RESUMEN
The effects of hydrostatic (HHP) and dynamic (HPH) high-pressure treatments on the activity of pectin methylesterase (PME) and polyphenol oxidase (PPO) as well as the physicochemical quality attributes of 'Ataulfo' mango nectar were assessed. HHP reduced PME relative activity by 28% at 100 MPa for 5 min but increased PPO activity almost five-fold. Contrarily, HPH did not affect PME activity, but PPO was effectively reduced to 10% of residual activity at 300 MPa and at three passes. Color parameters (CIEL*a*b*), °hue, and chroma were differently affected by each type of high-pressure processing technology. The viscosity and fluid behavior were not affected by HHP, however, HPH changed the apparent viscosity at low dynamic pressure levels (100 MPa with one and three passes). The viscosity decreased at high shear rates in nectar samples, showing a shear-thinning effect. The results highlight how different effects can be achieved with each high-pressure technology; thus, selecting the most appropriate system for processing and preserving liquid foods like fruit beverages is recommended.
Asunto(s)
Bebidas , Hidrolasas de Éster Carboxílico/química , Frutas/enzimología , Mangifera/enzimología , Proteínas de Plantas/química , Presión HidrostáticaRESUMEN
BACKGROUND: Under-Skin Browning (USB) is a physiological skin disorder that significantly reduces quality of 'Honey Gold' mango (HG) fruit. Relationships between potential causative factors (vibration, holding temperature, sap) and expression factors (enzymes activities, phenolic concentration, anatomy) were investigated. RESULTS: USB incidence was 2.6-3.6-fold higher in ripe HG fruit vibrated for 3-18 h at 12 °C to simulate transport damage and held then at 12 °C for 8 days compared to control fruit held under the same conditions. USB severity of fruit lightly abraded with sand paper to simulate physical damage and artificially induce USB was higher in fruit held at 10 °C than at 6-8 °C or 12-13 °C for 6-8 days. Compared to non-affected skin, USB-affected tissue had a 7.4% increase in total phenolics concentration. However, polyphenol oxidase (PPO) and peroxidase (POD) activities decreased by 19%. Anatomical similarities were observed between USB symptoms and sapburn caused by spurt sap or terpinolene (a major sap component) to abraded skin areas. Incidence of sapburn was higher in abraded fruit held at 12 °C than at 20 °C. CONCLUSION: Holding HG mango fruit at 10 °C can intensify USB. Activities of PPO and POD appear not to be regulatory factors in USB expression in HG. Sap components may be involved in USB expression under conducive postharvest conditions. © 2021 Society of Chemical Industry.
Asunto(s)
Conservación de Alimentos/métodos , Frutas/química , Mangifera/química , Catecol Oxidasa/metabolismo , Frutas/enzimología , Frutas/metabolismo , Mangifera/enzimología , Mangifera/metabolismo , Peroxidasa/metabolismo , Fenoles/análisis , Fenoles/metabolismo , Proteínas de Plantas/metabolismo , Control de Calidad , TemperaturaRESUMEN
Mango has been described as a valuable source of nutrients and enzymes that are beneficial to human health. Drying at different temperatures not only affects the nutritional properties but can also contribute to the degradation of valuable enzymes in dried fruit. The novelty of this paper is to investigate the quality of hot air dried mango in terms of activity retention of the heat-sensitive enzymes (HSE). For this, HSE was first screened in fresh mango flesh of the variety Samar Bahisht (SB) Chaunsa. Later, the combined effect of different drying temperatures (40 °C, 50 °C, 60 °C, 70 °C, and 80 °C) and air velocities (1.0 ms-1 and 1.4 ms-1) on the activity retention of HSE in dried mango slices of the varieties Sindri, SB Chaunsa, and Tommy Atkins were investigated. The results showed that the drying temperature had a significant impact on the degradation of HSE, while at the same time some influence of the air velocity was also observed. Drying at 40 °C and an air velocity of 1.4 ms-1 retained more HSE compared to those samples dried at higher temperatures. The least retention of HSE was found in samples dried at 80 °C.
Asunto(s)
Desecación , Calor , Mangifera/enzimología , Proteolisis , Humedad , CinéticaRESUMEN
The climacteric nature of mango makes it ripen quickly and increases its postharvest losses. The objective of the present search was to evaluate the efficacy of 1%-3% sodium alginate edible coating for maintaining the postharvest nutritional quality and increasing the marketability of the mango fruit during storage at 15 ± 1°C and 85 ± 1% relative humidity. Results revealed that the quality characteristics including acidity and ascorbic acid content were not affected by the alginate treatments. In contrast, treatment with 3% alginate significantly reduced weight loss and maintained higher firmness (2-fold), total phenols (1.3-fold), and flavonoids content (1.7-fold), as compared with the control. Higher antioxidant capacity was observed in the 3% alginate treatments than the control. Polyphenolxoidase activity in the coated mango remained below 30 U/g FW, while it was increased continuously in the uncoated samples during the storage. Fruits coated with alginate exhibited a higher antioxidant enzyme activity during storage. Sodium alginate had no significant effects on the external color parameters except the a* value. Generally, it was concluded that the mango storage life and its valuable nutritional characteristics were increased by applying the alginate edible coating. PRACTICAL APPLICATIONS: Recently, the edible coatings by natural sources have been widely demanded by consumers due to its nontoxic and biodegradable characteristics. Mango fruits as a climacteric high-nutritional tropical fruit being climatic have a limited shelf life and the maintenance of its quality is still a major challenge for the consumers. The results of this study showed that using sodium alginate coating at 3% concentration had a significant effect on preventing water loss, color changes and preserving antioxidant properties, phenol and flavonoids compounds of mango fruit during storage. Therefore, alginate coating as a biodegradable compound can be used to maintain the quality during the shelf life of fruits and vegetables.
Asunto(s)
Antioxidantes/análisis , Almacenamiento de Alimentos , Mangifera/química , Agua/fisiología , Alginatos/análisis , Ácido Ascórbico/análisis , Color , Frutas/química , Frutas/enzimología , Mangifera/enzimología , Fenoles/análisisRESUMEN
In higher plants, asparagine-linked oligosaccharides (N-glycans) in glycoproteins carry unique carbohydrate epitopes, namely, a core α1,3-fucose and/or a ß1,2-xylose, which are common determinants responsible for the cross-reactivity of plant glycoproteins due to their strong immunogenicity. While these determinants and the relevant genes have been well characterized for herbaceous plants, information concerning whether many food plants cross-react with airborne pollens is not available. In this paper, we report on the characterization of a novel core α1,3-fucosyltransferase gene identified from Mangifera indica L., one of the major plants potentially related to food allergy. Based on sequence information of plant homologues, we amplified a candidate cDNA (MiFUT11) from pericarp tissue. An in vitro assay demonstrated that the recombinant MiFUT11 protein transfers a fucose unit onto both non-fucosylated and core α1,6-fucosylated oligosaccharides. A glycoform analysis using MALDI-TOF mass spectrometry showed that the introduction of the MiFUT11 cDNA increased the production of a core α1,3- and α1,6-fucosylated pauci-mannosidic oligosaccharide in Spodoptera Sf21â¯cells. Our findings suggest that MiFUT11 is a functional core α1,3-fucosyltransferase gene that is involved in the assembly of cross-reactive N-glycans in mango fruit.
Asunto(s)
Carbohidratos/biosíntesis , Frutas/química , Fucosiltransferasas/metabolismo , Mangifera/enzimología , Secuencia de Aminoácidos , Carbohidratos/genética , Carbohidratos/inmunología , Frutas/inmunología , Frutas/metabolismo , Fucosiltransferasas/química , Fucosiltransferasas/genética , Mangifera/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Alineación de SecuenciaRESUMEN
Mango (Mangifera indica L.) is abundant in proanthocyanidins (PAs) that are important for human health and plant response to abiotic stresses. However, the molecular mechanisms involved in PA biosynthesis still need to be elucidated. Anthocyanidin reductase (ANR) catalyzes a key step in PA biosynthesis. In this study, three ANR cDNAs (MiANR1-1,1-2,1-3) were isolated from mango, and expressed in Escherichia coli. In vitro enzyme assay showed MiANR proteins convert cyanidin to their corresponding flavan-3-ols, such as (-)-catechin and (-)-epicatechin. Despite high amino acid similarity, the recombinant ANR proteins exhibited differences in enzyme kinetics and cosubstrate preference. MiANR1-2 and MiANR1-3 have the same optimum pH of 4.0 in citrate buffer, while the optimum pH for MiANR1-1 is pH 3.0 in phosphate buffer. MiANR1-1 does not use either NADPH or NADH as co-substrate while MiANR1-2/1-3 use only NADPH as co-substrate. MiANR1-2 has the highest Km and Vmax for cyanidin, followed by MiANR1-3 and MiANR1-1. The overexpression of MiANRs in ban mutant reconstructed the biosynthetic pathway of PAs in the seed coat. These data demonstrate MiANRs can form the ANR pathway, leading to the formation of two types of isomeric flavan-3-ols and PAs in mango.
Asunto(s)
Mangifera/enzimología , NADH NADPH Oxidorreductasas/química , NADH NADPH Oxidorreductasas/metabolismo , Secuencia de Aminoácidos , Antocianinas/metabolismo , Fenómenos Químicos , Clonación Molecular , Activación Enzimática , Expresión Génica , Concentración de Iones de Hidrógeno , Cinética , Mangifera/clasificación , Mangifera/genética , Redes y Vías Metabólicas , Mutación , NADH NADPH Oxidorreductasas/genética , Filogenia , Proteínas Recombinantes , Análisis Espectral , TemperaturaRESUMEN
Maturity has important effects on the phytochemical and biochemical characteristics of fruits. It affects the quality, nutritional value, harvest time and commercial operations. In this study, Keitt, Sensation and Xiangya mango cultivars in four distinct stages from southwest China were evaluated for their phytochemical profiling and antioxidant activities in real time. Furthermore, the biochemical characteristics indices polyphenol oxidase (PPO), peroxidase (POD), superoxide dismutase (SOD) and pectin methylesterase (PME) activities were determined. Antioxidant compounds such as vitamin C, total phenolic, total flavonoid and total carotenoid content were also analysed. A total of 34 phenolic compounds were identified and quantitatively monitored by UPLC-ESI-QTOF-MS. Consecutive degradation of phenolic acids and its derivatives were observed upon maturity. We found that in addition to carotenoids, phenolic acids could also be used as a measurement index of maturity in mango. Mango juices and its phenolic extracts may be used as potential prebiotics for modulating probiotic proliferation.
Asunto(s)
Antioxidantes/análisis , Mangifera/química , Fitoquímicos/análisis , Prebióticos/análisis , Ácido Ascórbico/análisis , Carotenoides/análisis , Catecol Oxidasa/metabolismo , China , Flavonoides/análisis , Frutas/química , Frutas/enzimología , Hidroxibenzoatos/análisis , Mangifera/enzimología , Valor Nutritivo , Peroxidasa/metabolismo , Proteínas de Plantas/metabolismo , Espectrometría de Masa por Ionización de Electrospray , Superóxido Dismutasa/metabolismoRESUMEN
The effects of 15â¯days of storage at 12⯰C and 7⯰C followed by fruit ripening at 20⯰C on oxidative status, antioxidant defense systems and carotenoid accumulation were studied for two successive years in mango fruits (Mangifera indica L.) cv. Cogshall. Changes in the non-enzymatic (ascorbate) and enzymatic (SOD, CAT, APX, MDHAR, DHAR and GR) antioxidant systems, as well as oxidative parameters (H2O2 and MDA) and the contents of the major carotenoids were measured for three maturity stages, at harvest and after ripening following cold temperature storage. In control conditions (20⯰C), ripening induced an increase in oxidation resulting in ROS production and a decrease in ascorbate content. Fruit tissue protection was activated by means of antioxidant and ascorbate regeneration enzyme systems. Carotenoid accumulated exponentially during ripening. Storage at low temperatures increased respiration crisis intensity and therefore increased oxidation in the fruit pulp. Fruit response to this increase varied according to the maturity stage, i.e., enzymatic responses in younger fruits were very low in comparison to the control, whereas second harvest fruits had a significantly higher degree of enzymatic activity to cope with the oxidative stress. Carotenoid contents decreased with low temperatures and first harvest fruits showed significantly lower values than the control, in opposition to second harvest fruits that appeared not to be affected. We also suggest that, based on a review of the literature, a link can be made between antioxidant system defense and carotenoid metabolism since ROS seems to play a central role as a stress signal in plants.
Asunto(s)
Carotenoides/metabolismo , Mangifera/fisiología , Estrés Oxidativo , Especies Reactivas de Oxígeno/metabolismo , Almacenamiento de Alimentos , Frutas/enzimología , Frutas/crecimiento & desarrollo , Frutas/fisiología , Mangifera/enzimología , Mangifera/crecimiento & desarrollo , TemperaturaRESUMEN
The activity, structure and morphology of mango soluble acid invertase (SAI) were investigated after high pressure processing (HPP) combined with mild temperature at 50-600MPa and 40-50°C. The activity of mango SAI was efficiently reduced by HPP at 50MPa/45 and 50°C, or 600MPa/40, 45 and 50°C, while it was increased by 10-30% after HPP at 50-200MPa/40°C. Significant antagonistic effect of pressure and temperature on the activity of SAI was observed at 50-400MPa/50°C. The secondary structure of SAI was not influenced by HPP. However, its tertiary structure was modified by HPP, and severer modification occurred with higher pressure, higher temperature, and longer treatment time. Results of atomic force microscope suggested that HPP at 400MPa/50°C for 2.5min induced dissociation of SAI, and HPP at 600MPa/50°C for 30min resulted aggregation of SAI.
Asunto(s)
Análisis de los Alimentos/métodos , Manipulación de Alimentos/métodos , Frutas/enzimología , Mangifera/enzimología , Proteínas de Plantas/metabolismo , beta-Fructofuranosidasa/metabolismo , Estabilidad de Enzimas , Cinética , Microscopía de Fuerza Atómica , Proteínas de Plantas/química , Proteínas de Plantas/aislamiento & purificación , Presión , Agregado de Proteínas , Desnaturalización Proteica , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Solubilidad , Relación Estructura-Actividad , Temperatura , beta-Fructofuranosidasa/química , beta-Fructofuranosidasa/aislamiento & purificaciónRESUMEN
The aim of the present work was to model the effect of combined pressure-temperature processing on spoilage-causing enzymes in mango pulp; which conventionally are inactivated using high temperatures leading to inevitable quality losses. The inactivation of enzymes pectin methylesterase (PME), polyphenol oxidase (PPO) and peroxidase (POD) was studied in mango pulp within the pressure, temperature and hold-time ranges of 0.1 to 600MPa, 40 to 70°C and 1s to 90min, respectively. The enzyme inactivation was described as a dual process: initial change in activity during dynamic pressure build-up phase and subsequent decrease under isobaric-isothermal conditions. The former led to considerable increase in activities of all the three enzymes (p<0.05); however, the increased activity reduced with increased intensity of applied pressure-temperature. On the other hand, isobaric-isothermal conditions led to substantial inactivation (p<0.05), with 600MPa/70°C/20min treatment being most effective in reducing the activities of PME, PPO and POD to 32, 15 and 26%, respectively. The enzyme inactivation data was non-linear under isobaric-isothermal conditions and fitted to the nth-order reaction model, indicative of the occurrence of series of reactions possibly due to pressure-temperature interaction effects. The estimated reaction order 'n' was 0.815, 1.106 and 1.137 for PME, PPO and POD, respectively. The estimated reaction rate constant k (min-1) depicted PME to be the most baroresistant enzyme followed by POD and PPO. Temperature and pressure dependency of k was expressed in terms of activation energy and activation volume using the Arrhenius- and Eyring-type relations, respectively. An empirical model with good correlation between actual and predicted data (R2>0.90) was proposed to simulate the rate of enzyme inactivation under isobaric-isothermal conditions as a function of pressure and temperature.
Asunto(s)
Manipulación de Alimentos/métodos , Mangifera , Proteínas de Plantas , Hidrolasas de Éster Carboxílico/química , Hidrolasas de Éster Carboxílico/metabolismo , Hidrolasas de Éster Carboxílico/efectos de la radiación , Catecol Oxidasa/química , Catecol Oxidasa/metabolismo , Catecol Oxidasa/efectos de la radiación , Estabilidad de Enzimas , Calor , Cinética , Mangifera/química , Mangifera/enzimología , Mangifera/efectos de la radiación , Peroxidasa/química , Peroxidasa/metabolismo , Peroxidasa/efectos de la radiación , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Proteínas de Plantas/efectos de la radiación , PresiónRESUMEN
In higher plants, complex type N-glycans contain characteristic carbohydrate moieties that are not found in mammals. In particular, the attachment of the Lewis a (Lea) epitope is currently the only known outer chain elongation that is present in plant N-glycans. Such a modification is of great interest in terms of the biological function of complex type N-glycans in plant species. However, little is known regarding the exact molecular basis underlying their Lea expression. In the present study, we cloned two novel Lewis type fucosyltransferases (MiFUT13) from mango fruit, Mangifera indica L., heterologously expressed the proteins and structurally and functionally characterized them. Using an HPLC-based assay, we demonstrated that the recombinant MiFUT13 proteins mediate the α1,4-fucosylation of acceptor tetrasaccharides with a strict preference for type I-based structure to type II. The results and other findings suggest that MiFUT13s are involved in the biosynthesis of Lea containing glycoconjugates in mango fruits.
Asunto(s)
Clonación Molecular , ADN Complementario/genética , ADN Complementario/metabolismo , Fucosiltransferasas/genética , Fucosiltransferasas/metabolismo , Mangifera/enzimología , Secuencia de Aminoácidos , ADN Complementario/aislamiento & purificación , Fucosiltransferasas/aislamiento & purificación , Alineación de SecuenciaRESUMEN
Alphonso is known as the "King of mangos" due to its unique flavor, attractive color, low fiber pulp and long shelf life. We analyzed the transcriptome of Alphonso mango through Illumina sequencing from seven stages of fruit development and ripening as well as flower. Total transcriptome data from these stages ranged between 65 and 143 Mb. Importantly, 20,755 unique transcripts were annotated and 4,611 were assigned enzyme commission numbers, which encoded 142 biological pathways. These included ethylene and flavor related secondary metabolite biosynthesis pathways, as well as those involved in metabolism of starch, sucrose, amino acids and fatty acids. Differential regulation (p-value ≤ 0.05) of thousands of transcripts was evident in various stages of fruit development and ripening. Novel transcripts for biosynthesis of mono-terpenes, sesqui-terpenes, di-terpenes, lactones and furanones involved in flavor formation were identified. Large number of transcripts encoding cell wall modifying enzymes was found to be steady in their expression, while few were differentially regulated through these stages. Novel 79 transcripts of inhibitors of cell wall modifying enzymes were simultaneously detected throughout Alphonso fruit development and ripening, suggesting controlled activity of these enzymes involved in fruit softening.
Asunto(s)
Frutas/crecimiento & desarrollo , Frutas/genética , Mangifera/crecimiento & desarrollo , Mangifera/genética , Odorantes , Transcripción Genética , Pared Celular/metabolismo , Inhibidores Enzimáticos/farmacología , Flores/genética , Frutas/efectos de los fármacos , Perfilación de la Expresión Génica , Regulación del Desarrollo de la Expresión Génica/efectos de los fármacos , Regulación de la Expresión Génica de las Plantas/efectos de los fármacos , Ontología de Genes , Genes de Plantas , Glicósido Hidrolasas/metabolismo , Mangifera/efectos de los fármacos , Mangifera/enzimología , Filogenia , ARN Mensajero/genética , ARN Mensajero/metabolismo , Reproducibilidad de los Resultados , Transcripción Genética/efectos de los fármacos , Transcriptoma/genéticaRESUMEN
Uniqueness and diversity of mango flavour across various cultivars are well known. Among various flavour metabolites lactones form an important class of aroma volatiles in certain mango varieties due to their ripening specific appearance and lower odour detection threshold. In spite of their biological and biochemical importance, lactone biosynthetic pathway in plants remains elusive. Present study encompasses quantitative real-time analysis of 9-lipoxygenase (Mi9LOX), epoxide hydrolase 2 (MiEH2), peroxygenase, hydroperoxide lyase and acyl-CoA-oxidase genes during various developmental and ripening stages in fruit of Alphonso, Pairi and Kent cultivars with high, low and no lactone content and explains their variable lactone content. Study also covers isolation, recombinant protein characterization and transient over-expression of Mi9LOX and MiEH2 genes in mango fruits. Recombinant Mi9LOX utilized linoleic and linolenic acids, while MiEH2 utilized aromatic and fatty acid epoxides as their respective substrates depicting their role in fatty acid metabolism. Significant increase in concentration of δ-valerolactone and δ-decalactone upon Mi9LOX over-expression and that of δ-valerolactone, γ-hexalactone and δ-hexalactone upon MiEH2 over-expression further suggested probable involvement of these genes in lactone biosynthesis in mango.
Asunto(s)
Epóxido Hidrolasas/genética , Lactonas/química , Lipooxigenasa/genética , Mangifera/enzimología , Proteínas de Plantas/genética , Aldehído-Liasas/química , Sistema Enzimático del Citocromo P-450/química , Ácidos Grasos , Frutas/química , Mangifera/genética , Oxigenasas de Función Mixta/química , Pironas/químicaRESUMEN
We studied a mango glutathione S-transferase (GST) (Mangifera indica) bound to glutathione (GSH) and S-hexyl glutathione (GSX). This GST Tau class (MiGSTU) had a molecular mass of 25.5 kDa. MiGSTU Michaelis-Menten kinetic constants were determined for their substrates obtaining a Km, Vmax and kcat for CDNB of 0.792 mM, 80.58 mM min-1 and 68.49 s-1 respectively and 0.693 mM, 105.32 mM min-1 and 89.57 s-1, for reduced GSH respectively. MiGSTU had a micromolar affinity towards GSH (5.2 µM) or GSX (7.8 µM). The crystal structure of the MiGSTU in apo or bound to GSH or GSX generated a model that explains the thermodynamic signatures of binding and showed the importance of enthalpic-entropic compensation in ligand binding to Tau-class GST enzymes.
Asunto(s)
Glutatión Transferasa/metabolismo , Mangifera/enzimología , Glutatión/metabolismo , Glutatión Transferasa/química , Cinética , Unión ProteicaRESUMEN
Flavour of ripe Alphonso mango is invariably dominated by the de novo appearance of lactones and furanones during ripening. Of these, furanones comprising furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone) are of particular importance due to their sweet, fruity caramel-like flavour characters and low odour detection thresholds. We isolated a 1056 bp complete open reading frame of a cDNA encoding S-adenosyl-L-methionine-dependent O-methyltransferase from Alphonso mango. The recombinantly expressed enzyme, MiOMTS showed substrate specificity towards furaneol and protocatechuic aldehyde synthesizing mesifuran and vanillin, respectively, in an in vitro assay reaction. A semi-quantitative PCR analysis showed fruit-specific expression of MiOMTS transcripts. Quantitative real-time PCR displayed ripening-related expression pattern of MiOMTS in both pulp and skin of Alphonso mango. Also, early and significantly enhanced accumulation of its transcripts was detected in pulp and skin of ethylene-treated fruits. Ripening-related and fruit-specific expression profile of MiOMTS and substrate specificity towards furaneol is a suggestive of its involvement in the synthesis of mesifuran in Alphonso mango. Moreover, a significant trigger in the expression of MiOMTS transcripts in ethylene-treated fruits point towards the transcriptional regulation of mesifuran biosynthesis by ethylene.
Asunto(s)
Mangifera/enzimología , Metiltransferasas/genética , Secuencia de Aminoácidos , Clonación Molecular , ADN Complementario/genética , Metiltransferasas/química , Metiltransferasas/metabolismo , Homología de Secuencia de AminoácidoRESUMEN
A green and cost-effective process for the convenient synthesis of acylphloroglucinol 3-C-glucosides from 2-O-glucosides was exploited using a novel C-glycosyltransferase (MiCGTb) from Mangifera indica. Compared with previously characterized CGTs, MiCGTb exhibited unique de-O-glucosylation promiscuity and high regioselectivity toward structurally diverse 2-O-glucosides of acylphloroglucinol and achieved high yields of C-glucosides even with a catalytic amount of uridine 5'-diphosphate (UDP). These findings demonstrate for the first time the significant potential of a single-enzyme approach to the synthesis of bioactive C-glucosides from both natural and unnatural acylphloroglucinol 2-O-glucosides.
Asunto(s)
Glucósidos/química , Glucósidos/síntesis química , Glicósidos/química , Glicósidos/síntesis química , Glicosiltransferasas/química , Mangifera/química , Mangifera/enzimología , Cromatografía Líquida de Alta Presión , Glicósidos/metabolismo , Glicosilación , Glicosiltransferasas/metabolismo , Mangifera/metabolismo , Estructura MolecularRESUMEN
UNLABELLED: 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. PRACTICAL APPLICATION: Exploration of additional hurdles such as pH, TSS, and temperature for enzyme inactivation during high pressure processing of fruits is useful from industrial point of view, as these parameters play key role in preservation process design.
Asunto(s)
Hidrolasas de Éster Carboxílico/química , Catecol Oxidasa/química , Manipulación de Alimentos/métodos , Frutas/enzimología , Mangifera/enzimología , Peroxidasa/química , Presión , Humanos , Concentración de Iones de Hidrógeno , Cinética , Solubilidad , TemperaturaRESUMEN
The catalytic promiscuity of the novel benzophenone C-glycosyltransferase, MiCGT, which is involved in the biosynthesis of mangiferin from Mangifera indica, was explored. MiCGT exhibited a robust capability to regio- and stereospecific C-glycosylation of 35 structurally diverse druglike scaffolds and simple phenolics with UDP-glucose, and also formed O- and N-glycosides. Moreover, MiCGT was able to generate C-xylosides with UDP-xylose. The OGT-reversibility of MiCGT was also exploited to generate C-glucosides with simple sugar donor. Three aryl-C-glycosides exhibited potent SGLT2 inhibitory activities with IC50 â values of 2.6×, 7.6×, and 7.6×10(-7) M, respectively. These findings demonstrate for the first time the significant potential of an enzymatic approach to diversification through C-glycosidation of bioactive natural and unnatural products in drug discovery.
Asunto(s)
Glicosiltransferasas/metabolismo , Mangifera/enzimología , Glucosa/análogos & derivados , Glucosa/metabolismo , Glicósidos/química , Glicósidos/metabolismo , Glicosilación , Glicosiltransferasas/química , Mangifera/química , Mangifera/metabolismo , Especificidad por Sustrato , Uridina Difosfato/análogos & derivados , Uridina Difosfato/metabolismo , Xantonas/metabolismo , Xilosa/análogos & derivados , Xilosa/metabolismoRESUMEN
The effects of a reduction in water supply during fruit development and postharvest fruit ripening on the oxidative status and the antioxidant defense system were studied in the mango fruit (Mangifera indica L.) cv. Cogshall. Changes in non-enzymatic (ascorbate) and enzymatic (SOD, CAT, APX, MDHAR, DHAR and GR) antioxidants, as well as oxidative parameters (H2O2 and MDA) and major carotenoids, were measured in unripe and ripe fruits from well-irrigated and non-irrigated trees. Under non-limiting water supply conditions, ripening induced oxidation as a result of the production of ROS and decreased ascorbate content. Antioxidant enzymatic systems were activated to protect fruit tissues and to regenerate the ascorbate pool. The carotenoid pool, mainly represented by ß-carotene and esterified violaxanthine isomers, accumulated naturally during mango ripening. The suppression of irrigation decreased fruit size and induced accumulation of ABA and of its storage form, ABA-GE, in fruit pulp from the earliest harvest. It also increased oxidation, which was observable by the high levels of ascorbate measured at the early stages at harvest, and by the delay in the time it took to reach the pseudo constant carotene-to-xanthophyll ratio in ripe fruits. Nevertheless, differences between the irrigation treatments on the antioxidant system in ripe fruits were not significant, mainly because of the drastic changes in this system during ripening.
Asunto(s)
Antioxidantes/metabolismo , Carotenoides/metabolismo , Mangifera/metabolismo , Estrés Oxidativo , Agua/metabolismo , Riego Agrícola , Frutas/enzimología , Frutas/crecimiento & desarrollo , Frutas/metabolismo , Mangifera/enzimologíaRESUMEN
The objectives of this work were to evaluate infrared (IR) dry blanching in comparison with conventional water blanching prior to hot air drying of mango to inactivate polyphenol oxidase (PPO) and ascorbic acid oxidase (AAO) enzymes, and to study its effect on color change and retention of vitamin C and ß-carotene. Mango cylinders were blanched under similar temperature-time conditions either by IR heating or by immersion in a water bath during 2 min at 90 °C (high-temperature-short-time-HTST) or for 10 min at 65 °C (low-temperature-long-time-LTLT). After blanching mango was hot air dried at 70 °C. PPO was completely inactivated during the blanching treatments, but AAO had a moderate remaining activity after LTLT treatment (â¼30%) and a low remaining activity after HTST treatment (9% to 15%). A higher retention of vitamin C was observed in mango subjected to IR dry blanching, 88.3 ± 1.0% (HTST) and 69.2 ± 2.9% (LTLT), compared with water blanching, 61.4 ± 5.3% (HTST) and 50.7 ± 9.6% (LTLT). All-trans-ß-carotene retention was significantly higher in water blanched dried mango, 93.2 ± 5.2% (LTLT) and 91.4 ± 5.1% (HTST), compared with IR dry blanched, 73.6 ± 3.6% (LTLT) and 76.9 ± 2.9% (HTST). Increased levels of 13-cis-ß-carotene isomer were detected only in IR dry blanched mango, and the corresponding dried mango also had a slightly darker color. IR blanching of mango prior to drying can improve the retention of vitamin C, but not the retention of carotenoids, which showed to be more dependent on the temperature than the blanching process. A reduction of drying time was observed in LTLT IR-blanching mango.