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.     

Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase

Alkali (pH₁₂) and acid (pH_1.5) pH-treated soy protein isolates (SPI) were incorporated (0.25–0.75% protein) into sols of myofibrillar protein (MP, 3%, in 0.6 M NaCl at pH 6.25) with or without 0.1% microbial transglutaminase (TG) to investigate the potential as meat processing ingredients. Static and dynamic rheological measurements showed significant enhancements of MP gelling ability by the inclusion of pH_1.5-treated as well as preheated SPI (90 °C, 3 min). A 7-h incubation with TG accentuated the gel-strengthening effect by these SPI samples. The B subunit in 11S of SPI was the main component manifesting structure reinforcement in the mixed gels. The MP gelling properties were also greatly improved (P < 0.05) by the addition of 10% canola oil emulsions stabilized by pH-treated SPI. The principal force in the MP gels incorporated with pH-treated SPI was hydrophobic patches; in the presence of TG, cross-linking of previously dissociated A and B subunits of 11S was also intimately involved.     

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 300–400 MPa improved water-binding capacity and decreased TPA parameters of SSMP-CK gels (P < 0.05), while 100 MPa could increase hardness and chewiness of the gels. The thermal transition temperature peak for the myosin head (T_peak1) of SSMP disappeared on addition of CaCl₂ and κ-carrageenan. 300 MPa 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 Ca^2 +. It is of interest to develop low-fat and sodium-reduced meat products.     

Xanthan Enhances Water Binding and Gel Formation of Transglutaminase-Treated Porcine Myofibrillar Proteins

ABSTRACT: In this study, the effect of xanthan on dynamic rheological properties, textural profile, and water binding of transglutaminase (TG)-treated myofibrillar protein (MP) gels was investigated. In experiment 1, MP suspensions (40 mg/mL protein, 0.6 M NaCl) at pH 6.45 with or without 0.05% xanthan were treated with 0%, 0.1%, 0.2%, 0.3%, 0.4%, and 0.5% TG; in experiment 2, MP suspensions (40 mg/mL protein, 0.6 M NaCl) at pHs 6.13, 6.30, 6.45, 6.69 with or without 0.05% xanthan were treated with 0.3% TG. Treated samples were analyzed with differential scanning calorimetry for thermal stability and oscillatory rheometry and Instron penetration tests for gelation properties. The TG treatments lowered the transition temperature (T_m) of MP by as much as 6 °C (P < 0.05) but increased apparent enthalpy of denaturation. However, there was no detectable thermal stability difference between MP samples with or without xanthan. The shear storage modulus (G′) of MP gels increased markedly upon treatments with ≥0.3% TG, and the presence of xanthan further enhanced the gel strength (P < 0.05). The addition of 0.05% xanthan decreased cooking loss of TG-treated MP gels by 17% to 23% when compared with gels without xanthan at all pH levels evaluated (6.13 to 6.67). Thus, the combination of TG and xanthan offered a feasible means to promote cross-linking and gelation of MP while reducing cooking losses.     

Microstructure, rheology and storage stability of low-fat yoghurt structured by carrot cell wall particles

Plant cell wall particles derived from fruits and vegetables are natural fibre materials with a low calorie content that can be used as a healthy alternative to gum stabilisers and starches for structuring low-fat yoghurt. In this study we investigated the effect of cell wall particle (CWP) addition on the gelation kinetics, viscoelastic properties, microstructure, texture and whey loss of the set yoghurt gels as a function of CWP concentration, particle size and storage time. Three particle sizes of dried carrot CWP (d_0.5 = 34, 71 and 80 ??m) were produced from an industrial carrot pomace. Rehydrated CWP was added to skim milk prior to acidification. The results showed that the addition of carrot CWP accelerated the rate of pH reduction and induced earlier gelation. The gel viscoelastic properties were enhanced with increased CWP concentration. This was accompanied with progressive reduction in the whey loss. The smallest cell wall particles (d_0.5 = 34 ??m) gave better gel strength and lower whey loss compared to the larger CWP particles, possibly due to higher contact between the CWP and casein particles thus contributing to the stronger gel network. The CLSM images of yoghurt gels containing CWP showed that carrot CWP occupied the void space within casein particle network. The enhanced gel strength and reduced whey loss achieved by the addition of CWP were maintained throughout the 28 day storage period. The reduction of fermentation processing by almost 1 h, yet still achieving good gel properties for the yoghurt type product could be a significant benefit from a manufacturing point of review.     

The determination of vitamin D3 in bovine milk by liquid chromatography mass spectrometry

A renewed international interest in vitamin D status has revealed significant deficiencies in several populations, including Australia. Vitamin D exists in two forms, cholcalciferol (D₃) and ergocalciferol (D₂). The main source of vitamin D₃ is from exposure of 7-dehydrocholesterol present in the skin to UV irradiation. However, there is an absolute requirement for vitamin D through proper dietary intake if humans live in the absence of sunlight or exclusively indoors. Bovine milk is considered to be a good dietary source of vitamin D₃, even though the levels are quite low. This paper describes robust methods using liquid chromatography–linear ion trap mass spectrometry (LC–MSⁿ) and liquid chromatography–tandem mass spectrometry (LC–MS/MS) to measure the levels of vitamin D₃ in fresh bovine milk (0.05 μg/100 ml), commercial (natural and fortified) milk samples (0.01–2 μg/100 ml) and a dairy based infant formula (8 μg/100 g), without the need for extensive clean-up procedures. The limits of quantification (LOQ) are 0.01 μg/100 ml and 0.02 μg/100 ml for LC–MSⁿ and LC–MS/MS, respectively. Recoveries of vitamin D₃ added to the samples prior to saponification were satisfactory (range 60–90%). 25-Hydroxyvitamin D₃ was not present in any of the samples analysed (LOQ = 0.01 μg/100 ml, recovery range 30–40%).     

Using whey protein gel as a model food to study dielectric heating properties of salmon (Oncorhynchus gorbuscha) fillets

It is desirable to develop rapid commercial microwave and radio frequency sterilization processes to produce high quality shelf stable muscle foods, particularly aquatic foods. Whey protein gels containing d-ribose and salt were studied as a model food to determine heating patterns in salmon fillets during high temperature microwave sterilization processes. Dielectric constant (?′) and loss factor (?″) of whey protein gels with d-ribose (0.5 g/100 g, 1 g/100 g, and 1.5 g/100 g) at different salt contents (0, 0.1 g/100 g, 0.2 g/100 g, 0.3 g/100 g, 0.4 g/100 g, and 0.5 g/100 g) and frozen and thawed pink salmon (Oncorhynchus gorbuscha) fillets were determined over the frequency range of 27-1800 MHz at temperatures ranging from 20 to 120 °C. The dielectric properties of whey protein gels containing 1 g/100 g d-ribose and 0.2 g/100 g or 0.3 g/100 g salt closely matched the dielectric behavior of salmon fillets in both radio frequency (RF, 27 MHz) and microwave (MW, 915-1800 MHz) ranges. Altering the salt content had a greater impact on dielectric constant and loss factors at lower frequencies. These results suggest that whey protein gel may be a good model food for microwave sterilization process development, particularly for determining the locations of cold and hot spots in complex muscle foods.     

Sweetness and texture perception in mixed pectin gels with 30% sugar and a designed rheology

Pure low-methoxyl (LM) pectin and mixtures of LM and high-methoxyl (HM) pectin in different ratios were used to produce gels with control over the rheological parameter storage modulus (G′). The gels either had similar pectin concentrations and different G′ values, or different pectin concentrations and similar G′ values. All gels were prepared with 30 g/100 g sugar, in the presence of 0.1 g/100 g CaCl₂, at pH 3.5; these are conditions that favour gel formation of both LM and HM pectin.The gels were compared for their sensory characteristics; specifically sweetness, sourness, thickness, and glueyness. Sweetness was found to increase with increasing storage modulus (G′) in pectin gels of similar pectin concentration, but different G′ values. Gels with higher proportions of LM pectin were perceived as sweeter than those with low LM pectin ratios. These gels also had increasing loss modulus (G″), and increasing differences between G′ and G″, which indicates that diffusion has a bearing on the perception of sweetness in pectin gels. Thickness and glueyness were mostly determined by total pectin concentration. Thickness also increased with increasing LM pectin concentration while glueyness increased with increasing HM pectin concentration.     

Inactivation of Cronobacter sakazakii by ultrasonic waves under pressure in buffer and foods

The objective of this research was to characterize the resistance of Cronobacter sakazakii to ultrasonic waves under pressure (manosonication, MS). The D_MS value (decimal reduction time value) of C. sakazakii in standard conditions (35 °C, 117 μm, 200 kPa, citrate-phosphate buffer pH 7.0) was 0.41 min. This value was higher than that of Yersinia enterocolitica (D_MS = 0.19 min) and lower than those of Salmonella enterica serovar Enteritidis (D_MS = 0.61 min), Listeria monocytogenes (D_MS = 0.86 min), and Enterococcus faecium (D_MS = 1.2 min). Strain studied (ATCC 29544, NCTC 8155, 9238, and 9529), growth temperature (10, 20, 30, and 37 °C), and pH of the treatment media (4.0, 5.0, 6.0, and 7.0) did not significantly change C. sakazakii MS resistance. Conversely, entry into stationary growth phase, decreasing water activity of the treatment media (0.98, 0.96, and 0.94), and treatment in food products (apple and orange juices, chicken and vegetable soups, and rehydrated powdered milk) resulted in up to a 1.6-, 3.9-, and 2.5-fold maximum change in D_MS values, respectively. Whereas an exponential relationship between the amplitude of ultrasonic waves and D_MS values was found, the relationship between static pressure and D_MS values was better described by a quadratic equation. The energy transferred into the medium determined the lethality of the ultrasonic waves regardless of the combination of pressure (0, 50, 100, 200 and 300 kPa) and amplitude (34, 62, 90, 117 and 145 μm) applied. There was an exponential relationship between D_MS values and the power input: an increase of 134 W increased the inactivation rate ten times regardless of the treatment medium. No C. sakazakii cells with sublethally injured cytoplasmic membrane or with sublethal oxidative damage occurred after MS treatments, but the results indicated that damage to the outer membrane preceded microbial death.     

Improved creaminess of low-fat yoghurt: The impact of amylomaltase-treated starch domains

Amylomaltase-treated starch (ATS) is an excellent creaminess enhancer in yoghurt. Small amounts of ATS raised the creaminess perception of low-fat yoghurt (1.5%) to that of full-fat yoghurt (5%). In this way, a reduction in fat-related energy value could be achieved from 45 to 21.5 kcal/100 g product. The functionality of ATS in set yoghurt resulted from discrete domains of ATS that resemble the microstructural behaviour of fat particles. The microstructure of the yoghurt is dominated by the protein and the ATS domains are enclosed in or bound to this protein network. The perceived creaminess resulted from in-mouth melting of these ATS domains due to a combined effect of their physical melting and hydrolysis by amylase present in the saliva.     

Rheology and microstructure of myofibrillar protein-plant lipid composite gels: Effect of emulsion droplet size and membrane type

Composite gels were prepared from 2% myofibrillar protein (MP) with 10% imbedded pre-emulsified plant oils (olive and peanut) of various particle sizes at 0.6 M NaCl, pH 6.2. Dynamic rheological testing upon temperature sweeping (20-70 °C at 2 °C/min) showed substantial increases in G′ (elastic modulus) of MP sols/gels with the addition of emulsions, and the G′ increases were inversely related to the emulsion droplet size. Furthermore, gels containing emulsified olive oil had a greater (P < 0.05) hardness than those containing emulsified peanut oil. Regardless of oil types, MP-coated oil droplets exhibited stronger reinforcement of MP gels than Tween 80-stablized oil droplets; the latter composite gels had considerable syneresis. Light microscopy with paraffin sectioning revealed a stable gel structure when filled with protein-coated oil droplets, compared to gels with Tween 80-treated emulsions that showed coalesced oil droplets. These results suggest that rheological characteristics, hardness, texture, and water-holding capacity of MP gels were influenced by type of oils, the nature of the interfacial membrane, and the size of emulsion droplets.     

Evaluation of sodium alginate and glucono-δ-lactone levels on the cold-set gelation of porcine myofibrillar proteins at different salt concentrations

This study investigated the effects of sodium alginate (SA) and glucono-δ-lactone (GdL) levels on the cold-set gelation of porcine myofibrillar protein (MP) at different salt concentrations. The addition of GdL at 0.1 M salt concentration had no effects on cold-set MP gelation, and GdL level higher than 1% was necessary at 0.3 M salt concentration to form a MP gel. The SA system with 0.5% GdL showed an effect on MP gelation at 0.1 M salt, while SA with 1.5% GdL could be form a cold-set MP gel at 0.3 M salt level. The endothermic peaks were reduced or completely disappeared by the addition of GdL more than 1%. These results indicated that the SA was favorable in forming a cold-set MP gel under low salt concentrations (<0.1 M), and that the SA could be applicable at higher salt concentrations by combining with the GdL level more than 1% (>1%).     

Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation

The effects of freeze–thaw cycles (FT, 0, 1, 3 and 5 times) on protein functional properties of porcine longissimus muscle were investigated. FT increased gapping between muscle fibres and tore muscle fiber bundles. Myofibrillar protein (MP) isolated from FT muscle showed an increased hydrophobicity (P < 0.05), reduced thermal transition temperatures (T_max) and enthalpy of denaturation (ΔH) (P < 0.05), and enhanced susceptibility to thermal aggregation. These structural changes resulted in major losses in protein functionalities, e.g., 41–43% reductions (P < 0.05) in MP emulsifying capacity and emulsion stability after five FT cycles. The ability of MP to form a viscoelastic gel network, as analyzed by small-strain oscillatory rheological testing, also attenuated with FT cycles. The FT process lowered (P < 0.05) water-holding capacity (WHC), whiteness, and texture (hardness, springiness, chewiness and cohesiveness) of MP gels. Overall, repeated FT had a detrimental effect on the general functionality of porcine MP, and protein denaturation and aggregation were implicated in the functionality losses.     

Color improvement by titanium dioxide and its effect on gelation and texture of proteins recovered from whole fish using isoelectric solubilization/precipitation

Whiteness is a critical attribute for restructured fish products such as surimi seafood. However, the whiteness of gels made from proteins recovered from fish processing by-products or whole fish using isoelectric solubilization/precipitation is poor. The by-products and whole fish contain bones, scales, skin, etc. that affect gel color. Therefore, whiteness needs to be improved if marketable products are to be developed from recovered proteins. The objectives of this study were to determine effects of titanium dioxide (TiO₂) on: (1) color; (2) texture; and (3) viscoelasticity (G′) of gels made from isolated carp proteins and Alaska pollock surimi. Carp proteins were recovered with isoelectric solubilization/precipitation. TiO₂ was added to carp proteins at 0-0.5 g/100 g. TiO₂ was not added to surimi. Due to much higher (P < 0.05) yellowness (b^∗) and lower (P < 0.05) lightness (L^∗), the whiteness of carp gels without TiO₂ was lower (P < 0.05) than surimi gels. TiO₂ at ≥ 0.2 g/100 g resulted in better (P < 0.05) whiteness of carp gels than surimi gels without chalky and artificially white appearance. TiO₂ did not affect texture or viscoelasticity. This research demonstrates that whiteness of restructured fish products based on proteins recovered from whole fish via isoelectric solubilization/precipitation can be similar to the whiteness of surimi seafood.     

Hydroxyl Radical and Ferryl-Generating Systems Promote Gel Network Formation of Myofibrillar Protein

ABSTRACT: The objective of the study was to examine how oxidatively induced protein cross-linking would influence the gelation properties of myofibrillar protein (MP) under meat processing conditions. MP suspensions in 0.6 M NaCl at pH 6 were treated with an iron-catalyzed oxidizing system (IOS: 10 μM FeCl₃, 0.1 mM ascorbic acid, 0.05 to 5 mM H₂O₂) or a H₂O₂-activated metmyoglobin oxidizing system (MOS: 0.01 to 0.1 mM metmyoglobin/H₂O₂) that produced hydroxyl radical and ferryl species, respectively. Both oxidizing systems promoted MP thermal gelation, which was evidenced by rapid protein–protein interaction and the enhancement in storage modulus (elasticity) of the gel network as revealed by dynamic rheological testing in the 20 to 74 °C temperature range. This gelation-enhancing effect was attributed to the shift of myosin aggregation in the early stage of heating from predominantly head–head association (nonoxidized control samples) to prevalently tail–tail cross-linking through disulfide bonds. However, both hardness and water-holding capacity of chilled gels tended to decline when MP was exposed to ≥1 mM H₂O₂ in IOS and to all concentrations of metmyoglobin in MOS. Microscopic examination confirmed a more porous structure in oxidized gels when compared with nonoxidized protein gels. The results demonstrated that mild oxidation altered the mode of myosin aggregation in favor of an elastic gel network formation, but it did not improve or had a negative effect on water-binding properties of MP gels. Practical Application: Mild oxidation promotes protein network formation and enhances gelation of myofibrillar protein under normal salt and pH conditions used in meat processing. This oxidative effect, which involves disulfide linkages, is somewhat similar to that in bakery product processing where oxidants are used to improve dough performance through gluten protein interaction.     

Development and validation of analytical methods for ethyl carbamate in various fermented foods

The aim of this work was to develop and validate analytical methods for ethyl carbamate (EC) in various food matrices. Column chromatography was used for the analysis of EC in kimchi, a fermented soybean paste (doenjang), a fermented fish product (jeotgal), yoghurt, bread, and cheese. To remove the fat in the bread and cheese, a Florisil cartridge was selected. The volume of dichloromethane in the chromatography column was optimised to 60 mL for the kimchi, cheese, and fermented soybean paste. For the bread, jeotgal, and yoghurt, the best recovery rate was found by using 100 mL of dichloromethane. For the accurate analysis of EC in the vinegar, 150 mL of dichloromethane and a neutralisation process (pH = 8.0) were required. In the standard curve of EC, satisfactory linearity (R² = 0.998) was shown. The limit of quantification (LOQ) was 10 ng/mL and the recovery rates ranged from 76.9% to 118.1%. Intra- and inter-assay precision ranged from 3.5% to 34.2% and 3.8% to 41.9%, respectively.     

Physical properties of yoghurt manufactured with milk whey and transglutaminase

The effect of milk protein polymerization prior to the yoghurt fermentation process was evaluated by enzymatic reaction with microbial transglutaminase (Streptoverticillium mobaraense). Yoghurt samples were manufactured with 100% milk or by substituting milk with 20 or 30% of liquid milk whey, aimed at determining the use of natural milk whey in dairy products. Transglutaminase was added at a protein ratio of 0.5 U g⁻¹ to all samples and evaluated regarding rheological behavior, syneresis index and texture profile. The addition of enzyme transglutaminase contributed to syneresis prevention and increased the consistency index in yoghurt samples manufactured with milk whey. Yoghurt manufactured from 70% milk plus 20% milk whey, followed by enzymatic treatment, presented similar characteristics to traditionally manufactured yoghurt (C 100), with no alteration in the syneresis of the samples (p > 0.05) and presented texture parameters similar to the control yoghurt (C 100).     

Fermentative behavior of Saccharomyces strains during microvinification of raspberry juice (Rubus idaeus L.)

Sixteen different strains of Saccharomyces cerevisiae and Saccharomyces bayanus were evaluated in the production of raspberry fruit wine. Raspberry juice sugar concentrations were adjusted to 16°Brix with a sucrose solution, and batch fermentations were performed at 22 °C. Various kinetic parameters, such as the conversion factors of the substrates into ethanol (Y_p/s), biomass (Y_x/s), glycerol (Y_g/s) and acetic acid (Y_ac/s), the volumetric productivity of ethanol (Q_p), the biomass productivity (P_x), and the fermentation efficiency (E_f) were calculated. Volatile compounds (alcohols, ethyl esters, acetates of higher alcohols and volatile fatty acids) were determined by gas chromatography (GC-FID). The highest values for the E_f, Y_p/s, Y_g/s, and Y_x/s parameters were obtained when strains commonly used in the fuel ethanol industry (S. cerevisiae PE-2, BG, SA, CAT-1, and VR-1) were used to ferment raspberry juice. S. cerevisiae strain UFLA FW 15, isolated from fruit, displayed similar results. Twenty-one volatile compounds were identified in raspberry wines. The highest concentrations of total volatile compounds were found in wines produced with S. cerevisiae strains UFLA FW 15 (87,435 μg/L), CAT-1 (80,317.01 μg/L), VR-1 (67,573.99 μg/L) and S. bayanus CBS 1505 (71,660.32 μg/L). The highest concentrations of ethyl esters were 454.33 μg/L, 440.33 μg/L and 438 μg/L for S. cerevisiae strains UFLA FW 15, VR-1 and BG, respectively. Similar to concentrations of ethyl esters, the highest concentrations of acetates (1927.67 μg/L) and higher alcohols (83,996.33 μg/L) were produced in raspberry wine from S. cerevisiae UFLA FW 15. The maximum concentration of volatile fatty acids was found in raspberry wine produced by S. cerevisiae strain VR-1. We conclude that S. cerevisiae strain UFLA FW 15 fermented raspberry juice and produced a fruit wine with low concentrations of acids and high concentrations of acetates, higher alcohols and ethyl esters.     

The effect of high pressure and residual oxygen on the color stability of minced cured restructured ham at different levels of drying,pH, and NaCl

Color stability of minced cured restructured ham was studied by considering the effects of high pressure (HP) (600 MPa, 13 °C, 5 min), raw meat pH₂₄ (low, normal, high), salt content (15, 30 g/kg), drying (20%, 50% weight loss), and residual oxygen level (0.02%–0.30%). Raw hams were selected by pH₂₄ in Semimembranosus, mixed with additives, frozen, sliced, and dried by the Quick-Dry-Slice® (QDS) process followed by HP treatment or not (control). Packaging and storage simulated industrial packaging: modified atmosphere containing 80% N₂, 20% CO₂, and residual O₂ in one of three intervals: < 0.1%, 0.1%–0.2%, or 0.2%–0.3%, and retail storage conditions: chill storage, 12 h light, 12 h darkness. HP improved the stability of the redness of 20% QDS hams, while the stabilizing effect on 50% QDS hams was smaller, concluding that water has the dominating role. Raw meat pH₂₄, salt content, and residual oxygen level had varying effects on the stability of the red color.     

Survival of probiotics encapsulated in chitosan-coated alginate beads in yoghurt from UHT- and conventionally treated milk during storage

Survival of the microencapsulated probiotics, Lactobacillus acidophilus 547, Bifidobacterium bifidum ATCC 1994, and Lactobacillus casei 01, in stirred yoghurt from UHT- and conventionally treated milk during low temperature storage was investigated. The probiotic cells both as free cells and microencapsulated cells (in alginate beads coated with chitosan) were added into 20 g/100 g total solids stirred yoghurt from UHT-treated milk and 16 g/100 g total solids yoghurt from conventionally treated milk after 3.5 h of fermentation. The products were kept at 4 °C for 4 weeks. The survival of encapsulated probiotic bacteria was higher than free cells by approximately 1 log cycle. The number of probiotic bacteria was maintained above the recommended therapeutic minimum (10⁷ cfu g⁻¹) throughout the storage except for B. bifidum. The viabilities of probiotic bacteria in yoghurts from both UHT- and conventionally treated milks were not significantly (P>0.05) different.