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1.
Environ Sci Pollut Res Int ; 31(13): 19294-19303, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38361100

RESUMO

In this work, the adsorption of nickel ions from a real effluent from a metal-mechanic industry was investigated in a fixed-bed column using biochar. Biochar was prepared from winemaking residues originating from the Beifiur® composting process. The use of wine industry residues as precursor materials for biochar production is established in biomass residue valorization using the existing logistics and the lowest possible number of manipulations and pre-treatments. The results found in the work showed that the optimal conditions for nickel adsorption in fixed-bed columns were bed height (Z) of 7 cm, initial nickel concentration (C0) of 1.5 mg L-1, and flow rate (Q) of 18 mL min-1. In this condition, the maximum adsorption capacity of the column was 0.452 mg g-1, the mass transfer zone (Zm) was 3.3 cm, the treated effluent volume (Veff) was 9.72 L, and the nickel removal (R) was 92.71%. The Yoon-Nelson and BDST dynamic models were suitable to represent the breakthrough curves of nickel adsorption. Finally, the fixed-bed column adsorption using biochar from winemaking residues proved to be a promising alternative for nickel removal from real industrial effluents.


Assuntos
Poluentes Químicos da Água , Purificação da Água , Níquel/química , Purificação da Água/métodos , Adsorção , Carvão Vegetal/química , Poluentes Químicos da Água/análise
2.
Food Chem ; 286: 98-105, 2019 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-30827672

RESUMO

Three cooking temperatures (72, 80, and 88 °C) were applied to two rice genotypes (Puitá Inta CL and INOV CL) for preparing quick cooking brown rice. Samples were analyzed for cooking time, color, scanning electron microscopy (SEM), damaged grains, amylose, protein content and extractability, differential scanning calorimetry (DSC), X-ray diffraction (XRD), sensory properties, and in vitro digestion. Cooking time was reduced from 23.0-23.6 to 5.5-6.9 min when the highest temperature was applied, depending on genotype. The greatest grain deformation was observed for treatments from Puitá Inta CL. XRD showed greater ability of brown rice from Puitá Inta CL to gelatinize at 88 °C. Appearance, texture, and flavor of quick cooking brown rice prepared at 88 °C was inferior to its brown rice counterparts. Starch digestibility decreased by around 20-22% in 88 °C-prepared-quick cooking brown rice. Lower digestibility values were determined for 88 °C-treated-INOV CL, and were associated with grain integrity.


Assuntos
Culinária/métodos , Qualidade dos Alimentos , Oryza/química , Amilose/análise , Amilose/química , Varredura Diferencial de Calorimetria , Cor , Digestão , Genótipo , Humanos , Microscopia Eletrônica de Varredura , Oryza/genética , Proteínas de Vegetais Comestíveis/análise , Proteínas de Vegetais Comestíveis/química , Proteínas de Vegetais Comestíveis/farmacocinética , Amido/farmacocinética , Paladar , Temperatura , Difração de Raios X
3.
Int J Biol Macromol ; 126: 834-841, 2019 Apr 01.
Artigo em Inglês | MEDLINE | ID: mdl-30610943

RESUMO

The objective of this study was to immobilize α-amylase in ultrafine polyvinyl alcohol (PVA) fibers by electrolysis and to evaluate its stability at different temperatures and pHs using various starch substrates such as corn starch and germinated and ungerminated wheat starches. The α-amylase-loaded ultrafine fibers were characterized by scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FT-IR), and loadability and enzymatic activity evaluations. Incorporation of the enzyme resulted in a slight change in fiber morphology; the fibers became flatter and thicker with increasing enzyme concentration. The mean diameters ranged from 187 to 282 nm. FT-IR spectra indicated that the enzyme was incorporated into the fibers. PVA showed a high loading capacity for α-amylase at all concentrations tested (1.0, 1.5, and 2.0% w/v), indicating that PVA is an excellent support. The enzymatic activity of α-amylase was tested on the different starch substrates; the activity was higher in the immobilized form than in the free form. Enzymatic immobilization improved the stability of α-amylase over a wide range of temperatures and pHs. Enzymatic activity was highest when germinated wheat starch was used as the substrate at different temperatures and pHs, indicating great potential for its application in hydrolysis with α-amylase.


Assuntos
Enzimas Imobilizadas/metabolismo , Álcool de Polivinil/química , alfa-Amilases/metabolismo , Aspergillus/enzimologia , Estabilidade Enzimática , Concentração de Íons de Hidrogênio , Espectroscopia de Infravermelho com Transformada de Fourier , Temperatura
4.
Int J Biol Macromol ; 118(Pt B): 1676-1684, 2018 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-29981822

RESUMO

Xylanase (EC 3.2.1.8) is a key enzyme for degradation of xylan. A limitation of xylanase application in food and beverage industries is the low enzyme activity and stability at a wide pH and temperature range. In the present study, different levels of pure xylanase (XY) and xylanase-ß-cyclodextrin (XY-ß-CD) inclusion complex were immobilized in polyvinyl alcohol (PVA) via electrospinning. Morphological and structural characteristics of obtained fibers were investigated by Fourier-transformed infrared spectroscopy (FTIR), scanning electron microscopy (SEM), and X-ray diffraction (XRD) analyzes. Inclusion complex formation was evaluated by FTIR, XRD, and differential scanning calorimetry (DSC) analyzes. Obtained electrospun fibers showed a smooth surface with average diameter from around 200 to 600 nm. Greater diameters were observed at higher xylanase levels. In addition, inclusion complex provided thicker fibers than pure xylanase. Optimum xylanase activity changed from 60 to 70 °C when enzyme was immobilized in PVA. FTIR results suggest a more efficient enzyme conformation after immobilization. The greatest xylanase efficiency of immobilization was achieved at 0.5%-XY, with specific activity of 59.73 µM/min/mg of immobilized xylanase. Xylanase immobilized in PVA fibers exhibited higher activity at extremer pH conditions (4, 5, 7, and 8), as compared to free xylanase.


Assuntos
Endo-1,4-beta-Xilanases/química , Enzimas Imobilizadas , Álcool de Polivinil/química , beta-Ciclodextrinas/química , Ativação Enzimática , Concentração de Íons de Hidrogênio , Nanofibras/química , Nanofibras/ultraestrutura , Espectroscopia de Infravermelho com Transformada de Fourier , Temperatura , Difração de Raios X
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