Cellobiose hydrolysis
was investigated over acid-layered solids
H-[Al]-magadiite in a continuously operated fixed bed flow reactor.
Catalysts containing different Si/Al molar ratios were synthesized
to tune distinct acidity. The incorporation of Al into the silicate
framework created indeed active acid sites for cellobiose hydrolysis
reaction. The catalyst with the highest Al content (Si/Al = 17) was
the most active, displaying a constant cellobiose conversion of ∼80%.
Glucose was the main product observed; however, fructose and 5-hydroxymethylfurfural
(HMF) were also detected. The results indicated that H-[Al]-magadiite
catalysts have Lewis acid sites that are active even in the presence
of water. Characterization analysis performed on catalysts after the
reaction showed that the [Al]-magadiite structure was maintained and
no Al leaching was observed.
Ball-milled MCM-22 and dried mother liquor seeds proved to be effective in the synthesis of the MCM-22P lamellar precursor with a low Si/Al ratio. Crystallization times were reduced from 25 to 2–4 days with a considerable decrease in crystallite sizes.
Vapor adsorption experiments support the catalytic results of H-[Al]-magadiite and H-[Al]-RUB-18, once the interlamellar space swell and accommodate substrate molecules.
Introduction: Capillary zone electrophoresis with direct UV detection (CZE-UV) was used to investigate the hypothesis about the extract of Baccharis trimera enzymatic activities as an analytical approach to monitoring the phenomenon.Objective: The aim of this work was to investigate enzymatic bioactivities of the hydroalcoholic and infusion extracts of B. trimera through screening evaluation of the inhibition of the enzymes acetylcholinesterase (AChE) and α-glycosidase (α-GLY).Method: An alternative approach using CZE-UV to hydroalcoholic and infusion extracts of B. trimera monitoring was applied to evaluate the inhibition ability of the enzymes AChE and α-GLY. The result of the reaction of acetylthiocholine (AThCh) with AChE was thiocholine (TCh) and acetic acid, and from the amount of TCh generated, the AChE inhibition was calculated. For the inhibition study of the two enzymes, the reactions of the extracts were optimised to be performed in situ, inside the capillary column, and the introduction of the solutions was performed through ordered sequential plug injections.Results: Samples extracted with 70% ethanol presented 7.80% inhibition for AChE and 0.51% for α-GLY, while samples extracted with 96% ethanol resulted in 6.89% inhibition for AChE and no inhibition activity for α-GLY.
Conclusion:In the present work, the potentialities of CZE-UV for the study of hydroalcoholic and infusion extracts of B. trimera were demonstrated. The experimental results were useful for the calculation of the percentage of the inhibition activities of the AChE and α-GLY enzymes.
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