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1.
Food Chem ; 405(Pt A): 134797, 2023 Mar 30.
Article in English | MEDLINE | ID: mdl-36371834

ABSTRACT

Plasma-activated water (PAW) is liquid treated with plasma. This liquid develops a higher oxygen reduction potential, a lower pH, and conductivity due to the delivery of reactive species from plasma to water. In this article, we review the antimicrobial activity and other applications of PAW in various food products. We discuss the effects of PAW treatment parameters on microbial inactivation efficiency as well as the underlying mechanisms, pesticide dissipation and its degradation pathway, meat curing and strategies to improve the nitrite amount in PAW, enhancement of food functional characteristics, and seed germination and plant growth. Additionally, we highlight the effects of PAW on food quality attributes. We further introduce the synergistic interaction of PAW with other technologies. Finally, we provide an overview of future challenges that must be resolved in the application of PAW in the food industry.


Subject(s)
Plasma Gases , Water , Water/pharmacology , Plasma Gases/pharmacology , Microbial Viability , Meat , Food Quality
2.
Food Chem ; 338: 127928, 2021 Feb 15.
Article in English | MEDLINE | ID: mdl-32919374

ABSTRACT

We investigated the inhibitory effect and binding mechanism of four selected compounds (ascorbic acid, l-cysteine, glutathione, and citric acid) on membrane-bound polyphenol oxidases (mPPO) using spectroscopic and molecular docking techniques. Kinetic analysis demonstrated that these inhibitors reversibly inhibited the mPPO activity. Fluorescence spectroscopy revealed that the intrinsic fluorescence intensity of mPPO was quenched by inhibitors with a single class of the inhibition site on mPPO. Amino acid residues His 180, His 201, His 366, Cys 184, Glu 328, and Asn 333 were the important binding sites in the active center. These sites were identified using molecular docking techniques. Our findings suggested that the inhibitors were allosterically bound to the active center of mPPO through hydrogen bonds and ion contacts. This study provides new insights into the active site residues responsible for catalyzing mPPO and provides applicable information about the design of mPPO inhibitors.


Subject(s)
Catechol Oxidase/metabolism , Malus/enzymology , Molecular Docking Simulation , Plant Proteins/metabolism , Allosteric Regulation , Ascorbic Acid/chemistry , Ascorbic Acid/metabolism , Binding Sites , Catechol Oxidase/antagonists & inhibitors , Cysteine/chemistry , Cysteine/metabolism , Glutathione/chemistry , Glutathione/metabolism , Kinetics , Plant Proteins/antagonists & inhibitors , Spectrometry, Fluorescence
3.
Food Chem ; 289: 657-663, 2019 Aug 15.
Article in English | MEDLINE | ID: mdl-30955661

ABSTRACT

Polyphenol oxidase from Granny Smith apples was purified and characterized in both its soluble form (sPPO) and its membrane-bound form (mPPO). Both forms were purified by temperature-induced phase partitioning, precipitation with ammonium sulfate, and ion exchange chromatography. The specific activity of mPPO was 19.17 times that of sPPO. The optimum pH and temperature for both forms were 7.0 and 35 °C when catechol was the substrate. The Michaelis constant and maximum reaction rate for sPPO were 34.1 mM and 500 U/mL/min, whereas those for mPPO were 53 mM and 10,000 U/mL/min, respectively. The enzymes exhibited diphenolase activity, and their affinity was highest for catechol (sPPO) and 4-methylcatechol (mPPO). Inhibitors of sPPO and mPPO included ascorbic acid, glutathione, and l-cysteine. However, ethylenediaminetetraacetic acid increased the activity of mPPO. Purified sPPO was dimeric with a molecular weight of 31 kDa, whereas mPPO was monomeric with an estimated molecular weight of 65 kDa.


Subject(s)
Catechol Oxidase/metabolism , Fruit/enzymology , Malus/enzymology , Ascorbic Acid/metabolism , Catechols/chemistry , Cysteine/metabolism , Edetic Acid/metabolism , Glutathione/metabolism , Hydrogen-Ion Concentration , Molecular Weight , Plant Proteins/metabolism , Substrate Specificity , Temperature
4.
Food Chem ; 183: 72-7, 2015 Sep 15.
Article in English | MEDLINE | ID: mdl-25863612

ABSTRACT

Membrane-bound polyphenol oxidase (mPPO) in Fuji apple (Malus domestica Borkh. cv. Red Fuji) was purified and analyzed with a nanoelectrospray ionization mass spectrometer. The three-dimensional model and binding site of mPPO to 4-methyl catechol were also studied using molecular docking. mPPO was purified 54.41-fold using temperature-induced phase partitioning technique and ion exchange chromatography. mPPO had a molecular weight of 67.3kDa. Even though a significant level of homology was observed between mPPO and the soluble polyphenol oxidase in the copper binding sequence, there was another region, rich in histidine residues, which differed in 13 amino acids. The three-dimensional structure of mPPO consisted of six α-helices, two short ß-strands, and ten random coils. The putative substrate-binding pocket contained six polar or charged amino acids, His191, His221, Trp224, Trp228, Phe227, and Val190. Trp224 and Trp228 formed hydrogen bonds with 4-methyl-catechol.


Subject(s)
Catechol Oxidase/chemistry , Fruit/chemistry , Malus/chemistry , Binding Sites , Food Additives/analysis , Molecular Docking Simulation
5.
Food Chem ; 173: 86-91, 2015 Apr 15.
Article in English | MEDLINE | ID: mdl-25465998

ABSTRACT

This study compared membrane-bound with soluble polyphenol oxidase (mPPO and sPPO, respectively) from Fuji apple. Purified mPPO and partially purified sPPO were used. mPPO was purified by temperature-induced phase partitioning and ion exchange chromatography. The specific activity of mPPO was 34.12× higher than that of sPPO. mPPO was more stable than sPPO at pH 5.0-8.5. Although mPPO was more easily inactivated at 25-55 °C, it is still more active than sPPO in this temperature range. The optimum substrate of mPPO was 4-methyl catechol, followed by catechol. L-cysteine had the highest inhibitory effects on mPPO followed by ascorbic acid and glutathione. Surprisingly, EDTA increased mPPO activity. The results revealed that purified mPPO is a dimer with a molecular weight of approximately 67 kDa.


Subject(s)
Catechol Oxidase/chemistry , Cell Membrane/enzymology , Malus/enzymology , Plant Proteins/chemistry , Catechol Oxidase/metabolism , Cell Membrane/chemistry , Dimerization , Fruit/chemistry , Fruit/classification , Fruit/enzymology , Kinetics , Malus/chemistry , Malus/classification , Molecular Weight , Plant Proteins/metabolism , Solubility
6.
Guang Pu Xue Yu Guang Pu Fen Xi ; 32(11): 2997-3001, 2012 Nov.
Article in Chinese | MEDLINE | ID: mdl-23387165

ABSTRACT

The red wine fermentation needs fast and nondestructive techniques, which can help to control the fermentation process and assure the quality of wine. In the present study, near infrared spectroscopy (NIR) and electronic nose (EN) were used to predict the alcohol content during the red wine alcoholic fermentation. Calibration models were developed between instru- mental data and chemical analysis using principal component regression (PCR) and partial least squares regression (PLSR) with cross validation. Good correlations (R > 0.99) were acquired for both the models developed by the NIR and EN data. However, RMSEC and RMSEP were a little larger. Combining NIR and EN can optimize the model and improve the prediction accuracy. The PLSR model based on combined data shows the best correlation (R = 0.999 2), with RMSEC and RMSEP being 0. 206 and 0.205% (v/v), respectively. Both NIR spectroscopy and EN can predict the alcohol concentration during the alcoholic fermentation of red wine, and the combination of two instruments can improve the analysis precision. Although the measurements were carried out in off-line mode, this study demonstrates that NIR and EN can be used as on line, fast, nondestructive and in time techniques to provide in-time information about the fermentation process and to assure the quality of final products.


Subject(s)
Electronic Nose , Ethanol/analysis , Fermentation , Spectroscopy, Near-Infrared/methods , Wine/analysis , Least-Squares Analysis , Principal Component Analysis
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