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1.
Phytochemistry ; 199: 113175, 2022 Jul.
Article in English | MEDLINE | ID: mdl-35398331

ABSTRACT

Identifying compounds present in the sugarcane epicuticular wax and using these compounds to classify the genotypes susceptible and resistant to the initial attack of sugarcane borer (Diatraea saccharalis) was the aim of this study. A greenhouse experiment was performed in a factorial scheme with and without borer infestation using genotypes previously characterized as resistant or susceptible in field-based experiments. Sugarcane whorls of six-month-old plants were collected before (BI) and after (AI) 72 h of sugarcane borer infestation. The sugarcane epicuticular wax was extracted in both times, i.e., BI and AI and its chemical composition was assessed by gas chromatography coupled to mass spectrometry (GC-MS). Twenty-five compounds were identified for both BI and AI. Classification models were built using partial least squares for discriminant analysis (PLS-DA) and linear discriminant analysis (LDA). Variable selection methods were used to improve the classification models. Ordered predictors selection for discriminant analysis (OPSDA) selected compounds that correctly classified all the test samples before borer infestation (Error = 0.000), and exhibited the most suitable classification parameters for the test set after borer infestation (Error = 0.111). The C30 pentacyclic triterpene friedelin and a high alcohol/aldehyde ratio were associated with the classification of resistant genotypes. Our findings have applicability in developing a screening methodology for breeding programs interested in identifying genotypes resistant to the initial feeding of sugarcane borer.


Subject(s)
Moths , Saccharum , Animals , Edible Grain , Genotype , Larva , Plant Breeding , Saccharum/genetics
2.
Anal Chem ; 93(33): 11388-11397, 2021 08 24.
Article in English | MEDLINE | ID: mdl-34375077

ABSTRACT

The construction of a dispersive optical spectrometer using three-dimensional (3D) design software and printing, without applying any optical adjustments, its validation, and application to quantification of ethanol in multiproduct liquids, is the objective of this work. A 3D design software was used to design a near-infrared (NIR) spectrometer in the region from 800 to 1600 nm from the dimensions of commercially available optical components. The project was printed on a polymer filament 3D printer, and the components were fitted to the printed part. Software calculations using the model design parameters were applied to attribute the wavelength values to the abscissa axis in the spectra and estimate errors due to 3D printing limitations. The alignment of the spectrum was proven using the chloroform absorbance spectrum, which presented a maximum mispositioning of 4.1 nm concerning the literature data and effective bandwidths equivalent to commercial instruments. The 3D-printed instrument was applied to quantify ethanol in samples of cachaça, rum, beer, brandy, whiskey, vodka, mouth wash, alcohol gel, and commercial alcohol solutions. Partial least-squares regression models were built for the 3D-printed instrument and two commercial NIR instruments, the MPA II (Bruker) and the NIR DLP NIRscan (Texas Instruments), using a group of 180 standards. The three instruments reached excellent predictive capability with similar root mean square error of cross-validation (2.36-2.68) and prediction (2.31-2.87). The correlation coefficient of cross-validation and prediction for all models were between 0.97 and 0.98. The results show the feasibility of building a 3D-printed dispersive spectrometer ready for application with the simple docking of the optics, presenting acceptable accuracy to the project design concerning the printing limitations.


Subject(s)
Ethanol , Polymers , Calibration , Printing, Three-Dimensional , Software
3.
Int J Biol Macromol ; 161: 204-213, 2020 Oct 15.
Article in English | MEDLINE | ID: mdl-32522547

ABSTRACT

Chardonnay grape pomace was evaluated as a source of pectin. A central composite design was used in order to determine the effect of pH, extraction time (Et) and liquid: solid ratio (LS) on the yield and uronic acid (UA) content of the pectins extracted using boiling HNO3 solution. The optimized extraction condition to reach the maximum yield and UA was pH = 2.08, Et = 135.23 min and LS = 35.11 ml/g, resulting in theoretical yield of 12.8% and UA of 64.4%. The experimental yield of the pectic fraction obtained under the optimized conditions (GPOP) was 11.1% and the UA was 56.8%. GPOP had ~25% glucose. It was treated with α-amylase and amyloglucosidase, resulting in the fraction α-GPOP. The starch-free pectic fraction was composed of 63.5% UA, 7.8% rhamnose, 6.0% arabinose, 13.6% galactose and minor amounts of other neutral monosaccharides. It contained a low-methoxyl pectin (degree of methyl-esterification 18.1%) and had an average molar mass of 154,100 g/mol. It consisted of 55.7% homogalacturonan and 35.2% rhamnogalacturonan I (RG-I). NMR analyses suggest that RG-I portion of α-GPOP is highly branched by short chains or single residues of arabinose and galactose.


Subject(s)
Pectins/chemistry , Pectins/isolation & purification , Plant Extracts/chemistry , Plant Extracts/isolation & purification , Vitis/chemistry , Chemical Fractionation , Chromatography, Gel , Hydrogen-Ion Concentration , Magnetic Resonance Spectroscopy , Monosaccharides , Uronic Acids
4.
Int J Biol Macromol ; 153: 995-1004, 2020 Jun 15.
Article in English | MEDLINE | ID: mdl-31751721

ABSTRACT

Nanostructures from conjugates of tara gum and α-lactalbumin were obtained via the heat-gelation process with pH adjustment. The conjugates were produced by Maillard reaction using the dry-heating method in lyophilized or spray-dried mixtures of TG and α-la and were characterized by browning index (BI) and percentage of free amino groups (% FAG). Nanostructured systems were characterized by dynamic light scattering, ζ-potential, circular dichroism, and intrinsic fluorescence to evaluate the structures. The most appropriate time of conjugation was 2 days. The spray-dried and lyophilized mixtures presented different values of BI and % FAG (p < 0.05), indicating that the glycosylation was more intense in lyophilized mixtures. Nanostructures with average sizes lower than 300 nm were formed under different conditions of temperature, pH, and heating time. Analyses of circular dichroism and intrinsic fluorescence showed conformational changes in the nanostructures, mainly a decrease in the α-helix content in spray-dried systems. The characteristics presented by the studied systems showed that it is possible to obtain nanostructures from conjugates of tara gum and α-lactalbumin.


Subject(s)
Lactalbumin/chemistry , Nanostructures/chemistry , Plant Gums/chemistry , Freeze Drying , Models, Molecular , Protein Conformation
5.
Int J Biol Macromol ; 117: 385-391, 2018 Oct 01.
Article in English | MEDLINE | ID: mdl-29753767

ABSTRACT

A central composite experimental design was used to evaluate the influence of pH, extraction time and liquid:solid ratio on the yield and uronic acid content of the pectin from ponkan peel. The response surface methodology showed that the yield is positively influenced by lower pHs, longer extraction times and higher liquid:solid ratio, whereas the uronic acid content decreases with increasing extraction time. The conditions that resulted in the highest yield and highest uronic acid content were defined as pH 1.6, extraction time of 100 min and liquid:solid ratio of 36 mL/g. The pectin obtained under these conditions (PPOP) had an experimental yield of 25.6%, below the predicted theoretical value despite the good fit of the model (R2 = 0.96) and the galacturonic acid content was 84.5%, in close agreement with the predicted theoretical value. PPOP was composed mainly of a homogalacturonan with degree of methyl esterification of 85.7% and a rhamnogalacturonan I region mainly branched by galactans. In addition, PPOP had a very low degree of acetylation (0.1%) and average molar mass of 80,650 g/mol, determined by light scattering. The results showed that ponkan peel may be used as a source of citrus pectin in the regions where this species is cultivated.


Subject(s)
Citrus/chemistry , Pectins/chemistry , Pectins/isolation & purification , Hydrogen-Ion Concentration , Pressure , Proton Magnetic Resonance Spectroscopy , Uronic Acids/analysis
6.
Food Res Int ; 100(Pt 1): 674-681, 2017 10.
Article in English | MEDLINE | ID: mdl-28873736

ABSTRACT

Combination of ß-lactoglobulin (ß-Lg) and lactoferrin (Lf), biomacromolecules derived from bovine whey, was used in the formation of supramolecular structures by thermal gelation technique to adjust the pH. Furthermore, the influence of the molar ratio, temperature, pH, and heating time in the formation of supramolecular structures were also studied. The characterization of the protein supramolecular structures was performed using dynamic light scattering, zeta potential measurements, molecular spectrofluorimetry, and circular dichroism spectroscopy. The thermal behavior of the pure proteins was investigated by differential scanning calorimetry. The protein denaturation temperatures were of around 85°C for the ß-Lg and around 52°C and 85°C (a small portion) for the Lf. The protein molar ratio of 2:1 Lf/ß-Lg was used to form the structures, whose characterization showed that the best conditions of supramolecular structure formation occurred at pH6.5 and at temperatures of 62.5°C. In those conditions, more stable systems with reduced hydrophobic surface and average sizes between 30 and 100nm were generated. The correlation between pH and temperature suggests that the method of preparation of the supramolecular structure affects its size during storage.


Subject(s)
Lactoferrin/chemistry , Lactoferrin/metabolism , Lactoglobulins/chemistry , Lactoglobulins/metabolism , Multiprotein Complexes/chemistry , Multiprotein Complexes/metabolism , Animals , Calorimetry, Differential Scanning , Cattle , Hot Temperature , Hydrophobic and Hydrophilic Interactions , Lactoferrin/analysis , Lactoglobulins/analysis , Multiprotein Complexes/analysis , Protein Stability , Spectrum Analysis
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