Effect of pH on Enzyme Inactivation Kinetics in High-Pressure Processed Pineapple (Ananas comosus L.) Puree Using Response Surface Methodology

Effect of pH and high-pressure process treatments viz. pressure, temperature, and dwell time on inactivation of polyphenoloxidase (PPO), peroxidase (POD), bromelain (BRM), and pectinmethylesterase (PME) in pineapple puree was studied. Experiments were conducted according to rotatable central composite design (RCCD) within the range (?α to?+?α) of 100–600 MPa, 20–70 °C, and 0–30 min at three different pH levels (3.0, 3.5, and 4.0) followed by analysis through response surface methodology (RSM). Enzyme inactivation was significantly (p?k in min^?1) revealed that PPO was the most resistive (k ranged between 0.0020 and 0.0379 min^?1) when compared with other three enzymes within the experimental domain. Increased k at lower pH with constant pressure and temperature depicted that pH had negative effect on the inactivation process. The optimized conditions targeting maximum inactivation of PPO, POD and PME with simultaneous retention of BRM in pineapple puree, were 600 MPa/60 °C/9 min, 600 MPa/60 °C/10 min and 600 MPa/60 °C/10 min for the samples of pH 3.0, 3.5, and 4.0, respectively.     

Gelation of Persimmon Puree and Its Prevention by Enzymatic Treatment

Fresh persimmon puree showed a rheological behavior corresponding to a weak gel, where storage modulus (G′) prevailed over loss modulus (G″). In a temperature sweep test (from 25–80–25 °C), G′ values increased at temperatures above 60 °C and continued increasing during the subsequent cooling step showing a wide scattering. These changes indicated a gelation phenomena that resulted in a more rigid and irregular gel structure. The gelation was lower in the acidified puree (pH 4.4) than in the puree at its natural pH (5.9). The addition of ethylenediaminetetraacetate sodium avoided the increase of G′ during the heating and reduced the G′ increase in the cooling step. Thus, gelation in persimmon puree occurred by a heat-set gelation influenced by pH, and also by cold-set gelation depending on an ionotropic mechanism. The incubation of persimmon puree with Viscozyme L (1 g/L, 25 °C, 30 min) allowed to obtain a more fluid product able to tolerate a thermal processing at 85 °C without gelation. During the incubation with Viscozyme L, the pH of the persimmon puree decreased monotonically as a consequence of its pectinmetylesterase activity, and the continuous measurement of pH could be used to monitor this process.     

High pressure and thermal inactivation kinetics of polyphenol oxidase and peroxidase in strawberry puree

The objective of this work was to study the thermal and high pressure inactivation kinetics of polyphenol oxidase (PPO) and peroxidase (POD) in strawberry puree. PPO from two strawberry cultivars (‘Festival’ and ‘Aroma’) was found to be highly thermostable in strawberry puree with no significant inactivation even after 30 min treatment at 100 °C. In contrast, POD from the two cultivars displayed very high thermosensitivity with complete inactivation in less than 5 min at 70 °C. The thermal inactivation kinetics of strawberry POD was described by a biphasic model. The activation energies for the inactivation of the stable and the labile fractions were estimated to be 254.9 and 221.6 kJ/mol respectively. Combined high pressure–thermal treatment at pressures ranging from 100 to 690 MPa, temperatures ranging from 24 to 90 °C and treatment times between 5 and 15 min did not have significant effect on PPO while substantial inactivation of POD was observed. The inactivation kinetics of POD during combined high pressure–thermal processing was well described by first-order kinetics probably due to the inactivation of the labile fraction during the pre-heating and the compression phase.Industrial relevanceThe oxidative enzymes polyphenol oxidase and peroxidase cause the degradation of anthocyanins and other polyphenols in strawberry products, leading to discoloration and loss of antioxidant activity. In this work the thermal and high pressure inactivation of strawberry polyphenol oxidase and peroxidase was investigated so as to assess the suitability of high pressure processing as an alternative to thermal processing. Strawberry polyphenol oxidase was found to be highly resistant to both thermal and high pressure inactivation. Thus in order to maintain the quality of processed strawberry products, high pressure processing should be accompanied by additional measures such as exclusion of oxygen, refrigerated storage and the use of natural enzyme inhibitors.     

Thermal inactivation kinetics parameters of browning enzymes in starfruit (Averrhoa carambola L.) juice

This study aimed to evaluate the thermal inactivation kinetics of polyphenol oxidase (PPO) and peroxidase (POD) in starfruit juice. It followed the Malaysia Food Regulations 1985 and CODEX STAN 247-2005. Glucose, fructose and sucrose were the main sugars in starfruit juice. The total soluble solids, pH, titratable acidity, and total phenolics content of the starfruit juice produced were 8.13 ± 0.25 °Brix, 3.80 ± 0.05, 0.43% ± 0.02% malic acid, and 93.67 ± 4.96 mg GAEL⁻¹, respectively. Thermal inactivation kinetics of PPO and POD followed the first-order kinetic model. The decimal reduction time at 83.6 °C (D_83.6) of PPO and POD was 198.48 and 98.4 s, respectively, while the thermal resistance constant (z value) of PPO and POD was 12.8 and 5.4 °C, respectively. In conclusion, PPO might be a suitable signal for thermal processing on starfruit juice since it has higher heat resistance than POD.     

Effect of High Hydrostatic Pressure and Temperature on Enzymatic Activity and Quality Attributes in Mango Puree Varieties (cv. Tommy Atkins and Manila)

Pectinmethylesterase (PME), peroxidase (POD), and polyphenoloxidase (PPO) residual activities (RAs) and physicochemical parameters (pH, total soluble solids (TSS), water activity (a_w), viscosity and color) of Tommy Atkins and Manila mango purees (MPs) were evaluated after high hydrostatic pressure (HHP) treatments at 400–550 MPa/0–16 min/34 and 59 °C. HHP treatment applied at 59 °C induced higher enzyme inactivation levels than the treatment applied at 34 °C in both MPs. The lowest RA of PME (26.9–38.6%) and POD (44.7–53%) was achieved in Manila MP treated at 450 MPa/8–16 min/59 °C and 550 MPa/4–16 min/59 °C, respectively. Otherwise, Tommy Atkins puree pressurized at 550 MPa/8–16 min/59 °C had the lowest PPO RA (28.4–34%). A slight decrease in pH and TSS values of both HHP-processed MPs at 34 and 59 °C was observed, whereas the a_w remained constant after processing. The viscosity of MPs tended to augment up to 2.1 times due to the application of HHP. No significant changes were observed in color parameters of Tommy Atkins MP, except at 550 MPa and 59 °C where higher yellow index (YI) (122.4?±?3.3) and lower L* (37.3?±?5.3) were obtained compared to the untreated MP. HHP caused an increase in L* values in Manila MP, whereas no clear trend was observed in YI. HHP processing at 550 MPa combined with mild temperature (59 °C) during 8 min could be a feasible treatment to reduce enzymatic activity and preserve fresh-like quality attributes in MP.     

High Pressure Inactivation of Polyphenoloxidases

Pressure stabilities of polyphenoloxidases (PPO) from apples, avocados, grapes, pears and plums were determined at pH 6-7. These PPOs differed in pressure stability, but all were rather pressure-stable. Inactivation of PPO from apple, grape, avocado and pear at room temperature (25°C) became noticeable at 600, 700, 800 and 900 MPa respectively, and followed first-order kinetics. Plum PPO was not inactivated at room temperature by pressures up to 900 MPa. For the two most pressure-stable PPOs, we investigated whether pressure stability would be reduced by the simultaneous application of mild heat. In case of plum PPO, activity reduction was detectable at 900 MPa and 50°C. Further temperature increase resulted in increase of the inactivation rate constant (E_a 63 kJ/mol). In case of pear PPO, temperature increase up to 35°C resulted in a 3-fold reduction of the inactivation rate constant. Only at higher temperatures, increase of the inactivation rate constant with increasing temperature was noted (Ea 120 kJ/mol).     

High pressure thermal processing of pears: Effect on endogenous enzyme activity and related quality attributes

The effect of high pressure-thermal (HPT) processing (600 MPa, 20–100 °C) on the activity of pear enzymes and related quality attributes was investigated. HPT processing at 20 °C for 5 min resulted in 32%, 74% and 51% residual activities of polyphenol oxidase (PPO), peroxidase (POD) and pectin methylesterase (PME), respectively. Increasing processing temperature to 40 and 60 °C reduced the level of PPO and POD inactivation, with the maximum residual activities of 64% and 123%, respectively observed after 3-min treatments at 40 and 60 °C. Overall, HPT at 20 to 60 °C had minimal effect on quality, although enzymatic browning was observed upon air exposure. HPT at 80 to 100 °C caused almost complete inactivation of PPO and POD with 90% and 92% inactivation respectively after 3-min processing at 100 °C, which reduced browning upon air exposure. Nevertheless, the lowest texture retention of 22% was observed under this condition.Industrial relevanceThe study examined the effects of combined high pressure thermal processing on quality related pear enzymes and related instrumental quality attributes such as colour and texture. The study enabled identification of processing regimes for enzyme inactivation and quality retention. The excellent quality retention following HPP at 20 to 40 °C makes this condition suitable for ‘fresh-like’ small portion products for immediate consumption after unpacking that do not require complete PPO and POD inactivation. On the other hand, the almost complete inactivation of oxidative enzymes PPO and POD at 100 °C makes this condition more appropriate for the production of bulk products for food service applications or pureed ingredients for baby food, or pear pieces for yoghurt, that require PPO inhibition but not necessarily high firmness retention.     

Inactivation kinetics of polygalacturonase in tomato juice

The inactivation kinetics of polygalacturonase (PG) in tomato juice was studied during thermal and high-pressure/thermal processing. In the temperature range of 55–70 °C the thermal inactivation of polygalacturonase in tomato juice followed a fractional conversion model, with a thermostable fraction of approximately 14%. Under conditions of combined high-pressure/thermal processing, 200–550 MPa/5–50 °C, PG inactivation presented first order kinetics. A mathematical model to describe the inactivation rate constant as a function of pressure and temperature was formulated. Industrial relevance: Polygalacturonase is responsible for the decrease of viscosity in tomato-based products. However, little research on thermal and high pressure/thermal inactivation kinetics of tomato Polygalacturonase has been reported. This research clearly shows that it is possible to selectively inactivate PG by high pressure/thermal processing without applying high temperatures. This leads to tomato-based products with improved functional properties while other quality attributes (color, flavor, nutritional value) are maintained.     

Impact of pH and Total Soluble Solids on Enzyme Inactivation Kinetics during High Pressure Processing of Mango (Mangifera indica) Pulp

This study was undertaken with an aim to enhance the enzyme inactivation during high pressure processing (HPP) with pH and total soluble solids (TSS) as additional hurdles. Impact of mango pulp pH (3.5, 4.0, 4.5) and TSS (15, 20, 25 °Brix) variations on the inactivation of pectin methylesterase (PME), polyphenol oxidase (PPO), and peroxidase (POD) enzymes were studied during HPP at 400 to 600 MPa pressure (P), 40 to 70 °C temperature (T), and 6‐ to 20‐min pressure‐hold time (t). The enzyme inactivation (%) was modeled using second order polynomial equations with a good fit that revealed that all the enzymes were significantly affected by HPP. Response surface and contour models predicted the kinetic behavior of mango pulp enzymes adequately as indicated by the small error between predicted and experimental data. The predicted kinetics indicated that for a fixed P and T, higher pulse pressure effect and increased isobaric inactivation rates were possible at lower levels of pH and TSS. In contrast, at a fixed pH or TSS level, an increase in P or T led to enhanced inactivation rates, irrespective of the type of enzyme. PPO and POD were found to have similar barosensitivity, whereas PME was found to be most resistant to HPP. Furthermore, simultaneous variation in pH and TSS levels of mango pulp resulted in higher enzyme inactivation at lower pH and TSS during HPP, where the effect of pH was found to be predominant than TSS within the experimental domain.     

Thermal and High-Pressure Stability of Pectinmethylesterase, Polygalacturonase, β-Galactosidase and α-Arabinofuranosidase in a Tomato Matrix: Towards the Creation of Specific Endogenous Enzyme Populations Through Processing

The thermal and pressure stability of tomato pectinmethylesterase (PME), polygalacturonase (PG), β-galactosidase (β-Gal), and α-arabinofuranosidase (α-Af) were investigated in situ. Enzyme inactivation by thermal and high-pressure processing (respectively 5 min at 25–95 °C at 0.1 MPa and 10 min at 0.1–800 MPa at 20 °C) was monitored by measuring the residual activity in crude enzyme extracts of treated tomato purée samples. PME was completely inactivated after a 5-min treatment at 75 °C. Only 30 % of the pressure stable PME was inactivated after a treatment at 800 MPa (20 °C, 10 min). A 5-min treatment at 95 °C and a treatment at 550 MPa (20 °C, 10 min) caused complete PG inactivation. β-Gal and α-Af activities were already reduced significantly by thermal treatments at 42.5–52.5 °C and 45–60 °C, respectively. These enzymes were, however, rather pressure resistant: treatments at respectively 700 and 600 MPa were necessary to reduce the activity below 10 % of the initial value. Assuming that first-order, fractional conversion or biphasic inactivation models could be applied to the respective enzyme inactivation data, inactivation rate constants and their temperature or pressure dependence for the different enzymes were determined. Based on differences in process stability of the enzymes, possibilities for the creation of specific “enzyme populations” in tomato purée by selective enzyme inactivation were identified. For industrially relevant process conditions, the enzyme inactivation data obtained for tomato purée were shown to be transferable to intact tomato tissue.     

Thermal inactivation of strawberry polyphenoloxidase and its impact on anthocyanin and color retention in strawberry (Fragaria x ananassa Duch.) purées

Strawberry (Fragaria x ananassa Duch.) cultivars were screened for their polyphenoloxidase (PPO) activities, and thermal stability of PPO was evaluated in vitro for three cultivars under different time–temperature regimes (60, 75 and 90 °C for 3 and 5 min, respectively). Heating strawberry purées should further elucidate the impact of thermal treatments on strawberry PPO in its natural matrix (‘in situ’ activity). To evaluate the consequences of PPO inactivation on anthocyanin and color stability, the purées were stored for 28 days at +20 °C monitoring the contents of monomeric, polymeric (spectrophotometrically) and individual anthocyanins (HPLC–DAD–MSⁿ) as well as color properties (CIE L*a*b*). Antioxidant activities (FRAP), total phenolic (Folin–Ciocalteu) and ascorbic acid contents of freshly prepared and stored purées, respectively, were determined spectrophotometrically. PPO activities varied considerably among the cultivars investigated. Accordingly, different time–temperature regimes were required for their complete in vitro and in situ inactivation. Unexpectedly, thermal inactivation of PPO was disadvantageous regarding pigment and color retention of strawberry purées, which was ascribed to partial regeneration of PPO. Hence, protection of antioxidants, total phenolics and ascorbic acid from oxidative degradation could not be achieved by heating the purées prior to storage.     

Beta-carotene isomerisation in mango puree as influenced by thermal processing and high-pressure homogenisation

The present study describes a case study on mango puree, in which focus is given to the effect of thermal processing (100–130 °C, 0–80 min) and high-pressure homogenisation (0–1300 bar) on the isomerisation of β-carotene. Both unit operations are of relevance for the production of mango puree. β-Carotene is an essential micronutrient which is present in a high amount in most mango cultivars, and it is important for human health due to its antioxidant and provitamin A capacity. It is known that these health-related properties of β-carotene are negatively affected by the conversion to cis-isomers. The results have shown that during high-pressure homogenisation of mango puree, β-carotene isomerisation was negligible. During thermal processing, on the other hand, an increase in β-carotene cis-isomer formation with increasing treatment intensity could be observed, although high temperatures and/or long treatment times were required to observe clear additional isomer formation. From a kinetic point of view, a fractional conversion model could be used to model the all-trans-β-carotene isomerisation in mango puree in the temperature and time range studied. In general, it can be concluded that a high percentage of β-carotene is present as cis-isomers in raw mango puree. Furthermore, only intense thermal processing of mango puree leads to the formation of additional cis-isomers in relevant amounts.     

Thermal Chlorophyll Degradation Kinetics of Mint Leaves Puree

Thermal degradation kinetics of chlorophyll ‘a’, ‘b’ and total chlorophyll in mint leaves puree were investigated as function of pH (4.5–8.5) and processing temperature (80–145°C), respectively. Mint puree was processed at 80°to 100°C at pH 4.5, while that at pH 5.5 to 8.5 was processed at 105°to 145°C. Chlorophyll degradation followed the first order reaction kinetics. Good agreement was found between estimated and experimental chlorophyll retention in all cases (R² > 0.86; MRQE < 0.27). Activation energies ranged from 6.45 to 47.67 kJ/mol. Reaction rate and activation energy data indicated that chlorophylls were more stable at alkaline pH. Transition state theory was applied to estimate the enthalpy, entropy and Gibbs free energy of activation. Enthalpy (ΔH^#) ranged from 3.14 to 44.66 kJ/mol, while entropy (ΔS^#) ranged from ?0.157 to ?0.266 kJ/(mol K). The overall free energy change was 105.76 kJ/mol. Results indicated that, the compensation effect did not exist for chlorophyll degradation in mint puree during thermal processing.     

Effect of rice bran protein extract on enzymatic browning inhibition in potato puree

Effect of rice bran protein extract (RBPE) on enzymatic browning inhibition in potato puree was studied by colour measurement and polyphenol oxidase (PPO) inhibition. RBPE inhibited browning in potato puree and showed a higher per cent potato PPO inhibition at pH 4.0 and 5.0 than those at pH 3.0, 6.0 and 7.0 (P ≤ 0.05). RBPE heated to 40 and 60 °C had browning inhibition in potato puree and per cent potato PPO inhibition at a similar extent to unheated RBPE (P > 0.05). Browning inhibition and per cent potato PPO inhibition of RBPE were decreased when it was heated to 80 °C (P ≤ 0.05). RBPE inhibited browning in potato puree higher than 5, 10 and 20 mm ascorbic acid and 5 and 10 mm citric acid (P ≤ 0.05). Regarding the kinetics study, RBPE exhibited a mixed‐type inhibition for potato PPO. Therefore, RBPE has a potential to be used as a natural antibrowning agent in the potato industry.     

High pressure processing of cocoyam,Peruvian carrot and sweet potato: Effect on oxidative enzymes and impact in the tuber color

High pressure processing (HPP) is a non-thermal technology used to activate or inactivate enzymes. This study investigated the effects of HPP (600 MPa for 5 or 30 min at 25 °C) on cocoyam, Peruvian carrot and sweet potato color, and the polyphenoloxidase (PPO) and peroxidase (POD) activities in tuber cubes, puree, and enzyme extract subjected to HPP. The results showed enzyme inactivation by HPP in cocoyam (up to 55% PPO inactivation in puree and 81% POD inactivation in extract) and Peruvian carrot (up to 100% PPO and 57% POD inactivation the extract). In contrast, enzyme activation was observed in sweet potato (up to 368% PPO and 27% POD activation in puree). The color results were compatible to enzyme activity: the color parameters remained unchanged in cocoyam and Peruvian carrot, which showed high PPO and POD inactivation after HPP. Furthermore, the impact of HPP on the enzymes was influenced by the matrix in which HPP was carried out, evidencing that the enzyme structure can be protected in the presence of other food constituents.Industrial relevanceThe enzymes PPO and POD are an important concern for vegetable processing, due its ability to induce browning after vegetables are cut. The HPP at 600 MPa for 5 or 30 min can be used to inactivate these enzymes in cocoyam and Peruvian carrot, guaranteeing the color and freshness of the tubers similar to the fresh cut vegetable.     

High Pressure and Temperature Effects on Enzyme Inactivation in Strawberry and Orange Products

High hydrostatic pressure treatment (50-400 MPa) combined with heat treatment (20–60°C) effects on peroxidase (POD), polyphenoloxidase (PPO) and pectin methylesterase (PME) activities of fruit-derived products were studied. Assays were carried out on fresh orange juice and strawberry puree. Pressurization/depressurization treatments caused a significant loss of strawberry PPO (60%) up to 250 MPa and POD activity (25%) up to 230 MPa, while some activation was observed for treatments carried out in 250–400 MPa range for both enzymes. Optimal inactivation of POD was using 230 Mpa and 43°C in strawberry puree. Combinations of high pressure and temperature effectively reduced POD activity in orange juice (50%) to 35°C. The effects of high pressure and temperature on PME activity in orange juice were very similar to those for POD.     

Inactivation Kinetics of the Most Baro-Resistant Enzyme in High Pressure Processed Litchi-Based Mixed Fruit Beverage

This work focused on a litchi-based mixed fruit beverage, comprising of coconut water and lemon juice, mixed in an optimized proportion. Based on preliminary studies, three resistant spoilage enzymes were identified in the beverage, viz. polyphenol oxidase (PPO), peroxidase (POD), and pectin methyl esterase (PME). The response surface methodology (RSM) based on central composite face-centered design (FCCD) screened out PPO as the most resistant enzyme within the high pressure processing (HPP) domain of 200–600 MPa/30–70 °C/0–20 min. A detailed kinetic study was conducted on PPO inactivation within the same HPP domain along with a set of thermal treatments (0.1 MPa/30–70 °C). A synergistic effect of pressure and temperature on PPO inactivation was observed, throughout the HPP domain. However, PPO was almost completely inactivated at 500 MPa/70 °C/20 min. The inactivation order (n) values for PPO were 1.10 and 1.25 for thermal and HPP treatments, respectively. For every 10 °C rise in temperature, the inactivation rate constant (k, U^n-1 min^?1) increased approximately by 1.5 times, within 50–70 °C (at 0.1 MPa), while a 10-fold increase was obtained in the case of HPP treatments. The activation energy (E _a ) and the activation volume (V _a), depicting the temperature and pressure dependence of k, was found to decrease slightly, with an increase in pressure and temperature, respectively. The PPO inactivation rate constant was modeled as a function of both temperature and pressure conditions by combining both Arrhenius and Eyring equations.     

砀山酥梨膜结合态与可溶态多酚氧化酶性质比较

为探究砀山酥梨膜结合态多酚氧化酶（mPPO）性质,本文以砀山酥梨为原料,研究其mPPO催化特性及热失活动力学,并与可溶态多酚氧化酶（sPPO）性质进行比较。结果表明:以邻苯二酚为底物时,mPPO与sPPO催化特性及热失活动力学性质不同。mPPO比活力及对底物亲和力高于sPPO。mPPO在pH4.50时酶活最高,而sPPO最适pH为5.00。mPPO酸碱稳定性高于sPPO,mPPO在pH3.50～4.50环境中保持24 h后酶活大于原始酶活。砀山酥梨mPPO在35～45 ℃温度区间内活性最高,且mPPO在55～75 ℃区间热稳定性高于sPPO。热失活动力学分析结果表明,热处理对sPPO及mPPO的钝化均符合一级反应动力学,动力学参数E_a值及Z_T值分析表明mPPO比sPPO催化反应对温度的依赖性更小,热耐受性更高。     

Response Surface Optimization of Process Parameters and Fuzzy Analysis of Sensory Data of High Pressure–Temperature Treated Pineapple Puree

The high‐pressure processing conditions were optimized for pineapple puree within the domain of 400‐600 MPa, 40‐60 °C, and 10‐20 min using the response surface methodology (RSM). The target was to maximize the inactivation of polyphenoloxidase (PPO) along with a minimal loss in beneficial bromelain (BRM) activity, ascorbic acid (AA) content, antioxidant capacity, and color in the sample. The optimum condition was 600 MPa, 50 °C, and 13 min, having the highest desirability of 0.604, which resulted in 44% PPO and 47% BRM activities. However, 93% antioxidant activity and 85% AA were retained in optimized sample with a total color change (?E*) value less than 2.5. A 10‐fold reduction in PPO activity was obtained at 600 MPa/70 °C/20 min; however, the thermal degradation of nutrients was severe at this condition. Fuzzy mathematical approach confirmed that sensory acceptance of the optimized sample was close to the fresh sample; whereas, the thermally pasteurized sample (treated at 0.1 MPa, 95 °C for 12 min) had the least sensory score as compared to others.     

Quality of Banana Puree During Storage: a Comparison of High Pressure Processing and Thermal Pasteurization Methods

The quality features of banana puree after high pressure processing (HPP) at 500 MPa for 10 min and thermal pasteurization (TP) at 90 °C for 2 min during 30 days of refrigerated storage were compared in this study. Initial counts in banana puree of greater than 3.80 log colony-forming units (CFU)/g of total aerobic bacteria (TAB) and 3.10 log CFU/g of molds and yeasts (M&Y) were reduced by HPP and TP. TAB were approximately 1.0 CFU/g, and M&Y were less than 0.3 log CFU/g in HPP- and TP-processed puree during storage. HPP and TP did not change pH, titratable acidity (TA), total soluble solids (TSS), lightness (L), and yellowness (b), total phenolic content (TPC), and antioxidant capacity (AC), but HPP raised redness (a) and TP reduced a and ascorbic acid (AA). During storage, L, a, and b in HPP- and TP-processed purees did not change but HPP-processed puree increased pH and decreased TA. After storage, the percentage of TPC and AA was 75.85 and 55.09 % in the HPP group and 96.30 and 68.09 % in the TP group, indicating a significant loss of TPC and a greater loss of AA in HPP-processed puree. The loss of AC agreed with the loss of AA and TPC. HPP preserved particle size distribution and viscosity of purees, whereas TP increased the number of smaller particles and viscosity after processing and in storage. Twenty-six volatiles (18 esters) and 22 volatiles (15 esters) were detected in HPP- and TP-processed purees, and the ester fraction was 69.79 and 52.36 %, respectively. HPP was found to be an effective alternative pasteurization method for preserving the quality of fresh banana puree.