Thermal inactivation of polyphenoloxidase in pineapple puree

Chutintrasri, Benjar; Noomhorm, Athapol

doi:10.1016/j.lwt.2005.04.006

Cited by 89 publications

(53 citation statements)

References 15 publications

(16 reference statements)

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“…Good color stability over the storage period for the mild thermal treated product indicates sufficient inactivation of the heat sensitive PPO enzyme. Normally, heat treatments of 70-90°C significantly destroy the catalytic activity of the PPO (Chisari, Barbagallo and Spagna, 2007;Chutintrasri & Noomhorm, 2006;Weemaes et al, 1997). The data suggest that the maximum temperatures of 73.4 ± 0.3°C achieved during the mild pasteurization in combination with the low pH, refrigerated storage, and the barrier properties of the pouches inhibited the PPO enzyme activity of the purée product.…”

Section: Physical and General Physicochemical Analysismentioning

confidence: 96%

Effect of high pressure processing on the quality of acidified Granny Smith apple purée product

Landl

Abadías²,

Sárraga

et al. 2010

Innovative Food Science & Emerging Technologies

204

117

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Section: Physical and General Physicochemical Analysismentioning

confidence: 96%

Effect of high pressure processing on the quality of acidified Granny Smith apple purée product

Landl

Abadías²,

Sárraga

et al. 2010

Innovative Food Science & Emerging Technologies

204

117

View full text Add to dashboard Cite

“…The thermal inactivation of polyphenoloxidase in pineapple puree when heated from 70°C to 90°C, with D-values varying from 91.3 and 11.4 min, corresponded to a z-value of 21.5°C and E a of 82.8 kJ/mol (1 cal = 4.18 J; 19.81 kcal/mol) (16). GFP showed greater stability than polyphenoloxidase in the systems composed with water (>5% NaCl), or with phosphate (>10% NaCl) and acetate-buffered solutions (up to 30% NaCl).…”

Section: Activation Energymentioning

confidence: 99%

Evaluation of the pH- and thermal stability of the recombinant green fluorescent protein (GFP) in the presence of sodium chloride

Ishii

Kunimura

Jeng

et al. 2007

Appl Biochem Biotechnol

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The thermal stability of recombinant green fluorescent protein (GFP) in sodium chloride (NaCl) solutions at different concentrations, pH, and temperatures was evaluated by assaying the loss of fluorescence intensity as a measure of denaturation. GFP, extracted from Escherichia coli cells by the three-phase partitioning method and purified through a butyl hydrophobic interaction chromatography (HIC) column, was diluted in water for injection (WFI) (pH 6.0-7.0) and in 10 mM buffer solutions (acetate, pH 5.0; phosphate, pH 7.0; and Tris-EDTA, pH 8.0) with 0.9-30% NaCl or without and incubated at 80-95 degrees C. The extent of protein denaturation was expressed as a percentage of the calculated decimal reduction time (D-value). In acetate buffer (pH 4.84+/-0.12), the mean D-values for 90% reduction in GFP fluorescence ranged from 2.3 to 3.6 min, independent of NaCl concentration and temperature. GFP thermal stability diluted in WFI (pH 5.94+/-0.60) was half that observed in phosphate buffer (pH 6.08+/-0.60); but in both systems, D-values decreased linearly with increasing NaCl concentration, with D-values (at 80 degrees C) ranging from 3.44, min (WFI) to 6.1 min (phosphate buffer), both with 30% NaCl. However, D-values in Tris-EDTA (pH 7.65+/-0.17) were directly dependent on the NaCl concentration and 5-10 times higher than D-values for GFP in WFI at 80 degrees C. GFP pH- and thermal stability can be easily monitored by the convenient measure of fluorescence intensity and potentially be used as an indicator to monitor that processing times and temperatures were attained.

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“…Full squares, data on fresh sample; full circles, data of the partial sample 1 (on the top of the sample); upward triangles, data of the partial sample 2 (in the middle of the sample); downward triangles, data of the partial sample 3 (on the bottom of the sample) first degree inactivation kinetics. The poly-phenoloxidase activity is practically negligible at 100°C (Chutintrasri & Noomhorm 2006). Therefore, the MAP does not appreciably change the polyphenols total content with respect to the fresh product (i.e., the polyphenols total remains unaltered (Figure 2e) whereas the poly-phenol-oxidase activity in the microwave dried samples is negligible because of the high temperatures reached within the sample (Figure 2g).…”

Section: Resultsmentioning

confidence: 97%

Microwave assisted drying of banana: effects on reducing sugars and polyphenols contents

Barba¹,

D’Amore²,

Rispoli³

et al. 2014

Czech J. Food Sci.

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Barba A.A., d'Amore M., Rispol M., Marra F., Lamberti G. (2014): Microwave assisted drying of banana: effects on reducing sugars and polyphenols contents. Czech J. Food Sci., 32: 369-375.The effects of microwave assisted drying on banana fruit was evaluated. Water, reducing sugars, and polyphenol contents, as well as poly-phenol-oxidase activity were evaluated along the radial and axial positions in thick slices of banana, according to a properly defined cutting and assaying protocol. The effects of the microwave-assisted drying process were compared to the convective air-assisted drying resulting faster than the conventional process. In particular, the resulting samples were homogeneous in the water content; the contents of reducing sugars were strongly decreased on drying with microwaves; the poly-phenol-oxidase was inactivated by the high temperature produced by the process and thus the polyphenols content remained practically the same as in the fresh product.

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Thermal inactivation of polyphenoloxidase in pineapple puree

Cited by 89 publications

References 15 publications

Effect of high pressure processing on the quality of acidified Granny Smith apple purée product

Effect of high pressure processing on the quality of acidified Granny Smith apple purée product

Evaluation of the pH- and thermal stability of the recombinant green fluorescent protein (GFP) in the presence of sodium chloride

Microwave assisted drying of banana: effects on reducing sugars and polyphenols contents

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