesiveness were observed at NaCl level of 150 mmol/l. Increasing gelatin proportion caused an increase in gel turbidity at lower NaCl levels and a decrease in gel turbidity at higher NaCl levels. In general, WHC increased with increasing gelatin proportion and decreasing NaCl level. Color holding capacity significantly increased with increasing gelatin proportion. Flavor holding capacity increased by adding gelatin and then linearly decreased with increasing gelatin proportion. Therefore, this study suggests that there is an optimum NaCl concentration and gellan to gelatin ratio to enhance the physico-chemical properties of gellan/gelatin mixed solutions and gels.     

Intrinsic viscosity and viscoelastic properties of xanthan/guar mixtures in dilute solutions: Effect of salt concentration on the polymer interactions

An oscillating capillary rheometer was used to investigate the dynamic viscoelastic and intrinsic viscosity properties of deacetylated xanthan (0.025%), native xanthan (0.025%), guar gum (0.075%), and xanthan–guar mixtures in dilute solutions. Influence of ionic strength on xanthan conformation and interaction with guar gum was elaborated. As the salt concentration increased, a significant (P < 0.05) decrease in viscosity (η′) and elasticity (η″) values was observed for both native xanthan–guar mixtures and deacetylated xanthan–guar mixtures. In water and 2 mM NaCl solution, the relative viscosity and η″ of both native xanthan–guar mixtures and deacetylated xanthan–guar mixtures were much higher than of those calculated for mixtures assuming no interaction, whereas no pronounced increase was found for polysaccharide mixtures in 40 mM NaCl. The intrinsic viscosities of deacetylated xanthan–guar mixtures in water and 2 mM NaCl were higher, whereas the intrinsic viscosities of native xanthan–guar mixtures were lower than those calculated from the weight averages of the two individually, assuming no interaction. These results demonstrated that intermolecular interaction has occurred between xanthan and guar mixtures in water and 2 mM NaCl, but may not occur in 40 mM NaCl, and mutual incompatibility may occur. The results suggest that the degree of disordering of xanthan played a critical role in xanthan–guar interaction and may explain the differences in η′, η″, and intrinsic viscosity measurements between 2 and 40 mM NaCl.     

Ultrasonic processing influences rheological and optical properties of high-methoxyl pectin dispersions

The effect of high-intensity ultrasound on the rheological and optical properties of high-methoxyl pectin dispersions was studied. Pectin solutions (1.15 wt% pectin, 41.4 wt% sucrose) were treated with high-intensity ultrasound at intensity levels ranging from 0 to 40 W cm⁻² for various times (0–60 min). Samples were adjusted to pH 1.5 to initiate gelation and their dynamic rheological properties (G′, G″) were recorded as a function of time using a rotational rheometer. Ultrasonically pretreated pectin dispersions formed weaker gels with increasing sonication power and time. After 4 h, log G′ of the pectin dispersion that was pretreated at the highest intensity level (40 W cm⁻² and 30 min) was approximately five times lower than log G′ of the untreated dispersion. The change in phase angle [arctan (G′/G″)] with time indicated that the rate of gelation decreased as ultrasonic intensity and application time increased. The turbidity of ultrasonically pretreated pectin dispersions decreased by 50% yielding more transparent gels. Results were attributed to an overall reduction in the average molecular weight of pectin due to cavitational effects. A power law model was fitted to the flow curves of ultrasonically pretreated pectin dispersions to determine both flow behavior index n and consistency coefficient K. With increased sonication power and application time, n increased from 0.6 to 0.97 indicating that the flow behavior changed from viscoelastic to Newtonian.     

Gelling of microbial transglutaminase cross-linked soy protein in the presence of ribose and sucrose

Soy protein isolate (SPI) was incubated with microbial transglutaminase (MTGase) enzyme for 5 (SPI/MTG(5)) or 24 (SPI/MTG(24)) h at 40 °C and the cross-linked SPI obtained was freeze-dried, and heated with 2% (w/v) ribose (R) for 2 h at 95 °C to produce combined-treated gels. Longer incubation period resulted in more compact and less swollen SPI particle shape when reconstituted with sugar solution. Thus, this MTGase treatment affected samples in terms of flow behaviour and gelling capacity. Rheological study showed different gelling profiles with the cross-linking treatments and combined cross-linked SPI gave a higher G′ value compared to single treated samples. These are due to the formation of additional ε-(γ-glutamyl)lysine bonds and “Maillard cross-links” within the SPI protein network during the MTGase incubation and heating in the presence of ribose (i.e. reducing sugar). Network/non-network protein analysis found that network protein increased with cross-linking treatment, which also resulted in different SDS–PAGE profiles. As in non-network protein fraction, A₄ subunit was suggested to become part of the network protein as a result of combined cross-linking.     

Estimation of Residual Pepsin and Chymosin Activity in Curd,

Pasteurized milk (225 g) adjusted to pH 6.2 was set with 3.5 milk clotting units of chymosin (EC 3.4.23.4). The same amount of milk at pH 5.8 was set with 3.5 milk clotting units of porcine pepsin (EC 3.4.23.1). Fifteen minutes after clotting, the curd was broken, and curd and whey were separated by centrifugation at 3500 × g for 20 min. The curd (30 g) was extracted at pH 6.8 in 450 ml water or at pH 6.2 (chymosin) or 5.8 (pepsin) in 450 ml 1 M sodium chloride.Chymosin was completely released from the curd and accounted for by both methods of extraction. Pepsin was completely released and accounted for after extraction in 1 M sodium chloride at pH 5.8 but was partly inactivated during extraction at pH 6.8.Assay of curd extracts and whey by a linear agar diffusion test accounted for 102 ± 6% of the pepsin activity added to milk when the curd was extracted in 1 M sodium chloride. Extraction at pH 6.8 allowed recovery of only 63% of the activity. Chymosin recovery was 100 ± 5% by both methods of curd extraction.     

Purification and partial characterisation of X-prolyl dipeptidyl aminopeptidase of Lactobacillus helveticus ITG LH1

A X-prolyl dipeptidyl aminopeptidase (EC 3.4.14.5, XPDAP) from Lactobacillus helveticus ITG LH1, a strain used for Swiss-type cheese, was purified by ion exchange and affinity chromatographies. The enzyme appeared to be a 140 kDa monomer. Optimal activity occurred at pH 7 and 40°C, but it was rapidly inactivated above 50°C. The enzyme was activated by NaCl and KCl up to 50–200 mm but its activity levelled off at higher salt concentrations. Its complete inhibition was caused by 0.1 mm HgCl₂, 1 mm SnCl₂ and 2.5 mm CuCl₂. It was inactivated by reagents specific for serine proteases, such as phenylmethylsulfonyl fluoride and sulfhydryl group-blocking reagents. The enzyme hydrolysed p-nitroanilide-substituted X-Pro and X-Ala dipeptides, as well as β-casomorphin 1-4.     

Application of electro-activated potassium acetate and potassium citrate solutions combined with moderate heat treatment on the inactivation of Clostridium sporogenes PA 3679 spores

Combined effects of moderate temperatures and the electro-activated aqueous solutions of potassium acetate and potassium citrate on the inactivation of C. sporogenes PA 3679 spores (D_121°C = 1.18 min) were studied. Four types of solutions (potassium acetate with/without KCl and potassium citrate with/without KCl) were activated at 400 mA for 60 min. The oxidation reduction potential (ORP) and pH values ranged from + 417.50 to + 1043.33 mV and 3.18 to 3.47, respectively. The combination of these solutions with a moderate heat treatment (95 °C, 105 °C, and 115 °C) for different time (5, 10, 20, and 30 min) was sufficient to reach a 100% of spore destruction (inactivation) in a medium with an initial contamination level comprised between 7.0 and 7.8 log CFU/mL. The sporicidal effect of solutions was also present even if activated solutions were applied alone against spores without being combined with heat treatment. Spore morphology was determined under transmission electron microscopy and showed that there were important damages, such as rupture of spores and release of spore components in all of the treated spores. Thus, the sporicidal effect detected was the result of inactivation mechanisms of electro-activated solutions on spores. In almost all of observed micrographs, there were coreless spores, deformed spores, or debris of spores. The current investigation can be used for achieving further studies in order to better understand the mechanisms of inactivation of C. sporogenes spores by electro-activated solutions.Industrial relevanceThis research article aims to study the combined effect of electro-activated potassium acetate and citrate solutions and moderate heat treatment on the viability of Clostridium sporogenes in model solutions as a non-pathogenic surrogate of Clostridium botulinum. The objective was to use hurdle technology to produce nutritious, minimally processed foods while ensuring food safety. Moreover, this approach allowed for a reduced level of sodium in canned foods since the solutions were sodium-free.     

Roles of components of rice-based fat substitute in gelation

The roles of maltodextrin, protein and fat in the gelation of the rice-based fat substitute were investigated. Rheological properties and gel strength of samples were measured. Results showed that the rising rates of both G′ and G″ of rice starch-based fat substitute were higher than those of rice-based fat substitute when temperature was lower than 35 °C. G′ was equal to G″ at 60 °C for 25% rice-based fat substitute whilst it was at 35 °C for rice starch-based fat substitute. The presence of rice protein and fat increased G′ and G″. Gel strength of rice-based fat substitute was lower than that of starch-based fat substitute at 25% solid content. However, gel strength of a fat substitute increased in the presence of protein. SEM showed that protein particles aggregated to gel. Therefore, protein in rice-based fat substitute gelled firstly, followed by maltodextrin which formed the main matrix of the rice-based fat substitute gel. Fat benefited for gel formation.     

Rheological properties of stirred yoghurt as affected by gel pH on stirring,storage temperature and pH changes after stirring

The rheological properties of stirred yoghurt were studied as a function of the delay between milk heat-treatment and inoculation (0, 1 and 2 days), of pH in the acid gel on stirring (4.4, 4.7, and 5.0), of the storage temperature (4, 12, and 20 °C) for 24 h following stirring and of over-acidification (allowed or inhibited). At low pH values, the gels exhibited higher elastic modulus (G′) and fracture strength. They yielded stirred yoghurts with higher G′ and viscosity, and higher increase in G′ and viscosity during storage (“rebodying”). Rebodying was only partially explained by over-acidification and cooling. Changing the storage temperature had no impact on the evolution of G′ after stirring; hydrophobic interactions were therefore probably not involved in rebodying. Electrostatic interactions seemed to play a major role in rebodying, as pH on stirring was the significant factor.     

Comparison of corneal hysteresis and corneal resistance factor after small incision lenticule extraction and femtosecond laser-assisted LASIK: A prospective fellow eye study

PurposeTo compare corneal hysteresis (CH) and corneal resistance factor (CRF) between eyes treated with small incision lenticule extraction (SMILE) and femtosecond laser-assisted laser in situ keratomileusis (femto-LASIK).SettingBeyoğlu Eye Training and Research Hospital.DesignProspective comparative case series.MethodsSixty eyes from 30 patients with bilateral myopia or myopic astigmatism were studied. Inclusion criteria were spherical equivalent of subjective manifest refraction (SE) <10 diopters (D) and a difference ≤0.50 D between the SEs of both eyes. One eye of each patient was treated with SMILE, and the fellow eye underwent femto-LASIK. Randomization was performed using a sealed envelope system. The main outcome measures were CH and CRF measured preoperatively and postoperatively (1 and 6 months).ResultsPreoperative SE was similar in both groups (p = 0.852). CH and CRF values were reduced postoperatively in both groups compared to their corresponding preoperative values (p < 0.001). At the 6-month follow-up visit, the mean CH values in the SMILE and femto-LASIK groups were 8.95 ± 1.47 and 9.02 ± 1.27, respectively (p = 0.852), and the mean CRF values were 7.77 ± 1.37 and 8.07 ± 1.26, respectively (p = 0.380).ConclusionCH and CRF decreased after SMILE. There were no differences between SMILE and femto-LASIK treatments in postoperative CH or CRF values.