Alline Artigiani Lima Tribst

Review: Microbiological quality and safety of fruit juices--past, present and future perspectives.

In this review paper, several aspects of fruit juice microbiology, from past to future perspectives, are considered. An overview of the most relevant outbreaks involving foodborne pathogens and spoilage microorganisms associated with fruit juices is provided. One of the sections provides data on the sources of fruit juice contamination, followed by perspectives on preservation methods. Furthermore, considerations on the role of international guidelines about exotic fruit juices in respect to public health, and of the microbiological status of fruit juices used as food/beverage ingredients are discussed. Issues and challenges highlight how the microbiology of fruit juices has evolved over the years, when aspects of stability or microbiological safety are under consideration.In this review paper, several aspects of fruit juice microbiology, from past to future perspectives, are considered. An overview of the most relevant outbreaks involving foodborne pathogens and spoilage microorganisms associated with fruit juices is provided. One of the sections provides data on the sources of fruit juice contamination, followed by perspectives on preservation methods. Furthermore, considerations on the role of international guidelines about exotic fruit juices in respect to public health, and of the microbiological status of fruit juices used as food/beverage ingredients are discussed. Issues and challenges highlight how the microbiology of fruit juices has evolved over the years, when aspects of stability or microbiological safety are under consideration.

Quality of Mango Nectar Processed by High‐Pressure Homogenization with Optimized Heat Treatment

UNLABELLEDnThis work aimed to evaluate the effect of high-pressure homogenization (HPH) with heat shock on Aspergillus niger, vitamin C, and color of mango nectar. The nectar was processed at 200 MPa followed by heat shock, which was optimized by response surface methodology by using mango nectar ratio (45 to 70), heat time (10 to 20), and temperature (60 to 85 °C) as variables. The color of mango nectar and vitamin C retention were evaluated at the optimized treatments, that is, 200 MPa + 61.5 °C/20 min or 73.5 °C/10 min. The mathematical model indicates that heat shock time and temperature showed a positive effect in the mould inactivation, whereas increasing ratio resulted in a protective effect on A. niger. The optimized treatments did not increase the retention of vitamin C, but had positive effect for the nectar color, in particular for samples treated at 200 MPa + 61.5 °C/20 min.nnnPRACTICAL APPLICATIONnThe results obtained in this study show that the conidia can be inactivated by applying HPH with heat shock, particularly to apply HPH as an option to pasteurize fruit nectar for industries.

Inactivation of Aspergillus niger in mango nectar by high-pressure homogenization combined with heat shock.

This research evaluated the inactivation of a heat-resistant Aspergillus niger conidia in mango nectar by high-pressure homogenization (HPH) combined with heat shock. A. niger were inoculated in mango nectar (10(6) conidia mL(-1)) and subjected to HPH (300 to 100 MPa) and heat shock (80 degrees C for 5 to 20 min) before or after HPH. Processes were evaluated according to number of decimal reductions reached by each isolated or combined process. Scanning electron microscopy was performed to observe conidia wall after pressure treatment. Pressures below 150 MPa did not inactivate A. niger while pressures of 200 and 300 MPa resulted in 2 and more than 6 log reductions, respectively. D(80 degrees C) of A. niger was determined as 5.03 min. A heat shock of 80 degrees C/15 min, reaching 3 decimal conidia reductions, was applied before or after a 200 MPa pressure treatment to improve the decimal reduction to 5 log cycles. Results indicated that HPH inactivated A. niger in mango nectar at 300 MPa (>6.24 log cycles) and that, with pressure (200 MPa) combined with post heat shock, it was possible to obtain the same decimal reduction, showing a synergistic effect. On the other hand, pre heat shock associated with HPH resulted in an additive effect. The observation of A. niger conidia treated by HPH at 100 and 200 MPa by scanning electron microscopy indicated that HPH promoted intense cell wall damage, which can sensitize the conidia to post heat shock and possibly explain the synergistic effect observed. Practical Application: The results obtained in this paper are relevant to elucidate the mechanism of conidia inactivation in order to develop the application of HPH as an alternative pasteurization process for the fruit nectar industry.

The effect of high pressure homogenization on the activity of a commercial β-galactosidase

High pressure homogenization (HPH) has been proposed as a promising method for changing the activity and stability of enzymes. Therefore, this research studied the activity of β-galactosidase before and after HPH. The enzyme solution at pH values of 6.4, 7.0, and 8.0 was processed at pressures of up to 150xa0MPa, and the effects of HPH were determined from the residual enzyme activity measured at 5, 30, and 45xa0°C immediately after homogenization and after 1xa0day of refrigerated storage. The results indicated that at neutral pH the enzyme remained active at 30xa0°C (optimum temperature) even after homogenization at pressures of up to 150xa0MPa. On the contrary, when the β-galactosidase was homogenized at pH 6.4 and 8.0, a gradual loss of activity was observed, reaching a minimum activity (around 30xa0%) after HPH at 150xa0MPa and pH 8.0. After storage, only β-galactosidase that underwent HPH at pH 7.0 retained similar activity to the native sample. Thus, HPH did not affect the activity and stability of β-galactosidase only when the process was carried out at neutral pH; for the other conditions, HPH resulted in partial inactivation of the enzyme. Considering the use of β-galactosidase to produce low lactose milk, it was concluded that HPH can be applied with no deleterious effects on enzyme activity.

Evaluation of methodologies for mathematical modeling of packaged conductive foods heat process.

The heat process is a safe method of food preservation. The use of mathematical modeling for heat transfer by finite elements analysis (FEA) makes it possible to determine the cold spot of conventional and non conventional packages, evaluate their thermal history, microbial and enzyme inactivation and nutrients retention for an optimum process design. Several works use simplifications during mathematical modeling, such as adiabatic headspace, considering the thermal resistance of package negligible. The impact of these simplifications is rarely evaluated. The aim of the present work was to evaluate the effect of these simplifications on sterilization value (Fp) for a conductive food. Two commercial glass bottles (G1 and G2) were selected for the assays. FEA model was built using the bottles real geometries. Three methodologies were evaluated, considering (i) the four components of the system, i.e., product, glass wall, headspace and metal cap, and uniform heating (PGHM); (ii) adiabatic headspace, i.e., a model considering product and glass wall, with its upper side adiabatic (PG); and (iii) only product, with adiabatic upper side (P). A tomato concentrate industrial pasteurizator profile was used as boundary condition. The Fp was determined by using two values of thermal coefficient (z), 5.5ºC and 12.5ºC, representing a possible range of contaminantx92s z-value. The cold spot of the two packages was located at 32% (G1) and 46% (G2) of the product height. For the same process, the differences of Fp for the two packages ranged between 62 and 320%. Comparing the Fp by PGHM and PG models, differences were observed between 4 and 13%. These differences were over 45% when comparing PGHM with P models, even with similar thermal history. The results indicated the importance of the previous evaluation of the impact of each simplification on the accuracy of the model. Due to exponential relationship between temperature and reactions during the heat process, the need for Fp evaluation instead of thermal history in conductive food was confirmed.

Effects of high pressure homogenization on the activity, stability, kinetics and three-dimensional conformation of a glucose oxidase produced by Aspergillus niger.

High pressure homogenization (HPH) is a non-thermal method, which has been employed to change the activity and stability of biotechnologically relevant enzymes. This work investigated how HPH affects the structural and functional characteristics of a glucose oxidase (GO) from Aspergillus niger. The enzyme was homogenized at 75 and 150 MPa and the effects were evaluated with respect to the enzyme activity, stability, kinetic parameters and molecular structure. The enzyme showed a pH-dependent response to the HPH treatment, with reduction or maintenance of activity at pH 4.5–6.0 and a remarkable activity increase (30–300%) at pH 6.5 in all tested temperatures (15, 50 and 75°C). The enzyme thermal tolerance was reduced due to HPH treatment and the storage for 24 h at high temperatures (50 and 75°C) also caused a reduction of activity. Interestingly, at lower temperatures (15°C) the activity levels were slightly higher than that observed for native enzyme or at least maintained. These effects of HPH treatment on function and stability of GO were further investigated by spectroscopic methods. Both fluorescence and circular dichroism revealed conformational changes in the molecular structure of the enzyme that might be associated with the distinct functional and stability behavior of GO.

Thermal Inactivation of Alicyclobacillus acidoterrestris in a Model Food

Thermal process is among the safer and most used food preservation technique. The utilization of model foods in thermal processes studies has several advantages, and the determination of microorganisms thermal inactivation kinetics in model foods is extremely interesting for studying thermal processes and heat transfer. This work has determined the thermal inactivation kinetics of Alicyclobacillus acidoterretris in a liquid model food, thus providing subsidies for thermal process studies and design. The A. acidoterretris thermal inactivation was determined through the three-neck flask method, and was well described according to a first order kinetics. The D85°C, D88°C, D92°C and D95°C values were 105.4 min, 2.75 min, 7.0 min and 2.3 min, respectively. The observed z-value was 6.1°C. Due to the lack of such data in literature, the obtained results contribute to future studies on food thermal processes.

High Pressure Homogenization of Porcine Pepsin Protease: Effects on Enzyme Activity, Stability, Milk Coagulation Profile and Gel Development.

This study investigated the effect of high pressure homogenization (HPH) (up to 190 MPa) on porcine pepsin (proteolytic and milk-clotting activities), and the consequences of using the processed enzyme in milk coagulation and gel formation (rheological profile, proteolysis, syneresis, and microstructure). Although the proteolytic activity (PA) was not altered immediately after the HPH process, it reduced during enzyme storage, with a 5% decrease after 60 days of storage for samples obtained with the enzyme processed at 50, 100 and 150 MPa. HPH increased the milk-clotting activity (MCA) of the enzyme processed at 150 MPa, being 15% higher than the MCA of non-processed samples after 60 days of storage. The enzyme processed at 150 MPa produced faster aggregation and a more consistent milk gel (G’ value 92% higher after 90 minutes) when compared with the non-processed enzyme. In addition, the gels produced with the enzyme processed at 150 MPa showed greater syneresis after 40 minutes of coagulation (forming a more compact protein network) and lower porosity (evidenced by confocal microscopy). These effects on the milk gel can be associated with the increment in MCA and reduction in PA caused by the effects of HPH on pepsin during storage. According to the results, HPH stands out as a process capable of changing the proteolytic characteristics of porcine pepsin, with improvements on the milk coagulation step and gel characteristics. Therefore, the porcine pepsin submitted to HPH process can be a suitable alternative for the production of cheese.

Effect of High-Pressure Technologies on Enzymes Applied in Food Processing

High isostatic pressure (HIP) and high-pressure homogenization (HPH) are considered important physical technologies that able to induce changes on enzymes. HIP and HPH are emerging food processing technologies that involve the use of ultra high pressures (up to 1200 MPa for HIP and up to 400 MPa for HPH), where the first process is based on the principle that the maintenance of a product inside vessels at high pressures induces changes in the molecules conformation and, consequently, in the functionality of polysaccharides, proteins and enzymes. To the contrary, for HPH process, the high shear and sudden pressure drop are the responsible phenomena for the changes on the processed product. This chapter aims to evaluate comparatively the effects of HIP and HPH on the activity of enzymes currently applied in food industry and to identify the main structural changes induced by each process. The overall evaluation of the results shows that mild conditions of both processes were recently highlighted as able to improve the activity and the stability of several enzymes, whereas extreme process conditions (pressure, time and temperature) induce enzyme denaturation with consequent reduction of biological activity. Considering the complexity and diversity involved in the enzyme structure and its ability to react, it is not possible to determine specific conditions that each process is able to promote increase or reduction of enzyme activity, being necessary to evaluate HIP and HPH for each enzyme. Finally, in terms of molecular structure, the effect of HIP and HPH on enzymes can be explained by the alterations in the quaternary, tertiary and secondary structures of enzymes, which directly affects its active site configuration.

Biophysical evaluation of milk-clotting enzymes processed by high pressure

High pressure processing (HPP) is able to promote changes in enzymes structure. This study evaluated the effect of HP on the structural changes in milk-clotting enzymes processed under activation conditions for recombinant camel chymosin (212MPa/5min/10°C), calf rennet (280MPa/20min/25°C), bovine rennet (222MPa/5min/23°C), and porcine pepsin (50MPa/5min/20°C) and under inactivation conditions for all enzymes (600MPa/10min/25°C) including the protease from Rhizomucor miehei. In general, it was found that the HPP at activation conditions was able to increase the intrinsic fluorescence of samples with high pepsin concentration (porcine pepsin and bovine rennet), increase significantly the surface hydrophobicity and induce changes in secondary structure of all enzymes. Under inactivation conditions, increases in surface hydrophobicity and a reduction of intrinsic fluorescence were observed, suggesting a higher exposure of hydrophobic sites followed by water quenching of Trp residues. Moreover, changes in secondary structure were observed (with minor changes seen in Rhizomucor miehei protease). In conclusion, HPP was able to unfold milk-clotting enzymes even under activation conditions, and the porcine pepsin and bovine rennet were more sensitive to HPP.