Using Fly Ash Wastes for the Development of New Building Materials with Improved Compressive Strength

Fly ash wastes (silica, aluminum and iron-rich materials) could be smartly valorized by their incorporation in concrete formulation, partly replacing the cement. The necessary binding properties can be accomplished by a simple procedure: an alkali activation process, involving partial hydrolysis, followed by gel formation and polycondensation. The correlations between the experimental fly ash processing conditions, particle characteristics (size and morphology) and the compressive strength values of the concrete prepared using this material were investigated by performing a parametric optimization study to deduce the optimal processing set of conditions. The alkali activation procedure included the variation of the NaOH solutions concentration (8–12 M), temperature values (25–65 °C) and the liquid/solid ratio (1–3). The activation led to important modifications of the crystallography of the samples (shown by powder XRD analysis), their morphologies (seen by SEM), particle size distribution and Blaine surface values. The values of the compressive strength of concrete prepared using fly ash derivatives were between 16.8–22.6 MPa. Thus, the processed fly ash qualifies as a proper potential building material, solving disposal-associated problems, as well as saving significant amounts of cement consumed in concrete formulation.

Direct Diels-Alder reaction of chitin derived 3-acetamido-5-acetylfuran

The Diels-Alder (DA) reaction of biomass derived furans is an emerging technology for the preparation of new molecular entities and “drop-in” commodity chemicals. In this work we address the challenge of the direct use of electron-poor furanic platforms as dienes through the use of an unexplored chitin derived furan, 3-acetamido-5-acetylfuran (3A5AF). The 3-acetamido group promoted a remarkable increase in the kinetics of the DA allowing for the preparation of 7-oxanorbornenes (7-ONB) at 50 ºC. Partial hydrolysis of the enamide to hemi-acylaminals was possible upon fine tuning of the reaction conditions, disabling retro-DA processes. Finally, DA reaction of the reduced form of 3A5AF allowed quantitative formation of 7-ONB in aqueous condition after 10 minutes. Certanly these are the first steps for expanding the toolbox of chitin derived 3A5AF as diene.

A Novel Agarase, Gaa16B, Isolated from the Marine Bacterium Gilvimarinus agarilyticus JEA5, and the Moisturizing Effect of Its Partial Hydrolysis Products

We recently identified a β-agarase, Gaa16B, in the marine bacterium Gilvimarinus agarilyticus JEA5. Gaa16B, belonging to the glycoside hydrolase 16 family of β-agarases, shows less than 70.9% amino acid similarity with previously characterized agarases. Recombinant Gaa16B lacking the carbohydrate-binding region (rGaa16Bc) was overexpressed in Escherichia coli and purified. Activity assays revealed the optimal temperature and pH of rGaa16Bc to be 55 ∘C and pH 6–7, respectively, and the protein was highly stable at 55 ∘C for 90 min. Additionally, rGaa16Bc activity was strongly enhanced (2.3-fold) in the presence of 2.5 mM MnCl2. The Km and Vmax of rGaa16Bc for agarose were 6.4 mg/mL and 953 U/mg, respectively. Thin-layer chromatography analysis revealed that rGaa16Bc can hydrolyze agarose into neoagarotetraose and neoagarobiose. Partial hydrolysis products (PHPs) of rGaa16Bc had an average molecular weight of 88–102 kDa and exhibited > 60% hyaluronidase inhibition activity at a concentration of 1 mg/mL, whereas the completely hydrolyzed product (CHP) showed no hyaluronidase at the same concentration. The biochemical properties of Gaa16B suggest that it could be useful for producing functional neoagaro-oligosaccharides. Additionally, the PHP of rGaa16Bc may be useful in promoting its utilization, which is limited due to the gel strength of agar.

Antioxidant activity of Gryllus assimilis meal hydrolysed by Aspergillus oryzae proteases

The consumption of insects is an alternative protein source of a high nutritional value, in comparison to other traditional animal and vegetable proteins, and is suitable for food and as animal feed. This work aimed to study the antioxidant activity of cricket meal (Gryllus assimilis) partially hydrolysed by proteases from a Aspergillus oryzae, which was cultivated in the cricket meal. The cricket meal showed great potential for obtaining protease from A. oryzae, with an average enzymatic activity of 112±8 U/g of dry substrate after 96 h of fermentation. The enzymatic extract applied to the cricket meal increased its antioxidant properties, increasing the reduction of the 2,2-diphenyl-1-picrylhydrazyl radical by 2 times, compared to non-hydrolysed cricket meal. These initial results are promising, demonstrating the benefits of the partial hydrolysis of cricket meal.

Antarctic polyester hydrolases degrade aliphatic and aromatic polyesters at moderate temperatures

Polyethylene terephthalate (PET) is one of the most widely used synthetic plastics in the packaging industry, and consequently has become one of the main components of plastic waste found in the environment. However, several microorganisms have been described to encode enzymes that catalyze the depolymerization of PET. While most known PET hydrolases are thermophilic and require reaction temperatures between 60°C to 70°C for an efficient hydrolysis of PET, a partial hydrolysis of amorphous PET at lower temperatures by the polyester hydrolase Is PETase from the mesophilic bacterium Ideonella sakaiensis has also been reported. We show that polyester hydrolases from the Antarctic bacteria Moraxella sp. strain TA144 (Mors1) and Oleispira antarctica RB-8 (OaCut) were able to hydrolyze the aliphatic polyester polycaprolactone as well as the aromatic polyester PET at a reaction temperature of 25°C. Mors1 caused a weight loss of amorphous PET films and thus constitutes a PET-degrading psychrophilic enzyme. Comparative modelling of Mors1 showed that the amino acid composition of its active site resembled both thermophilic and mesophilic PET hydrolases. Lastly, bioinformatic analysis of Antarctic metagenomic samples demonstrated that members of the Moraxellaceae family carry candidate genes coding for further potential psychrophilic PET hydrolases. IMPORTANCE A myriad of consumer products contains polyethylene terephthalate (PET), a plastic that has accumulated as waste in the environment due to its long-term stability and poor waste management. One promising solution is the enzymatic biodegradation of PET, with most known enzymes only catalyzing this process at high temperatures. Here, we bioinformatically identified and biochemically characterized an enzyme from an Antarctic organism that degrades PET at 25°C with similar efficiency than the few PET-degrading enzymes active at moderate temperatures. Reasoning that Antarctica harbors other PET-degrading enzymes, we analyzed available data from Antarctic metagenomic samples and successfully identified other potential enzymes. Our findings contribute to increasing the repertoire of known PET-degrading enzymes that are currently being considered as biocatalysts for the biological recycling of plastic waste.

Effect of mare and cow kumis on gastric secretion

Kumis is a product of two fermentation, brought to a well-known equilibrium - lactic acid and alcohol. In this case, milk proteins, mainly casein, undergo partial hydrolysis, passing into solution.

Gelatinization or Pasting? The Impact of Different Temperature Levels on the Saccharification Efficiency of Barley Malt Starch

Efficient enzymatic hydrolysis of cereal starches requires a proper hydrothermal pre-treatment. For malted barley, however, the exact initial temperature is presently unknown. Therefore, samples were micro-mashed according to accurately determined gelatinization and pasting temperatures. The impact on starch morphology, mash viscometry and sugar yields was recorded in the presence and absence of an amylase inhibitor to differentiate between morphological and enzymatic effects. Mashing at gelatinization onset temperatures (54.5–57.1 °C) led to negligible morphological and viscometric changes, whereas mashing at pasting onset temperatures (57.5–59.8 °C) induced significant starch granule swelling and degradation resulting in increased sugar yields (61.7% of upper reference limit). Complete hydrolysis of A-type and partial hydrolysis of B-type granules was achieved within only 10 min of mashing at higher temperatures (61.4–64.5 °C), resulting in a sugar yield of 97.5% as compared to the reference laboratory method mashing procedure (65 °C for 60 min). The results indicate that the beginning of starch pasting was correctly identified and point out the potential of an adapted process temperature control.