Maximum Rate Of Hydrolysis Research Articles

Phosphomonoesterase and phosphodiesterase activities in the eastern Mediterranean in two contrasting seasonal situations

Abstract. Hydrolysis of dissolved organic phosphorus by marine planktonic microorganisms is a key process in the P cycle, particularly in P-depleted, oligotrophic environments. The present study assessed spatiotemporal variations in phosphomonoesterase (PME) and phosphodiesterase (PDE) activities using concentration kinetics in the eastern Mediterranean Sea in two contrasting situations: the end of winter (including a small bloom period) and autumn. The distribution and regulation of the maximum hydrolysis rate (Vm) and half-saturation constant (Km) of both ectoenzymes were assessed in relation to the vertical structure of the epipelagic layers. PME reached its maximum activities (Vm) after the addition of 1 µM MUF-P (4-methylumbelliferyl phosphate), whereas, for PDE, it was necessary to add up to 50 µM bis(4-methylumbelliferyl)phosphate (bis-MUF-P) to reach saturation state. On average, the Km of PDE was 33 ± 25 times higher than that of PME. The Vm of PME and Vm of PDE were linearly correlated. Conversely to the Km values, Vm values were on the same order of magnitude for both ectoenzymes, with their ratio (Vm PME : Vm PDE) ranging between 0.2 and 6.3. Dissolved organic phosphorus (DOP) and the phosphomonoesterase hydrolysable fraction of DOP explained most of the lack of variability in Vm PME and Vm PDE. On the contrary, Vm of both phosphohydrolase enzymes was inversely correlated to the concentration of dissolved inorganic phosphorus. The particular characteristics of concentration kinetics obtained for PDE (saturation at 50 µM, high Km, high turnover times) are discussed with respect to the possible unequal distribution of PDE and PME among the size continuum of organic material and accessibility of phosphodiesters.

A missense mutation in the Hspa8 gene encoding heat shock cognate protein 70 causes neuroaxonal dystrophy in rats.

Neuroaxonal dystrophy (NAD) is a neurodegenerative disease characterized by spheroid (swollen axon) formation in the nervous system. In the present study, we focused on a newly established autosomal recessive mutant strain of F344-kk/kk rats with hind limb gait abnormalities and ataxia from a young age. Histopathologically, a number of axonal spheroids were observed throughout the central nervous system, including the spinal cord (mainly in the dorsal cord), brain stem, and cerebellum in F344-kk/kk rats. Transmission electron microscopic observation of the spinal cord revealed accumulation of electron-dense bodies, degenerated abnormal mitochondria, as well as membranous or tubular structures in the axonal spheroids. Based on these neuropathological findings, F344-kk/kk rats were diagnosed with NAD. By a positional cloning approach, we identified a missense mutation (V95E) in the Hspa8 (heat shock protein family A (Hsp70) member 8) gene located on chromosome 8 of the F344-kk/kk rat genome. Furthermore, we developed the Hspa8 knock-in (KI) rats with the V95E mutation using the CRISPR-Cas system. Homozygous Hspa8-KI rats exhibited ataxia and axonal spheroids similar to those of F344-kk/kk rats. The V95E mutant HSC70 protein exhibited the significant but modest decrease in the maximum hydrolysis rate of ATPase when stimulated by co-chaperons DnaJB4 and BAG1 in vitro, which suggests the functional deficit in the V95E HSC70. Together, our findings provide the first evidence that the genetic alteration of the Hspa8 gene caused NAD in mammals.

Kinetics of Egg-Yolk Protein Hydrolysis and Properties of Hydrolysates.

Lecithin-free egg yolk (LFEY) is a byproduct of the extraction of egg-yolk phospholipids, which contain approximately 46% egg yolk proteins (EYPs) and 48% lipids. The enzymatic proteolysis is the alternative to increase the commercial value of LFEY. The kinetics of proteolysis in full-fat and defatted LFEY with Alcalase 2.4 L was analyzed in terms of the Weibull and Michaelis-Menten models. A product inhibition effect was also studied in the full-fat and defatted substrate hydrolysis. The molecular weight profile of hydrolysates was analyzed by gel filtration chromatography. Results pointed out that the defatting process did not importantly affect the maximum degree of hydrolysis (DHmax) in the reaction but rather the time at which DHmax is attained. The maximum rate of hydrolysis (Vmax) and the Michaelis-Menten constant KM were higher in the hydrolysis of the defatted LFEY. The defatting process might have induced conformational changes in the EYP molecules, and this affected their interaction with the enzyme. Consequently, the enzymatic reaction mechanism of hydrolysis and the molecular weight profile of peptides were influenced by defatting. A product inhibition effect was observed when adding 1% hydrolysates containing peptides lower than 3 kDa at the beginning of the reaction with both substrates.

Evaluation of Cotton Seeds as Environmentally Liable Source for Neutral Protease

Proteases are considered one of the most imperative groups of enzymes and are used in bioremediation processes, leather, detergents, pharmaceutical and the food industry. The foremost aim of this study was to extract, purify, and characterize the protease enzyme from cotton seeds. Purification of the neutral protease was achieved with ammonium sulphate, which gave the best results at 60% concentration with a specific activity of 51 units/mg protein and 1.52 purification fold with a percentage yield of 10.5%. The protease was active and stable at a wide range of pH from 4.0–10.0 with an optimum pH of 7.0. The highest activity of the purified enzyme was found at 20 °C. The enzyme was thermally stable and retained 25% of its activity at 50o C. The activity of cottonseeds protease Fraction-IV was enhanced by 20% with ZnCl2 and 15% with CoCl2 as enzyme samples were heated for 10 minutes. The Casein and peptone assays were also performed to check its catalytic activity. Furthermore, the maximum hydrolysis rate (Vmax) and apparent Michaelis–Menten constant (Km) values of the purified protease were 19 μmol/min and 0.08 mol/L, respectively, while activation energy was found to be 12.47 KJ/mol.

Accelerating urea hydrolysis in fresh urine by modifying operating conditions of a sequencing batch reactor

ABSTRACT A number of existing and emerging technologies can recover nitrogen from urine. A preliminary step in many nitrogen recovery processes is hydrolyzing urea to ammonium, a biologically-mediated process that can take days to weeks without intervention. The ability to achieve urea hydrolysis quickly and reliably would increase the feasibility of decentralized nitrogen recovery, especially where space and treatment time are constrained. The goal of this research was to determine whether urea hydrolysis could be accelerated by providing an inoculum containing microorganisms likely to have urease activity (feces or soil), providing a carrier to support attached growth (plastic carriers, granular activated carbon, or no carrier), and modifying the hydraulic retention time (HRT; 1.3, 2, and 4 days) and feeding frequency (Δt = 4, 24 h). Inoculated reactors achieved significantly more urea hydrolysis, and reactors inoculated with soil were able to sustain higher urea hydrolysis rates over time than those inoculated with feces. The mean zero-order rate constants (mM/hr) for reactors with a soil inoculum (15.1) were about three times higher than that of reactors with an inoculum of feces (4.9). A reactor with GAC and an inoculum of soil fed daily with fresh urine achieved greater than 90% hydrolysis with an HRT of 2 days; results suggest the HRT could be reduced to 16 h without reducing performance. No significant benefit was provided by increasing the frequency of feedings for the same HRT, likely because urease enzymes were saturated and operating at maximum hydrolysis rates during most of the reaction period.

High photocatalytic capacity of porous ceramic-based powder doped with MgO

To purify water at low cost for our daily life, the effect of ceramic-based (mullite–cristobalite) and (mullite–zircon) powders doped with different amounts of magnesium oxide (MgO) (10 and 20 wt%) was studied. These compounds are made of a local raw material DD3 with addition of zirconia (ZrO2) to create an open porosity. The powders were prepared by the traditional mixing method with the help of an automated crushing. The effect of MgO doping on structural, morphological and photocatalytic properties of the material was studied by various analytical techniques such as X-ray diffraction, scanning electron microscopy, energy dispersive X-ray spectroscopy, infrared, and UV–visible spectrometry. The results of XRD proved that there was a deformation in the crystal structure of the two types of ceramics after addition, which resulted in a shift of the spectra to the right, while SEM proved the presence of pores with a larger size as the proportion of MgO increases. The chemical composition of the basic components of the ceramic compounds as well as the additive was confirmed with EDS and IR spectra. The final results show that ceramics with added zirconia (DD3Z) and doped with 10% of MgO have a better photocatalytic efficiency than ceramics without zirconia. This important effect could be related to the higher rate of porosity, which provides a more active surface. The 10% MgO content showed a high photoactivity of 77.33% in only 15 min. The maximum hydrolysis rate obtained with Orange II was 92.95% after a period of 45 min with DD3Z/MgO powders.

Isolation and Purification of Bacillus amyloliquefaciens D1 Protease and Its Application in the Fermentation of Soybean Milk to Produce Large Amounts of Free Amino Acids.

In this study, a strain of Bacillus amyloliquefaciens D1, with a notably high production of neutral protease, was isolated from Morchella crassipes. The protease was purified to 10.4-fold with a specific activity of 4542.9 U/mg and 2.7% recovery. The enzyme was purified by 70% (NH4)2SO4 and DEAE-Cellulose-52 column. The estimated molecular mass of the purified protease obtained by SDS-PAGE was approximately 40kDa. The enzyme was optimally active at pH 6.0 and 50°C. Furthermore, the maximum hydrolysis rate (Vmax) and apparent Michaelis-Menten constant (Km) values of the purified protease were 8.2mg/mL and 65.7µg/(min mL). The enzymatic properties and rapid and efficient purification of Bacillus amyloliquefaciens D1 provide the basis for its potential commercialization and industrial development. Moreover, more essential amino acids, such as isoleucine, leucine, and phenylalanine, would be released when the strain fermented soybean milk, and then a better amino acid profile would be formed in soybean milk. Results suggest that this strain exhibits great potential in fermented soybean milk, and the enzyme could lay a foundation for its industrial application and further research.

Particle Size Reduction of Poly(ethylene terephthalate) Increases the Rate of Enzymatic Depolymerization But Does Not Increase the Overall Conversion Extent

Enzymatic depolymerization of poly(ethylene terephthalate) (PET) has emerged as a potential method for PET recycling, but extensive thermomechanical preprocessing to reduce both the crystallinity and particle size of PET is often conducted, which is costly and energy-intensive. In the current work, we use high-crystallinity PET (HC-PET) and low-crystallinity cryomilled PET (CM-PET) with three distinct particle size distributions to investigate the effect of PET particle size and crystallinity on the performance of a variant of the leaf compost-cutinase enzyme (LCC-ICCG). We show that LCC-ICCG hydrolyzes PET, resulting in the accumulation of terephthalic acid and, interestingly, also releases significant amount of mono(2-hydroxyethyl)terephthalate. Particle size reduction of PET increased the maximum rate of reaction for HC-PET, while the maximum hydrolysis rate for CM-PET was not significantly different across particle sizes. For both substrates, however, we show that particle size reduction has little effect on the overall conversion extent. Specifically, the CM-PET film was converted to 99 ± 0.2% mass loss within 48 h, while the HC-PET powder reached only 23.5 ± 0.0% conversion in 144 h. Overall, these results suggest that amorphization of PET is a necessary pretreatment step for enzymatic PET recycling using the LCC-ICCG enzyme but that particle size reduction may not be required.

Potential Activities and Long Lifetimes of Organic Carbon-Degrading Extracellular Enzymes in Deep Subsurface Sediments of the Baltic Sea.

Heterotrophic microorganisms in marine sediments produce extracellular enzymes to hydrolyze organic macromolecules, so their products can be transported inside the cell and used for energy and growth. Therefore, extracellular enzymes may mediate the fate of organic carbon in sediments. The Baltic Sea Basin is a primarily depositional environment with high potential for organic matter preservation. The potential activities of multiple organic carbon-degrading enzymes were measured in samples obtained by the International Ocean Discovery Program Expedition 347 from the Little Belt Strait, Denmark, core M0059C. Potential maximum hydrolysis rates (Vmax) were measured at depths down to 77.9mbsf for the following enzymes: alkaline phosphatase, β-d-xylosidase, β-d-cellobiohydrolase, N-acetyl-β-d-glucosaminidase, β-glucosidase, α-glucosidase, leucyl aminopeptidase, arginyl aminopeptidase, prolyl aminopeptidase, gingipain, and clostripain. Extracellular peptidase activities were detectable at depths shallower than 54.95mbsf, and alkaline phosphatase activity was detectable throughout the core, albeit against a relatively high activity in autoclaved sediments. β-glucosidase activities were detected above 30mbsf; however, activities of other glycosyl hydrolases (β-xylosidase, β-cellobiohydrolase, N-acetyl-β-glucosaminidase, and α-glucosidase) were generally indistinguishable from zero at all depths. These extracellular enzymes appear to be extremely stable: Among all enzymes, a median of 51.3% of enzyme activity was retained after autoclaving for an hour. We show that enzyme turnover times scale with the inverse of community metabolic rates, such that enzyme lifetimes in subsurface sediments, in which metabolic rates are very slow, are likely to be extraordinarily long. A back-of-the-envelope calculation suggests enzyme lifetimes are, at minimum, on the order of 230days, and may be substantially longer. These results lend empirical support to the hypothesis that a population of subsurface microbes persist by using extracellular enzymes to slowly metabolize old, highly degraded organic carbon.

Formaldehyde preservation for deferred measurements of alkaline phosphatase activities in marine samples

Alkaline phosphatases are the main enzymes required by microorganisms to hydrolyse organic phosphorus into available phosphate in aquatic environments. The investigations of alkaline phosphatase activity (APA) usually generate numerous samples (size fractionation, Michaelis-Menten kinetics). Therefore, convenient and reliable preservation of incubated samples for a deferred analysis would be very useful when measurements cannot be performed right away. The APA of marine pond waters was measured using 4-Methylumbelliferyl phosphate (MUF-P) as the fluorogenic substrate modelling natural organic phosphorus compounds. Where typical inhibitors of other enzymatic activities, such as 1% sodium dodecyl sulfate, mercuric chloride, or buffered solutions of ammonium and glycine, failed to stop APA, the addition of formaldehyde efficiently inhibited APA. The effect of formaldehyde was the strongest with the highest concentration tested (4% final concentration) and in buffered (pH 8) solutions. Since a slow and gradual increase in APA may persist with time, the combination of the addition of 4% buffered formaldehyde with immediate freezing is the best method to entirely inhibit APA. The maximal rate of hydrolysis (Vmax) and the Michaelis constant (Km) of formaldehyde (4%)-inhibited samples did not significantly change during storage at -20 °C for 11 days. The method was successfully tested on samples with extremely high values of APA (15000–40000 nM h−1) that were preserved for 1 month at -20 °C (98% inhibition). This method is a reliable and useful means of preserving incubated samples, and it provides convenient controls for background fluorescence of water and substrate, without provoking abiotic hydrolysis of the substrate.

Environmentally Friendly Preparation of Magnetic Composites Featuring Proteolytic Properties

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.

Xylanase inhibition by the derivatives of lignocellulosic material

Hydrolysis of lignocellulosic materials into simple sugar plays an important role in biorefinery. Hemicellulosic sugars from the hydrolysis of lignocellulosic materials could be used in xylitol production. However, xylanase activity during hydrolysis process is affected by activators and inhibitors that may present in the reaction system. The pretreatment process was reported to produce compounds that may affect the enzymatic hydrolysis process, such as furans, aliphatic acid, and aromatics. The purpose of this study was to investigate the inhibition effect of these potential inhibitors on xylanase activity. Three groups of potential inhibitors were evaluated including, furan, aliphatic acid, and hydrolysis-fermentation products. The result showed that ethanol, vanillin, and formic acid gave the highest inhibition effect from each group. Ethanol competed with xylanase competitively. Vanillin showed non-competitive inhibition. Formic acid performed mixed-inhibition by reducing maximum hydrolysis rate and giving varied Michaelis constant values at different concentrations.

Ultrasound-assisted hydrolysis of lard for free fatty acids catalyzed by combined two lipases in aqueous medium

ABSTRACT Lard is a by-product of animal processing. It is inexpensive compared with vegetable oils; however, its use is limited due to the high calorific value and high-saturated fatty acid content. While using lard as the source of free fatty acids (FFA) can significantly increase its utilization value. This study aimed to research the method on efficient hydrolysis of lard catalyzed by combi-lipases and assisted with ultrasound pretreatment. A 1,3-specific lipase from Rhizomucor miehei (termed pRML, 1540 U/mL) and a nonspecific mono- and diacylglycerol lipase from Penicillium cyclopium (termed MDL, 2000 U/mL) were used as biocatalysts. Results showed that the maximum hydrolysis rate of lard after 6 h at 45°C by using pRML and MDL alone was, respectively, 39.9% and 8.5%. When pRML combined with MDL (combi-lipases), hydrolysis rate can reach to 78.1%. While combi-lipases were assisted with 5 min ultrasound pretreatment before the reaction, the hydrolysis rate can further increase to 97%. The combi-lipases with different specificity and assisted with ultrasound pretreatment may be a useful technology for the enzyme production of FFA from complex lipid substrates, such as lard.

Pectin hydrolysis in cashew apple juice by Aspergillus aculeatus URM4953 polygalacturonase covalently-immobilized on calcium alginate beads: A kinetic and thermodynamic study

The kinetics and thermodynamics of pectin hydrolysis in cashew apple juice by polygalacturonase (PG) from Aspergillus aculeatus URM4953 covalently-immobilized on calcium alginate beads were investigated. Immobilized-PG activity in cashew apple juice was the highest at 20 °C, showing a maximum hydrolysis rate of 58.2 mg/mL·min, a catalytic constant of 166.2 s−1 and an affinity constant of 113.0 mg/mL. Since the enzyme exhibited an allosteric behavior, the hydrolysis rate was modeled, with excellent accuracy, by the Hill Equation as function of pectin concentration. The Hill coefficient increased from 3 to 5 with increasing temperature from 20 to 50 °C, evidencing a positive cooperativity mechanism. The reaction activation energy and the standard enthalpy variation of enzyme unfolding were 80.3 and 16.6 kJ/mol, respectively. Consistently with the kinetic results, PG-catalyzed pectin hydrolysis proceeded with maximum spontaneity at 20 °C, showing activation Gibbs free energy, enthalpy and entropy of 59.3 kJ/mol, 77.9 kJ/mol and 63.4 J/mol·K, respectively. Immobilized PG was successful in the hydrolysis of cashew apple juice pectin, requiring a low temperature to act optimally.

Purification and characterization of neutral protease from Aspergillus oryzae Y1 isolated from naturally fermented broad beans

The strain Y1, with a notably high production of neutral protease, was isolated from naturally fermented broad beans and subsequently identified as Aspergillus oryzae, through the analysis of its morphology characteristics and 18S rDNA sequence. Naturally fermented broad beans are the main raw material in Sichuan broad-bean sauce. The neutral protease from Aspergillus oryzae Y1 was purified using ammonium sulphate precipitation and DEAE-Sepharose Fast Flow chromatography, which resulted in a 10.0-fold increase in the specific activity (2264.3 U/mg) and a recovery rate of 21%. The estimated molecular mass of the purified protease was approximately 45 kDa. The optimal pH and temperature of the purified protease were 7.0 and 55 °C, respectively. The heat resistance of the purified protease was significantly higher than the commercial protease. The effect of metal ions on the activity of the purified protease approximated that of commercial neutral protease. Furthermore, the maximum hydrolysis rate (Vmax) and apparent Michaelis–Menten constant (Km) values of the purified protease were 256.4103 μg/mL min and 20.0769 mg/mL, respectively. The purified protease had a higher affinity for the substrate than the commercial neutral protease. All the results suggest that this neutral protease exhibits the potential for application in industry due to its good resistance to high temperatures and wide range of acids and bases.

CFD Modeling of Anaerobic–Aerobic Hybrid Bioreactor Landfills

© 2018 American Society of Civil Engineers. Anaerobic-aerobic hybrid bioreactor landfills, operated in a specific way that combines the benefits afforded by both anaerobic and aerobic processes, can significantly enhance the degradation of municipal solid waste (MSW) and the recovery of energy. The present article describes an application of computational fluid dynamics (CFD) to the numerical simulation of subsurface leachate recirculation and aeration systems in hybrid bioreactor landfills. The objective of the study was to model and investigate the hydrodynamic and biochemical behavior within a hybrid bioreactor landfill. The results indicate that the suitable transition time that ensures that the most methane potential has been exploited and that the hybrid landfill changes to aerobic conditions to shorten the stabilization process effectively is when 70-80% of methane potential has been exploited. A relatively small injection pressure is suggested in the initial stage of aeration forMSWwith small permeability, and the injection pressure can be raised after the pore pressure dissipates and leachate flows out of landfills smoothly. Results also show that a reasonable method of intermittent leachate recirculation during aeration is to start it when the water content decreases to the minimum value required for the hydrolysis reaction and stop it once the maximum hydrolysis rate is reached and that the configuration of the group-well system has an obvious effect on the leachate volume, whereas it appears to have a relatively small effect on the air volume.

Comparative enzymatic studies using ion-selective electrodes. The case of cholinesterases

The application of traditional ion-selective electrodes for comparative enzymatic analysis was demonstrated for the first time in this study. A kinetic-potentiometric method based on the monitoring of the concentration of the ionic substrate involved in the enzymatic reaction catalyzed by different cholinesterases is used for this purpose. A comparative study was performed comprising both enzymatic assays using different ionic substrates and the corresponding inhibited reactions in presence of neostigmine (a synthetic anticholinesterase). The developed approach is used to obtain valuable comparative results through calculation of kinetic parameters, such as Michaelis and inhibition constants. Interesting results were obtained for acetylcholinesterase and butyrylcholinesterase enzymes, which were selected as proof-of-concept: (i) the binding affinity that these enzymes have for their natural substrates showed to be higher (acetylcholine and butyrylcholine respectively) than for their corresponding thiol derivatives (acetylthiocholine and butyrylthiocholine), which are traditionally used in spectrophotometric enzymatic assays; (ii) as expected, the maximum hydrolysis rate found in the assays of each enzyme was independent of the substrate used; (iii) acetylcholinesterase enzyme inhibition due to neostigmine was found to be higher (higher inhibition constant). Advantageously, the use of ion-selective electrodes permits to perform cholinesterases’ enzymatic assays using their natural substrates and under physiological conditions, unlike the traditional spectrophotometric methods used in routine enzymatic assays. Importantly, while well-known enzymes are use throughout this work, this approach can be extended to other types of enzymatic assays as a tangible alternative to traditional spectrophotometric methods.

Biodiesel preparation from microalgae lipid by two-step lipase catalysis

To overcome the high energy-consuming process of microalgae drying, a two-step lipase catalysis technique for the preparation of biodiesel from microalgae lipid of Chlorella spp. was developed. In the first step, free fatty acids (FAAs) and triacylglycerols (TAGs) are released after cell disruption and extracted, while the TAGs were hydrolysed by free lipase in aqueous phase. In the second step, FAAs were esterified with ethanol in the catalysis of free suspended lipase. The maximum rate of hydrolysis and esterification was 93.6% and 91.3%, respectively. The effects of reaction parameters, such as reaction time, enzyme amount, water content and molar ratio of lipid to ethanol on hydrolysis or esterification, were investigated. The results indicated that two-step reaction process (hydrolyse esterify) for biodiesel production were feasible.

음식물류 폐기물의 성상과 가수분해특성 평가

To optimize the operation parameters of a food waste biogas plant, the physico-chemical properties of food waste, leachate, and their hydrolysis characteristics, and rate were investigated by a survey and experiments. Food waste analysis during the survey revealed a pH of 4.92, TS of 16.25%, VS of 13.9%, TCODCr of 145,100 mg/L, SCODCr of 58,600 mg/L, T-N of 4,665 mg/L, T-P of 823 mg/L on average. Leachate analysis revealed a pH of 4.40, TS of 6.83%, VS of 6.17%, TCODCr of 80.635 mg/L, SCODCr of 40,700 mg/L, T-N of 3,747 mg/L, and T-P of 389 mg/L on average. The rate constants, k1 and k2, of hydrolysis with a mixture of the above mentioned food waste and leachate were determined by hydrolysis experiments at different temperatures with different TS concentrations. As a result, the optimal reaction time was determined to be less than 2 days and the maximum hydrolysis rate was shown to be 32 to 64%. This data is very useful for improving the operation and basic design of biogas plants using food waste and leachate as feed.

Impact of paint shop decanter effluents on biological treatability of automotive industry wastewater

A lab-scale Sequencing Batch Reactor (SBR) was implemented to investigate biological treatability and kinetic characteristics of paint shop wastewater (PSW) together with main stream wastewater (MSW) of a bus production factory. Readily biodegradable and slowly biodegradable COD fractions of MWS were determined by respirometric analysis: 4.2% (SS), 10.4% (SH) and 59.3% (XS). Carbon and nitrogen removal performance of the SBR feeding with MSW alone were obtained as 89% and 58%, respectively. When PSW was introduced to MSW, both carbon and nitrogen removal were deteriorated. Model simulation indicated that maximum heterotrophic growth rate decreased from 7.2 to 5.7day−1, maximum hydrolysis rates were reduced from 6 to 4day−1 (khS) and 4 to 1day−1 (khX). Based on the dynamic model simulation for the evaluation of nitrogen removal, a maximum specific nitrifier growth rate was obtained as 0.45day−1 for MSW feeding alone. When PSW was introduced, nitrification was completely inhibited and following the termination of PSW addition, nitrogen removal performance was recovered in about 100 days, however with a much lower nitrifier growth rate (0.1day−1), possibly due to accumulation of toxic compounds in the sludge. Obviously, a longer recovery period is required to ensure an active nitrifier community.