Thermal Stability of Fructooligosaccharides Extracted from Defatted Rice Bran: A Kinetic Study Using Liquid Chromatography-Tandem Mass Spectrometry.

Thermal degradation kinetics of fructooligosaccharides (FOS) in defatted rice bran were studied at temperatures of 90, 100, and 110 °C. FOS extracted from rice bran and dissolved in buffers at pH values of 5.0, 6.0, and 7.0 were prepared for the thermal treatments. The residual FOS (including 1-kestose (GF2), nystose (GF3), and 1F-fructofuranosylnystose (GF4)) contents were determined using the ultra-performance liquid chromatography-electrospray ionization-tandem mass spectrometry (UPLC-ESI-MS/MS) method. The results showed that the thermal degradation kinetics of GF2, GF3, and GF4 followed a first-order kinetic model. Thermal degradation rate constants (k values) of GF2, GF3, and GF4 at different temperature and pH values were estimated using the first-order kinetic equation and SAS 9.1. As a result, these k values decreased gradually as the pH of the sample increased from 5.0 to 7.0. The Arrhenius model was applied to describe the heat dependence of the k-values. The activation energy (Ea) was calculated for each case of GF2, GF3, and GF4 degradation at pH values of 5.0, 6.0, and 7.0. The result showed that rice bran FOS is very thermostable at neutral pH while more labile at acidic pH.

Quality of Set Yogurts Made from Raw Milk and Processed Milk Supplemented with Enriched Milk Fat Globule Membrane in a Two-Stage Homogenization Process.

Dairy products are relevant in the food industries as functional ingredients for several food products and contribute towards human nutrition in ameliorating certain disorders. In this study, set yogurts were produced from raw milk and processed milk combined with 4% Lacprodan®PL20 concentration and subjected to two-stage pressure homogenization. The total solids concentration of the mixture was raised to 15% using SMP (skim milk powder). The purpose of this study was to investigate the effect of Lacprodan®PL20 on the set yogurt quality produced by homogenization-induced pressure and its interaction with milk components. The changes in the physical and chemical attributes of the milk fat globule membrane (MFGM) via destabilization of the membrane significantly affected the physicochemical properties of set yogurts produced from processed or raw milk. There was a slight variation in MFGM-specific proteins detected in the set yogurts. Set yogurt produced from homogenized raw milk (HRM) had a considerably higher water-holding capacity, firmness, and apparent viscosity. The microstructure of HRM was dense and compacted, unlike non-homogenized raw milk (NRM) with large MFGM fragments and pore holes between the matrixes. The inclusion of homogenization showed a remarkable improvement in set yogurt quality, promoting interaction between MFGM components and milk proteins.

Decontamination of Pangasius fish (Pangasius hypophthalmus) with chlorine or peracetic acid in the laboratory and in a Vietnamese processing company.

This study evaluated the decontamination of Pangasius fillets in chlorine or peracetic acid treated wash water. First, the decontamination efficacy of the washing step with chlorinated water applied by a Vietnamese processing company during trimming of Pangasius fillets was evaluated and used as the basis for the experiments performed on a laboratory scale. As chlorine was only added at the beginning of the batch and used continuously without renewal for 239min; a rapid increase of the bacterial counts and a fast decrease of chlorine in the wash water were found. This could be explained by the rapid accumulation of organic matter (ca. 400mg O2/L of COD after only 24min). Secondly, for the experiments performed on a laboratory scale, a single batch approach (one batch of wash water for treating a fillet) was used. Chlorine and PAA were evaluated at 10, 20, 50 and 150ppm at contact times of 10, 20 and 240s. Washing with chlorine and PAA wash water resulted in a reduction of Escherichia coli on Pangasius fish which ranged from 0-1.0 and 0.4-1.4logCFU/g, respectively while less to no reduction of total psychrotrophic counts, lactic acid bacteria and coliforms on Pangasius fish was observed. However, in comparison to PAA, chlorine was lost rapidly. As an example, 53-83% of chlorine and 15-17% of PAA were lost after washing for 40s (COD=238.2±66.3mg O2/L). Peracetic acid can therefore be an alternative sanitizer. However, its higher cost will have to be taken into consideration. Where (cheaper) chlorine is used, the processors have to pay close attention to the residual chlorine level, pH and COD level during treatment for optimal efficacy.

Effect of intrinsic and extrinsic factors on the interaction of plant pectin methylesterase and its proteinaceous inhibitor from kiwi fruit.

A proteinaceous pectin methylesterase inhibitor (PMEI) was isolated from kiwi fruit (Actinidia chinensiscv. Hayward) and purified by affinity chromatography on a cyanogen bromide (CNBr) Sepharose 4B-orange PME column. The optimal pH of banana PME activity was 7.0, whereas that for carrot and strawberry PME activity was 9.0. The optimal pH for the binding between kiwi fruit PMEI and these PMEs was 7.0. The kiwi fruit PMEI has a different affinity for PME depending on the plant source. The inhibition kinetics of kiwi fruit PMEI to banana and strawberry PME followed a noncompetitive type, whereas that to carrot PME followed a competitive type. The kiwi fruit PMEI was mixed with banana, carrot, and strawberry PME to obtain PMEI-PME complexes, which were then subjected to thermal (40-80 degrees C, atmospheric pressure) or high-pressure (10 degrees C, 100-600 MPa) treatment. Experimental data showed that the PMEI-PME complexes were easily dissociated by both thermal and high-pressure treatments.

Inactivation kinetics of purified tomato polygalacturonase by thermal and high-pressure processing.

Tomato polygalacturonase (PG) was extracted from ripe tomatoes and purified by cation exchange and gel filtration chromatography. Cation exchange chromatography yielded two peaks with PG activity: the first peak was identified as PG2 (the heat labile form) and the second one as PG1 (the heat stable form). Both PG2 and PG1 presented a molar mass of 42 kDa when analyzed by SDS-PAGE and an isoelectric point >9.3. Thermal inactivation of purified tomato PG2, at pH 4.4, in the temperature range from 53 to 63 degrees C, followed first-order kinetics. Combined pressure-temperature inactivation of tomato PG2 was studied at 5-55 degrees C/100-600MPa. Under all pressure-temperature conditions, PG2 inactivation followed first-order kinetics. Purified tomato PG1, although more thermostable than PG2, showed a pressure stability very similar to that of PG2. These results indicate that high-pressure processing is an efficient alternative to inactivate tomato PG without the need for applying high temperatures.

Effect of mild-heat and high-pressure processing on banana pectin methylesterase: a kinetic study.

Pectin methylesterase (PME) was extracted from bananas and purified by affinity chromatography. The thermal-high-pressure inactivation (at moderate temperature, 30-76 degrees C, in combination with high pressure, 0.1-900 MPa) of PME was investigated in a model system at pH 7.0. Under these conditions, the stable fraction was not inactivated and isobaric-isothermal inactivation followed a fractional-conversion model. At lower pressure (< or =300-400 MPa) and higher temperature (> or =64 degrees C), an antagonistic effect of pressure and heat was observed. Third-degree polynomial models (derived from the thermodynamic model) were successfully used to describe the heat-pressure dependence of the inactivation rate constants.

Strawberry pectin methylesterase (PME): purification, characterization, thermal and high-pressure inactivation.

Pectin methylesterase (PME) was extracted from strawberries (Fragaria ananassa, cv Elsanta) and purified by affinity chromatography on a CNBr-Sepharose 4B-PME-inhibitor column. A single protein and PME activity peak was obtained. A biochemical characterization in terms of molecular mass, pI, and kinetic parameters of strawberry PME was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal and combined isothermal-isobaric inactivation of purified strawberry PME could be described by a fractional-conversion model. Purified strawberry PME is much more stable toward high-pressure treatments in comparison to those from oranges and bananas.

Partial purification, characterization, and thermal and high-pressure inactivation of pectin methylesterase from carrots (Daucus carrota L.).

Pectin methylesterase (PME) from carrots (Daucus carrota L.) was extracted and purified by affinity chromatography on a CNBr-Sepharose 4B-PME inhibitor column. A single protein and PME activity peak was obtained. A biochemical characterization in terms of molar mass (MM), isoelectric points (pI), and kinetic parameters of carrot PME was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal and combined isothermal-isobaric inactivation of purified carrot PME could be described by a fractional-conversion model.

Comparative study of the inactivation kinetics of pectinmethylesterase in tomato juice and purified form.

Pectinmethylesterase (PME) extracted from tomato fruit was purified by affinity chromatography. A single peak of PME activity was observed, presenting a molar mass of 33.6 kDa, an isoelectric point higher than 9.3, and an optimal temperature and pH for activity of 55 degrees C and 8.0, respectively. The processing stability of purified tomato PME in buffer solution was compared to PME stability in tomato juice. In both media, thermal inactivation of PME presented first-order inactivation kinetics, PME in tomato juice being more heat-labile than purified PME. Regarding high-pressure treatment, tomato PME showed to be very pressure-resistant, revealing an outspoken antagonistic effect of temperature and pressure. To avoid cloud loss in tomato juice, a time-temperature treatment of 1 min at 76.5 degrees C was calculated in order to have a residual PME activity of 1 x 10(-)(4) U/mL.