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Emulsions form a major part of processed food formulations, either being the end products in themselves or as parts of a more complex food system. For the past few decades, colloid scientists have focussed mainly on the effects of processing conditions (e.g. heat, high pressure, and shear) on the physicochemical properties of emulsions (e.g. viscosity, droplet size distribution and phase stability). However, the information about the behaviour of food structures post consumption is very limited. Fundamental knowledge of how the food structures behave in the mouth is critical, as these oral interactions of food components influence the common sensorial perceptions (e.g. creaminess, smoothness) and the release of fat-soluble flavours. Initial studies also suggest that the breakdown of emulsions in the gastrointestinal tract and the generated interfacial structures impact lipid digestion, which can consequently influence post-prandial metabolic responses. This area of research needs to be intensively investigated before the knowledge can be applied to rational design of healthier food structures that could modulate the rate of lipid metabolism, bioavailability of nutrients, and also help in providing targeted delivery of flavour molecules and/or bioactive components. Hence, the objective of this research was to gain understanding of how emulsions behave during their passage through the gastrointestinal tract. In vitro digestion models that mimic the physicochemical processes and biological conditions in the mouth and gastrointestinal tract were successfully employed. Behaviour of model protein-stabilized emulsions (both positively charged (lactoferrin) as well as negatively charged [β-lactoglobulin (β-lg)] oil-in-water emulsions) at each step of simulated physiological processing (using model oral, gastric and duodenal fluids individually) were investigated. In simulated mouth conditions, oil-in-water emulsions stabilized by lactoferrin or β-lg at the interfacial layers were mixed with artificial saliva at neutral pH that contained a range of mucin concentrations and salts. The β-lg emulsions did not interact with the artificial saliva due to the dominant repulsion between mutually opposite charges of anionic mucin and anionic β-lg interfacial layer at neutral pH. However, β-lg emulsions underwent some depletion flocculation on addition of higher concentrations of mucin due to the presence of unadsorbed mucin molecules in the continuous phase. In contrast, positively charged lactoferrin emulsions showed considerable salt-induced aggregation in the presence of salts (from the saliva) alone. Furthermore, lactoferrin emulsions underwent bridging flocculation because of electrostatic binding of anionic mucin to the positively charged lactoferrin-stabilized emulsion droplets. In acidic pH conditions (pH 1.2) of the simulated gastric fluid (SGF), both protein-stabilized emulsions were positively charged. Addition of pepsin resulted in extensive droplet flocculation in both emulsions with a greater extent of droplet instability in lactoferrin emulsions. Coalescence of the droplets was observed as a result of peptic hydrolysis of the interfacial protein layers. Conditions such as ionic strength, pH and exposure to mucin were shown to significantly influence the rate of hydrolysis of β-lg-stabilized emulsion by pepsin. Addition of simulated intestinal fluid (SIF) containing physiological concentrations of bile salts to the emulsions showed competitive interfacial displacement of β-lg by bile salts. In the case of lactoferrin-stabilized emulsion droplets, there was considerable aggregation in the presence of intestinal electrolytes alone (without added bile salts) at pH 7.5. Binding of anionic bile salts to cationic interfacial lactoferrin layer resulted in re-stabilization of salt-aggregated lactoferrin emulsions. On mixing with physiological concentrations of pancreatin (mixture of pancreatic lipase, amylase and protease), significant degree of coalescence and fatty acid release occurred for both the emulsions. This was attributed to the interfacial proteolysis by trypsin (proteolytic fractions of pancreatin) resulting in interfacial film rupturing. Exchange of initial interfacial materials by bile salts and trypsin-induced film breakage enhanced the potential for lipolytic fractions of pancreatin to act on the hydrophobic lipid core. The lipid digestion products (free fatty acids and mono and/or diglycerides) generated at the droplet surface further removed the residual intact protein layers from the interface by competitive displacement mechanisms. The sequential treatment of the cationic and anionic emulsions with artificial saliva, SGF and SIF, respectively, was determined to understand the impact of initial protein type during complete physiological processing from mouth to intestine. Broadly, both the protein-stabilized emulsions underwent charge reversals, extensive droplet flocculation, and significant coalescence as they passed through various stages of the in vitro digestion conditions. Except in the simulated mouth environment, the initial charge of the emulsifiers had relatively limited influence on droplet behaviour during the simulated digestion. The results contribute to the knowledge of how structure and charge of the emulsified lipid droplets impact digestion at various stages of physiology. This information might have important consequences for developing suitable microstructures that allow controlled breakdown of droplets in the mouth and predictable release of lipids in the gastrointestinal tract.

Emulsions form a major part of processed food formulations, either being the end products in themselves or as parts of a more complex food system. For the past few decades, colloid scientists have focussed mainly on the effects of processing conditions (e.g. heat, high pressure, and shear) on the physicochemical properties of emulsions (e.g. viscosity, droplet size distribution and phase stability). However, the information about the behaviour of food structures post consumption is very limited. Fundamental knowledge of how the food structures behave in the mouth is critical, as these oral interactions of food components influence the common sensorial perceptions (e.g. creaminess, smoothness) and the release of fat-soluble flavours. Initial studies also suggest that the breakdown of emulsions in the gastrointestinal tract and the generated interfacial structures impact lipid digestion, which can consequently influence post-prandial metabolic responses. This area of research needs to be intensively investigated before the knowledge can be applied to rational design of healthier food structures that could modulate the rate of lipid metabolism, bioavailability of nutrients, and also help in providing targeted delivery of flavour molecules and/or bioactive components. Hence, the objective of this research was to gain understanding of how emulsions behave during their passage through the gastrointestinal tract. In vitro digestion models that mimic the physicochemical processes and biological conditions in the mouth and gastrointestinal tract were successfully employed. Behaviour of model protein-stabilized emulsions (both positively charged (lactoferrin) as well as negatively charged [β-lactoglobulin (β-lg)] oil-in-water emulsions) at each step of simulated physiological processing (using model oral, gastric and duodenal fluids individually) were investigated. In simulated mouth conditions, oil-in-water emulsions stabilized by lactoferrin or β-lg at the interfacial layers were mixed with artificial saliva at neutral pH that contained a range of mucin concentrations and salts. The β-lg emulsions did not interact with the artificial saliva due to the dominant repulsion between mutually opposite charges of anionic mucin and anionic β-lg interfacial layer at neutral pH. However, β-lg emulsions underwent some depletion flocculation on addition of higher concentrations of mucin due to the presence of unadsorbed mucin molecules in the continuous phase. In contrast, positively charged lactoferrin emulsions showed considerable salt-induced aggregation in the presence of salts (from the saliva) alone. Furthermore, lactoferrin emulsions underwent bridging flocculation because of electrostatic binding of anionic mucin to the positively charged lactoferrin-stabilized emulsion droplets. In acidic pH conditions (pH 1.2) of the simulated gastric fluid (SGF), both protein-stabilized emulsions were positively charged. Addition of pepsin resulted in extensive droplet flocculation in both emulsions with a greater extent of droplet instability in lactoferrin emulsions. Coalescence of the droplets was observed as a result of peptic hydrolysis of the interfacial protein layers. Conditions such as ionic strength, pH and exposure to mucin were shown to significantly influence the rate of hydrolysis of β-lg-stabilized emulsion by pepsin. Addition of simulated intestinal fluid (SIF) containing physiological concentrations of bile salts to the emulsions showed competitive interfacial displacement of β-lg by bile salts. In the case of lactoferrin-stabilized emulsion droplets, there was considerable aggregation in the presence of intestinal electrolytes alone (without added bile salts) at pH 7.5. Binding of anionic bile salts to cationic interfacial lactoferrin layer resulted in re-stabilization of salt-aggregated lactoferrin emulsions. On mixing with physiological concentrations of pancreatin (mixture of pancreatic lipase, amylase and protease), significant degree of coalescence and fatty acid release occurred for both the emulsions. This was attributed to the interfacial proteolysis by trypsin (proteolytic fractions of pancreatin) resulting in interfacial film rupturing. Exchange of initial interfacial materials by bile salts and trypsin-induced film breakage enhanced the potential for lipolytic fractions of pancreatin to act on the hydrophobic lipid core. The lipid digestion products (free fatty acids and mono and/or diglycerides) generated at the droplet surface further removed the residual intact protein layers from the interface by competitive displacement mechanisms. The sequential treatment of the cationic and anionic emulsions with artificial saliva, SGF and SIF, respectively, was determined to understand the impact of initial protein type during complete physiological processing from mouth to intestine. Broadly, both the protein-stabilized emulsions underwent charge reversals, extensive droplet flocculation, and significant coalescence as they passed through various stages of the in vitro digestion conditions. Except in the simulated mouth environment, the initial charge of the emulsifiers had relatively limited influence on droplet behaviour during the simulated digestion. The results contribute to the knowledge of how structure and charge of the emulsified lipid droplets impact digestion at various stages of physiology. This information might have important consequences for developing suitable microstructures that allow controlled breakdown of droplets in the mouth and predictable release of lipids in the gastrointestinal tract.

Emulsions form a major part of processed food formulations, either being the end products in themselves or as parts of a more complex food system. For the past few decades, colloid scientists have focussed mainly on the effects of processing conditions (e.g. heat, high pressure, and shear) on the physicochemical properties of emulsions (e.g. viscosity, droplet size distribution and phase stability). However, the information about the behaviour of food structures post consumption is very limited. Fundamental knowledge of how the food structures behave in the mouth is critical, as these oral interactions of food components influence the common sensorial perceptions (e.g. creaminess, smoothness) and the release of fat-soluble flavours. Initial studies also suggest that the breakdown of emulsions in the gastrointestinal tract and the generated interfacial structures impact lipid digestion, which can consequently influence post-prandial metabolic responses. This area of research needs to be intensively investigated before the knowledge can be applied to rational design of healthier food structures that could modulate the rate of lipid metabolism, bioavailability of nutrients, and also help in providing targeted delivery of flavour molecules and/or bioactive components. Hence, the objective of this research was to gain understanding of how emulsions behave during their passage through the gastrointestinal tract. In vitro digestion models that mimic the physicochemical processes and biological conditions in the mouth and gastrointestinal tract were successfully employed. Behaviour of model protein-stabilized emulsions (both positively charged (lactoferrin) as well as negatively charged [β-lactoglobulin (β-lg)] oil-in-water emulsions) at each step of simulated physiological processing (using model oral, gastric and duodenal fluids individually) were investigated. In simulated mouth conditions, oil-in-water emulsions stabilized by lactoferrin or β-lg at the interfacial layers were mixed with artificial saliva at neutral pH that contained a range of mucin concentrations and salts. The β-lg emulsions did not interact with the artificial saliva due to the dominant repulsion between mutually opposite charges of anionic mucin and anionic β-lg interfacial layer at neutral pH. However, β-lg emulsions underwent some depletion flocculation on addition of higher concentrations of mucin due to the presence of unadsorbed mucin molecules in the continuous phase. In contrast, positively charged lactoferrin emulsions showed considerable salt-induced aggregation in the presence of salts (from the saliva) alone. Furthermore, lactoferrin emulsions underwent bridging flocculation because of electrostatic binding of anionic mucin to the positively charged lactoferrin-stabilized emulsion droplets. In acidic pH conditions (pH 1.2) of the simulated gastric fluid (SGF), both protein-stabilized emulsions were positively charged. Addition of pepsin resulted in extensive droplet flocculation in both emulsions with a greater extent of droplet instability in lactoferrin emulsions. Coalescence of the droplets was observed as a result of peptic hydrolysis of the interfacial protein layers. Conditions such as ionic strength, pH and exposure to mucin were shown to significantly influence the rate of hydrolysis of β-lg-stabilized emulsion by pepsin. Addition of simulated intestinal fluid (SIF) containing physiological concentrations of bile salts to the emulsions showed competitive interfacial displacement of β-lg by bile salts. In the case of lactoferrin-stabilized emulsion droplets, there was considerable aggregation in the presence of intestinal electrolytes alone (without added bile salts) at pH 7.5. Binding of anionic bile salts to cationic interfacial lactoferrin layer resulted in re-stabilization of salt-aggregated lactoferrin emulsions. On mixing with physiological concentrations of pancreatin (mixture of pancreatic lipase, amylase and protease), significant degree of coalescence and fatty acid release occurred for both the emulsions. This was attributed to the interfacial proteolysis by trypsin (proteolytic fractions of pancreatin) resulting in interfacial film rupturing. Exchange of initial interfacial materials by bile salts and trypsin-induced film breakage enhanced the potential for lipolytic fractions of pancreatin to act on the hydrophobic lipid core. The lipid digestion products (free fatty acids and mono and/or diglycerides) generated at the droplet surface further removed the residual intact protein layers from the interface by competitive displacement mechanisms. The sequential treatment of the cationic and anionic emulsions with artificial saliva, SGF and SIF, respectively, was determined to understand the impact of initial protein type during complete physiological processing from mouth to intestine. Broadly, both the protein-stabilized emulsions underwent charge reversals, extensive droplet flocculation, and significant coalescence as they passed through various stages of the in vitro digestion conditions. Except in the simulated mouth environment, the initial charge of the emulsifiers had relatively limited influence on droplet behaviour during the simulated digestion. The results contribute to the knowledge of how structure and charge of the emulsified lipid droplets impact digestion at various stages of physiology. This information might have important consequences for developing suitable microstructures that allow controlled breakdown of droplets in the mouth and predictable release of lipids in the gastrointestinal tract.

Emulsions form a major part of processed food formulations, either being the end products in themselves or as parts of a more complex food system. For the past few decades, colloid scientists have focussed mainly on the effects of processing conditions (e.g. heat, high pressure, and shear) on the physicochemical properties of emulsions (e.g. viscosity, droplet size distribution and phase stability). However, the information about the behaviour of food structures post consumption is very limited. Fundamental knowledge of how the food structures behave in the mouth is critical, as these oral interactions of food components influence the common sensorial perceptions (e.g. creaminess, smoothness) and the release of fat-soluble flavours. Initial studies also suggest that the breakdown of emulsions in the gastrointestinal tract and the generated interfacial structures impact lipid digestion, which can consequently influence post-prandial metabolic responses. This area of research needs to be intensively investigated before the knowledge can be applied to rational design of healthier food structures that could modulate the rate of lipid metabolism, bioavailability of nutrients, and also help in providing targeted delivery of flavour molecules and/or bioactive components. Hence, the objective of this research was to gain understanding of how emulsions behave during their passage through the gastrointestinal tract. In vitro digestion models that mimic the physicochemical processes and biological conditions in the mouth and gastrointestinal tract were successfully employed. Behaviour of model protein-stabilized emulsions (both positively charged (lactoferrin) as well as negatively charged [β-lactoglobulin (β-lg)] oil-in-water emulsions) at each step of simulated physiological processing (using model oral, gastric and duodenal fluids individually) were investigated. In simulated mouth conditions, oil-in-water emulsions stabilized by lactoferrin or β-lg at the interfacial layers were mixed with artificial saliva at neutral pH that contained a range of mucin concentrations and salts. The β-lg emulsions did not interact with the artificial saliva due to the dominant repulsion between mutually opposite charges of anionic mucin and anionic β-lg interfacial layer at neutral pH. However, β-lg emulsions underwent some depletion flocculation on addition of higher concentrations of mucin due to the presence of unadsorbed mucin molecules in the continuous phase. In contrast, positively charged lactoferrin emulsions showed considerable salt-induced aggregation in the presence of salts (from the saliva) alone. Furthermore, lactoferrin emulsions underwent bridging flocculation because of electrostatic binding of anionic mucin to the positively charged lactoferrin-stabilized emulsion droplets. In acidic pH conditions (pH 1.2) of the simulated gastric fluid (SGF), both protein-stabilized emulsions were positively charged. Addition of pepsin resulted in extensive droplet flocculation in both emulsions with a greater extent of droplet instability in lactoferrin emulsions. Coalescence of the droplets was observed as a result of peptic hydrolysis of the interfacial protein layers. Conditions such as ionic strength, pH and exposure to mucin were shown to significantly influence the rate of hydrolysis of β-lg-stabilized emulsion by pepsin. Addition of simulated intestinal fluid (SIF) containing physiological concentrations of bile salts to the emulsions showed competitive interfacial displacement of β-lg by bile salts. In the case of lactoferrin-stabilized emulsion droplets, there was considerable aggregation in the presence of intestinal electrolytes alone (without added bile salts) at pH 7.5. Binding of anionic bile salts to cationic interfacial lactoferrin layer resulted in re-stabilization of salt-aggregated lactoferrin emulsions. On mixing with physiological concentrations of pancreatin (mixture of pancreatic lipase, amylase and protease), significant degree of coalescence and fatty acid release occurred for both the emulsions. This was attributed to the interfacial proteolysis by trypsin (proteolytic fractions of pancreatin) resulting in interfacial film rupturing. Exchange of initial interfacial materials by bile salts and trypsin-induced film breakage enhanced the potential for lipolytic fractions of pancreatin to act on the hydrophobic lipid core. The lipid digestion products (free fatty acids and mono and/or diglycerides) generated at the droplet surface further removed the residual intact protein layers from the interface by competitive displacement mechanisms. The sequential treatment of the cationic and anionic emulsions with artificial saliva, SGF and SIF, respectively, was determined to understand the impact of initial protein type during complete physiological processing from mouth to intestine. Broadly, both the protein-stabilized emulsions underwent charge reversals, extensive droplet flocculation, and significant coalescence as they passed through various stages of the in vitro digestion conditions. Except in the simulated mouth environment, the initial charge of the emulsifiers had relatively limited influence on droplet behaviour during the simulated digestion. The results contribute to the knowledge of how structure and charge of the emulsified lipid droplets impact digestion at various stages of physiology. This information might have important consequences for developing suitable microstructures that allow controlled breakdown of droplets in the mouth and predictable release of lipids in the gastrointestinal tract.

A series of experiments were devised in order to establish the relationship between fibre addition to an extruded breakfast cereal base recipe and the physical, chemical and nutritional qualities of the breakfast cereals. A twin screw extruder was used for all experiments. Preliminary investigations using, guar gum and inulin additions, illustrated that screw configuration was important in determining the physical properties (degree of expansion, firmness and crunchiness) of the extruded products. Thus a screw configuration featuring a reverse screw and mixing zone within the barrel was selected for the larger research study. In the extended experimental design guar gum, inulin, wheat bran, swede fibre, and hi-maize were added to a base recipe at; 5, 10 and 15 % of total dry ingredient content. A further experiment was completed to investigate the synergistic effects of adding differing fibres in combination. Results illustrated that soluble dietary fibres (for instance guar and inulin) created a porous, less firm, but crispier breakfast cereals than the insoluble fibres, which generally produced denser, harder products. The inclusion of fibre into the extruded breakfast cereals did not affect the chemical composition of the breakfast cereal significantly (P=0.05) when taking into account the diluting factor of adding the fibre into the base recipe. However moisture loss / retention on extrusion varied significantly (P=0.05) between fibre combinations. Thus the moisture loss of samples containing guar or inulin were greater than those samples containing wheat bran and swede fibre. The process of extrusion did not significantly effect the amount of protein, starch or fibre in the samples when the extruded samples were compared to the control samples. Pasting properties of samples were evaluated using the Rapid Visco Analyser. This was conducted to try to determine associations between starch pasting properties (gelatinisation events) of the raw and extruded samples and the physical or nutritional quality of the products. However, the results did not show clear associations. An in vitro analysis was conducted to determine the effect of fibre addition on starch breakdown and subsequent release of reducing sugars. Breakfast cereals which included wheat bran, guar and swede fibre all showed a reduced rate of starch degradation compared to the control (P=0.05). These fibres appeared to inhibit the rate of enzyme degradation of starch, in effect increasing the amount of slowly digestible starch in the breakfast cereals. Cereal samples containing inulin did not show this pattern. Generally the rate of inhibition was related to the amount of fibre added to the base recipe. When used in combinations, samples containing inulin and hi-maize were not significantly different to the control in terms of reducing sugar release, whereas inclusion of guar gum significantly reduced this release. In conclusion, the addition of selected fibres can be used effectively as a method of manipulating the starch degradation rates of extruded breakfast cereals. This has nutritional implications in terms of glycaemic index and loading of breakfast cereals. Further work is required to develop clearer associations between the events of starch gelatinisation during extrusion and the potential glycaemic response.

Fouling of heat treatment equipment in the dairy processing industry is an expensive and persistent problem. The objective of this work was to develop a better understanding of the mechanisms of dairy fouling in heat exchangers and identify methods to control this build-up. This was part of a larger project investigating the interaction between spore-forming thermophilic bacilli (thermophiles) contamination and fouling deposits on internal surfaces of equipment. Two systems were developed to monitor the onset and build-up of fouling on the internal surfaces of two research heat exchangers. The first used a commercial sensor to measure the local heat flux and the temperature on the hot side of a plate type heat exchanger. The heat transfer coefficient was calculated and normalised with its value at the start of the run to reflect the contribution of fouling deposits to the thermal resistance, thus giving a real-time estimate of the rate of fouling. The second system used an energy balance over a tubular type heat exchanger and measured inlet and outlet temperatures to estimate the overall heat transfer coefficient thus giving a global measurement of fouling over the tubular heat exchanger. In both systems the plot of normalised heat transfer coefficient over time often stayed constant over an induction period, which was followed by a falling period indicative of growth in the fouling layer thickness and/or mass. Each system was validated by comparing the final value of the normalised heat transfer coefficient with direct measurements of fouling made at the end of a run namely: fouling deposit height for the local measurement and fouling deposit mass for the global measurement. The normalised heat transfer coefficient reported by each system correlated well with the corresponding direct measurement of the fouling layer. An important factor identified in this study was the effect of air bubble nucleation on fouling deposits. It was shown that bubbles that formed on the heated surface greatly reduced the length of the induction period to a matter of seconds rather than hours, as found in previous studies of fouling in the absence of surface bubbles. The rate of fouling was also enhanced while the bubbles remained at the surface. The structure of bubble type fouling layers was linked to the behaviour of the bubbles at the heated surface. Visual observations of these bubbles showed evidence of growth, vibration and coalescence during their period of attachment to the heated surface. Deposits from bubble type fouling consisted of all solid components found in the original milk solution, except lactose, in approximately the same ratio. By contrast fouling deposits reported in the literature with systems operating under the traditional protein denaturation mechanism were reported to consist mainly of whey proteins. Bubble induced fouling can be limited in a number of ways, the most effective being to maintain a high operating pressure in the equipment to ensure nucleation does not occur. Experiments conducted in this study showed that a pressure of 130 kPa.g was sufficient to suppress all bubble nucleation at the heated surface at a temperature of 90°C. Another method identified was the use of high linear fluid velocities to entrain any surface bubbles into the processing stream immediately upon nucleation. Linear velocities above 1.0 m/s were shown to achieve this goal in the miniature plate heat exchanger tested. However, this method is only partially successful because the local linear velocity varies with position in heat exchange equipment of complex geometries and can drop below the mainstream average velocity causing surface bubbles to form, especially in recirculation regions behind flow obstacles. A more reliable method, in situations where high operating pressures could not be used, involved conditioning the heated surface with a thin protein layer during the first few minutes of a run. Conditioning the surface resulted in bubble suppression even at high temperatures and low pressures, thus greatly extending the length of the induction period. Trials performed in this study showed that the addition of a proteolytic enzyme produced by psychrotrophic microbes greatly increased fouling. The enzyme destabilised the caseins which could attach directly to the heat exchange surface independently from the bubble fouling mechanism. Thus the quality of the milk is another important factor to consider. However, the addition of enzymes produced by thermophilic bacilli isolated from milk powder plants did not increase fouling. A theory describing the air bubble induced fouling mechanism is presented along with recommendations on how to reduce this fouling contamination in processing equipment.

Xenos Ltd. is a technology driven food company, that specializes in aseptic processing and packaging beverage products in bottles. Their aseptic filling technology is based on packaging sterilization with combined treatments of oxidizing agents and Ultraviolet radiation. Recent research studies have suggested that there is a synergistic effect of hydrogen peroxide (0.5 – 1 %) plus UV on inactivation of microorganisms including spores. Advantages of the combined treatment include rapid inactivation, minimum hydrogen peroxide residue in products, with the method being applicable to a wide range of packaging types. Based on this principle, a unique aseptic packaging technique has been developed by Xenos Ltd., which utilizes the combination of vaporized Perform (a commercial sterilizing agent manufactured by Orica Chemnet containing 25% hydrogen peroxide and 5% peracetic acid) and UV radiation at 7.5 – 12.5 W/m2. The aim of the project was to improve and validate the effectiveness of the packaging sterilization process through challenge tests. Challenge tests were conducted using Bacillus subtilis spores as the test microorganism to determine the log reductions delivered by the packaging sterilization system. The tests were firstly carried out on a pilot plant scale aseptic filling machine, in order to test the sterility of the small scale system, and investigate processing parameters (operational conditions) which could affect and improve sterility. The established operational conditions for achieving target sterility were used for designing and modifying an upgrade aseptic packaging system. Finally validation of the upgrade packaging sterilization system was conducted through challenge tests to prove sterility. It is highly recommended that in order to ensure sterility, the packaging sterilization system with vaporized Perform plus UV treatment must meet the requirements listed below during the sterilization process:  Hydrogen peroxide concentration of Perform condensate on bottles (after steaming) is best within 0.5 – 1 %;  Perform loading level should be minimum 300 mg/bottle after vaporized Perform treatment;  UV treatment time applied is greater than 2 seconds during UV treatment;  At least 20 seconds of penetration time (time between Perform treatment and UV treatment) should be allowed. The upgrade sterilization system used by Xenos Ltd. has been improved to meet the above operational conditions. With spore loading level of 106 per bottle and 105 per cap, the system is able to deliver at least a 6 log reduction of B. subtilis spores on PET or glass bottles and a 5 log reduction on bottle caps. Moruzzi et al. (2000) stated that at least a 4 log reduction is commercially required for an aseptic packaging process. Therefore, the system’s sterility would meet the commercial acceptable sterility.