Influence of Major Operational Parameters on Aerobic Granulation for the Treatment of Wastewater

Effective solids-liquid separation is the basic concept of any wastewater treatment system. Biological treatment methods involve microorganisms for the treatment of wastewater. Conventional activated sludge process (ASP) poses the problem of poor settleability and hence require a large footprint. Biogranulation is an effective biotechnological process which can overcome the drawbacks of conventional ASP to a great extent. Aerobic granulation represents an innovative cell immobilization strategy in biological wastewater treatment. Aerobic granules are selfimmobilized microbial aggregates that are cultivated in sequencing batch reactors (SBRs). Aerobic granules have several advantages over conventional activated sludge flocs such as a dense and compact microbial structure, good settleability and high biomass retention. For cells in a culture to aggregate, a number of conditions have to be satisfied. Hence aerobic granulation is affected by many operating parameters. The organic loading rate (OLR) helps to enrich different bacterial species and to influence the size and settling ability of granules. Hence, OLR was argued as an influencing parameter by helping to enrich different bacterial species and to influence the size and settling ability of granules. Hydrodynamic shear force, caused by aeration and measured as superficial upflow air velocity (SUAV), has a strong influence and hence it is used to control the granulation process. Settling time (ST) and volume exchange ratio (VER) are also two key influencing factors, which can be considered as selection pressures responsible for aerobic granulation based on the concept of minimal settling velocity. Hence, these four parameters - OLR, SUAV, ST and VER- were selected as major influencing parametersfor the present study. Influence of these four parameters on aerobic granulation was investigated in this work

Glucoamylase immobilized on montmorillonite: influence of nature of binding on surface properties of clay-support and activity of enzyme

Glucoamylase was immobilized on acid activated montmorillonite clay via two different procedures namely adsorption and covalent binding. The immobilized enzymes were characterized by XRD, NMR and N2 adsorption measurements and the activity of immobilized glucoamylase for starch hydrolysis was determined in a batch reactor. XRD shows intercalation of enzyme into the clay matrix during both immobilization procedures. Intercalation occurs via the side chains of the amino acid residues, the entire polypeptide backbone being situated at the periphery of the clay matrix. 27Al NMR studies revealed the different nature of interaction of enzyme with the support for both immobilization techniques. N2 adsorption measurements indicated a sharp drop in surface area and pore volume for the covalently bound glucoamylase that suggested severe pore blockage. Activity studies were performed in a batch reactor. The adsorbed and covalently bound glucoamylase retained 49% and 66% activity of the free enzyme respectively. They showed enhanced pH and thermal stabilities. The immobilized enzymes also followed Michaelis–Menten kinetics. Km was greater than the free enzyme that was attributed to an effect of immobilization. The immobilized preparations demonstrated increased reusability as well as storage stability.

Enhanced pH and thermal stabilities of invertase immobilized on montmorillonite K-10

Invertase was adsorbed onto micro-porous acid-activated montmorillonite clay (K-10) by two procedures, namely adsorption and covalent binding. The immobilized enzymes were characterized by XRD, surface area measurements and 27Al NMR. XRD measurements revealed an expansion of clay layers due to immobilization which suggests that intercalation had taken place. Surface area measurements also support this observation. 27Al NMR showed that interaction of enzyme with tetrahedral and octahedral Al changes with the immobilization procedure. Sucrose hydrolysis was performed in a batch reactor. The immobilized enzymes showed enhanced pH and thermal stabilities. Optimum pH and temperature were found to increase upon immobilization. The effectiveness factor (η) and Michaelis constant (Km) suggest that diffusional resistances play a major role in the reaction. The immobilized invertase could be stored in buffer of pH 5 and 6 at 5 °C without any significant loss in activity for 20 days.

Invertase immobilised on montmorillonite: reusability enhancement and reduction in leaching

Invertase was immobilised on microporous montmorillonite K-10 via adsorption and covalent binding. The immobilised enzymes were tested for sucrose hydrolysis activity in a batch reactor. Km for immobilised systems was greater than free enzyme. The immobilised forms could be reused for 15 continuous cycles without any loss in activity. After 25 cycles, 85% initial activity was retained. A study on leaching of enzymes showed that 100% enzyme was retained even after 15 cycles of reuse. Leaching increased with reaction temperature. Covalent binding resisted leaching even at temperatures of 70 °C.

Comparative effectiveness of solar disinfection using small-scale batch reactors with reflective, absorptive and transmissive rear surfaces

This study investigated the enhancement of solar disinfection using custom-made batch reactors with reflective (foil-backed) or absorptive (black-backed) rear surfaces, under a range of weather conditions in India. Plate counts of Escherichia coli ATCC11775 were made under aerobic conditions and under conditions where reactive oxygen species (ROS) were neutralised, i.e. in growth medium supplemented with 0.05% w/v sodium pyruvate plus incubation under anaerobic conditions. While the addition of either an absorptive or a reflective backing enhanced reactor performance under strong sunlight, the reflective reactor was the only system to show consistent enhancement under low sunlight, where the process was slowest. Counts performed under ROS-neutralised conditions were slightly higher than those in air, indicating that a fraction of the cells become sub-lethally injured during exposure to sunlight to the extent that they were unable to grow aerobically. However, the influence of this phenomenon on the dynamics of inactivation was relatively small

Continuous production of L-glutaminase by an immobilized marine Pseudomonas sp BTMS-51 in a packed bed reactor

A marine Pseudomonas sp BTMS-51, immobilized by Ca-alginate gel entrapment was used for the production of extracellular Lglutaminase under repeated batch process and continuous process employing a packed bed reactor (PBR). Immobilized cells could produce an average of 25 U/ml of enzyme over 20 cycles of repeated batch operation and did not show any decline in production upon reuse. The enzyme yield correlated well with the biomass content in the beads. Continuous production of the enzyme in PBR was studied at different substrate concentrations and dilution rates. In general, the volumetric productivity increased with increased dilution rate and substrate concentrations and the substrate conversion efficiency declined. The PBR operated under conditions giving maximal substrate conversion efficiency gave an average yield of 21.07 U/ml and an average productivity of 13.49 U/ml/h. The system could be operated for 120 h without any decline in productivity

Continuous Production of Extracellular L-Glutaminase by Ca-Alginate-Immobilized Marine Beauveria bassiana BTMF S-10 in Packed-Bed Reactor

L-Glutamine amidohydrolase (L-glutaminase, EC 3.5.1.2) is a therapeutically and industrially important enzyme. Because it is a potent antileukemic agent and a flavor-enhancing agent used in the food industry, many researchers have focused their attention on L-glutaminase. In this article, we report the continuous production of extracellular L-glutaminase by the marine fungus Beauveria bassiana BTMF S-10 in a packed-bed reactor. Parameters influencing bead production and performance under batch mode were optimized in the order-support (Na-alginate) concentration, concentration of CaCl2 for bead preparation, curing time of beads, spore inoculum concentration, activation time, initial pH of enzyme production medium, temperature of incubation, and retention time. Parameters optimized under batch mode for L-glutaminase production were incorporated into the continuous production studies. Beads with 12 × 108 spores/g of beads were activated in a solution of 1% glutamine in seawater for 15 h, and the activated beads were packed into a packed-bed reactor. Enzyme production medium (pH 9.0) was pumped through the bed, and the effluent was collected from the top of the column. The effect of flow rate of the medium, substrate concentration, aeration, and bed height on continuous production of L-glutaminase was studied. Production was monitored for 5 h in each case, and the volumetric productivity was calculated. Under the optimized conditions for continuous production, the reactor gave a volumetric productivity of 4.048 U/(mL·h), which indicates that continuous production of the enzyme by Ca-alginate-immobilizedspores is well suited for B. bassiana and results in a higher yield of enzyme within a shorter time. The results indicate the scope of utilizing immobilized B. bassiana for continuous commercial production of L-glutaminase