β-Glucosidase

The sustainable utilization of agricultural residues has garnered increasing attention in recent years, particularly in the context of functional food development. This paper explores the biotechnological transformation of lignocellulosic agricultural wastes into prebiotic oligosaccharides using engineered enzymes derived from Aspergillus species. Through genetic enhancement and enzyme immobilization, key carbohydrases such as xylanases and β-glucosidases exhibit superior activity, specificity, and thermal stability, making them ideal for oligosaccharide production. The paper outlines recent enzymatic engineering strategies, reaction optimizations, and bioconversion workflows applied to substrates like wheat straw, sugarcane bagasse, and corn husk. The potential applications in nutraceuticals and gut microbiota modulation are also highlighted.

The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes...

Background: On-site cellulase production using locally available lignocellulosic biomass (LCB) is essential for cost-effective production of 2 nd -generation biofuels. Cellulolytic enzymes (cellulases and hemicellulases) must be produced in fed-batch mode in order to obtain high productivity and yield. To date, the impact of the sugar composition of LCB hydrolysates on cellulolytic enzyme secretion has not been thoroughly investigated in industrial conditions. Results: The effect of sugar mixtures (glucose, xylose, inducer) on the secretion of cellulolytic enzymes by a glucose-derepressed and cellulase-hyperproducing mutant strain of Trichoderma reesei (strain CL847) was studied using a small-scale protocol representative of the industrial conditions. Since production of cellulolytic enzymes is inducible by either lactose or cellobiose, two parallel mixture designs were performed separately. No significant difference between inducers was observed on cellulase secretion performance, probably because a common induction mechanism occurred under carbon flux limitation. The characteristics of the enzymatic cocktails did not correlate with productivity, but instead were rather dependent on the substrate composition. Increasing xylose content in the feed had the strongest impact. It decreased by 2-fold cellulase, endoglucanase, and cellobiohydrolase activities and by 4-fold β-glucosidase activity. In contrast, xylanase activity was increased 6-fold. Accordingly, simultaneous high β-glucosidase and xylanase activities in the enzymatic cocktails seemed to be incompatible. The variations in enzymatic activity were modelled and validated with four fed-batch cultures performed in bioreactors. The overall enzyme production was maintained at its highest level when substituting up to 75% of the inducer with non-inducing sugars. The sugar substrate composition strongly influenced the composition of the cellulolytic cocktail secreted by T. reesei in fed-batch mode. Modelling can be used to predict cellulolytic activity based on the sugar composition of the culture-feeding solution, or to fine tune the substrate composition in order to produce a desired enzymatic cocktail.

In this investigation, effects of different compounds were evaluated on midgut alpha-amylase activity in male and female fifth in stars of the Mediterranean flour moth. Enzyme specific activity measured using a specific diagnostic kit for alpha-amylase. Total protein in enzyme samples was determined by Bradford's method. The effects of different degrees of ethanol (0, 25, 50, 75, 85, and 95%) and different concentrations of 0, 1, 2, 3, 4, and 5 mM of NaCl, EDTA, Tris, magnesium nitrate, and potassium phosphate were studied on larval midgut alpha-amylase. The effect of ethanol on enzyme activity was significantly different in male and female larvae and maximum enzyme inhibition occurred by 96% alcohol. Enzyme activity was significantly different in various concentrations of NaCl and it was decreased as NaCl concentration increased. Enzyme activity decreased with increasing SDS concentration and the most activity was observed in male and female larvae at the concentration of 1 mM. The concentration of 5 mM had the lowest activity levels. The effect of different concentrations of EDTA on enzyme activity in female larvae was significantly different but there was no significant difference in males. Different concentrations of Tris, showed a significant effect on enzyme activity of both sexes and enzyme activity decreased due to the increasing of Tris concentration. There was a significant difference among enzyme activities in different concentrations of magnesium nitrate, and enzyme activity decreased when the concentration increased. Enzyme activities in different concentrations of potassium phosphate showed a significant difference and increased due to the increase of concentration from 1 up to 5 mM. Having good understanding about the mode of action of different compounds on alpha-amylases can help us to identify the enzyme inhibitors and their application in pest control.

During recent decade, Lema melanopa L. has become one of the most important pests of wheat in Golstan province. Both adults and larvae of this pest feed on the leaves of most cereals and of course wheat and cause severe damage. Due to the lack of information about the physiology of this pest, in the present study, the biochemical properties of alpha amylase, glucosidase, galactosidase and gastrointestinal proteases from adult stage of this pest were investigated. The results showed that the highest level of optimal enzyme activity was observed in the range of 4 to 6 and the optimum temperature of 35 ° C. Electrophoresis showed two isoforms of alpha-amylase in the gut of the insect. The maximum activity of alpha and beta glucosidase enzymes and alpha and beta galactosidase of the gut was obtained in acidity 5 and in the temperature range of 35 to 45°C, respectively. The highest general protease activity was shown among gut proteases at pH 6 and at 45°C. Obtained results regarding the effect of enzymatic inhibitors including EDTA, TLCK, TPCK, PMSF, sodium Iodo Acetate and Iodoacetic acid protease activity showed that cysteine proteinase inhibitors had the greatest inhibitory effect on enzyme activity. Therefore, it can be concluded that this group of proteases is dominant in the gut of cereal leaf beetle. By determining the biochemical properties of important gut enzymes of pest, compounds can be synthesized that are more efficient and reduce the consumption of insecticides and reduce the amount of damage to the environment.

During recent decade, Lema melanopa L. has become one of the most important pests of wheat in Golstan province. Both adults and larvae of this pest feed on the leaves of most cereals and of course wheat and cause severe damage. Due to the lack of information about the physiology of this pest, in the present study, the biochemical properties of alpha amylase, glucosidase, galactosidase and gastrointestinal proteases from adult stage of this pest were investigated. The results showed that the highest level of optimal enzyme activity was observed in the range of 4 to 6 and the optimum temperature of 35 ° C. Electrophoresis showed two isoforms of alpha-amylase in the gut of the insect. The maximum activity of alpha and beta glucosidase enzymes and alpha and beta galactosidase of the gut was obtained in acidity 5 and in the temperature range of 35 to 45°C, respectively. The highest general protease activity was shown among gut proteases at pH 6 and at 45°C. Obtained results regarding the effect of enzymatic inhibitors including EDTA, TLCK, TPCK, PMSF, sodium Iodo Acetate and Iodoacetic acid protease activity showed that cysteine proteinase inhibitors had the greatest inhibitory effect on enzyme activity. Therefore, it can be concluded that this group of proteases is dominant in the gut of cereal leaf beetle. By determining the biochemical properties of important gut enzymes of pest, compounds can be synthesized that are more efficient and reduce the consumption of insecticides and reduce the amount of damage to the environment.

Storage roots of cassava clones arising from six crosses between cassava varieties of different cyanogen levels were analyzed for total cyanogen content and linamarase (b-glucosidase) activity. Total cyanogen content for 113 clones ranged from 120 to 1941 mg HCN equivalent/kg roots dry wt., the mean7s.d. being 6667387 mg HCN equivalent/kg roots dry wt. Among these, eight clones exhibited low cyanogen content (mean value o200 mg HCN equivalent/kg roots dry wt.) as compared to 19 clones which yielded cyanogen contents greater than 1000 mg HCN equivalent/kg root dry wt. Two clones had cyanogen levels lower than the parental variety with low cyanogen content. Depending on the cassava clones, the b-glucosidase activity of storage roots varied from 1.1 to 5.5 nkat/g root fresh weight and was not correlated with the total cyanogens of the storage roots (r=0.17). Some clones with even lower cyanogen content and higher linamarase activity than their parental variety were observed and these might contribute to safety in cassava consumption. Overall, data on total cyanogen content and linamarase activity in cassava roots have relevance to what processes should be developed for processing cassava roots for consumption.

In the recent decade, Lema melanopa L. has become one of the most important pests of wheat fields in Golstan province. Both adults and larvae of this pest feed on the leaves of most cereals and of course wheat and cause severe damage. Due to the lack of information about the physiology of this pest, in the present study, the biochemical properties of alpha amylase, glucosidase, galactosidase and gastrointestinal proteases from adult stage of this pest were investigated. The results showed that the highest level of optimal enzyme activity was observed in the range of 4 to 6 and the optimum temperature of 35 ° C. Electrophoresis showed two isoforms of alpha-amylase in the gut of the insect. The maximum activity of alpha and beta glucosidase enzymes and alpha and beta galactosidase of the gut was obtained in acidity 5 and in the temperature range of 35 to 45°C, respectively. The highest general protease activity was shown among gut proteases at pH 6 and at 45°C. Study Results of the effect of enzymatic inhibitors including EDTA, TLCK, TPCK, PMSF, sodium Iodo Acetate and Iodoacetic acid protease activity showed that cysteine proteinase inhibitors had the greatest inhibitory effect on enzyme activity. Therefore, it can be concluded that this group of proteases is dominant in the gut of cereal leaf beetle. By determining the biochemical properties of important gut enzymes of pest, compounds can be synthesized that are more efficient and reduce the consumption of insecticides and reduce the amount of damage to the environment.

Human nonlysosomal glucosylceramidase (GBA2) is one of several enzymes that controls levels of glycolipids and whose activity is linked to several human disease states. There is a major need to design or discover selective GBA2 inhibitors both as chemical tools and as potential therapeutic agents. Here, we describe the development of a fluorescence polarization activity-based protein profiling (FluoPol-ABPP) assay for the rapid identification, from a 350+ library of iminosugars, of GBA2 inhibitors. A focused library is generated based on leads from the FluoPol-ABPP screen and assessed on GBA2 selectivity offset against the other glucosylceramide metabolizing enzymes, glucosylceramide synthase (GCS), lysosomal glucosylceramidase (GBA), and the cytosolic retaining β-glucosidase, GBA3. Our work, yielding potent and selective GBA2 inhibitors, also provides a roadmap for the development of high-throughput assays for identifying retaining glycosidase inhibitors by FluoPol-ABPP on cell extracts containing recombinant, overexpressed glycosidase as the easily accessible enzyme source.

Soybean is one of the most important commodities in the world, being applied in feed crops and food, pharmaceutical industries in different ways. Soy is rich in isoflavones that in aglycone forms have exhibited significant anti-obesity and anti-lipogenic effects. Obesity is a global problem as several diseases have been related to this worldwide epidemic. The aim of this work was to verify the effect of free and immobilized β-glucosidase, testing Lentikats, and sol-gel as carriers. Moreover, we wanted to examine if the different types of hydrolysis would generate extracts with distinct biological activity concerning lipid accumulation, PPAR-α regulation, and TNF-α, IL-6, and IL-10 concentrations using in vitro assays. Our results show that all formulations of β-glucosidase could hydrolyze soy isoflavones. Thus, after 24 h of incubation, daidzein content increased 2.6-, 10.8-, and 12.2-fold; and genistein content increased 11.7, 11.4, and 11.4 times with the use of free enzyme, Lentikats®, and sol-gel immobilized enzyme, respectively. Moreover, both methodologies for enzyme immobilization led to promising forms of biocatalysts for application in the production of soy extracts rich in isoflavones aglycones, which are expected to bring about health benefits. A mild lipogenic effect was observed for some concentrations of extracts, as well as a slight inhibition in PPAR-α expression, although no significant differences were noticeable in the cytokines TNF-α, IL-10, and IL-6 as compared with the control.

Economic and sustainable production of bioethanol from biomass through enzymatic route depends on economics of cellulase availability, the key factor for the success of the technology. It has been realized that the bottleneck of the technology lies in obtaining highly efficient cellulase which could result in an economically feasible technology. In this study, we compared cellulase production by Penicillium janthinellum EMS UV-8 in shake flask in two different medium; modified Mandel and Weber (M & W) and the corn steep liquor (CSL) based medium. In CSL based medium, 3.02 FPU/mL was produced compared to 1.25 FPU/mL in modified r M & W medium. Hence, CSL based medium was employed in bioreactor for cellulase production. In cellulase production, Penicillium sp. is comparable to the widely acclaimed Trichoderma sp. Changing the production medium from modified M & W medium to CSL based medium, increased cellulase production by two fold. In the bioreactor, controlled monitoring of DO and pH resulted in increase in the cellulase activity upto 5.44±0.3 FPU/ml at 168 h.

Cellulose is the most abundant biopolymer in biosphere and the major constituent of plant biomass. Cellulose polymer is made up of β-glucose units linked by β-glucosidic bonds. Cellulase is an enzymatic system that catalyzes the hydrolysis of cellulose polymer to glucose monomers. This enzymatic system consists of three individual enzymes namely endoglucanase, exoglucanase and β-glucosidase which act synergistically to degrade cellulose molecules into glucose. Cellulases are produced by bacteria, fungi, plants, and animals and used in many industrial applications such as textile industries, laundry and detergent industries, paper and pulp industry, animal feeds, and biofuels production. β-Glucosidase is a diverse group of enzymes with wide distribution in bacteria, fungi, plants and animals and has the potential to be utilized in various biotechnological processes such as biofuel production, isoflavone hydrolysis, flavor enhancement and alkyl/aryl β-D-glucoside and oligosaccharides ...

Soybean is one of the most important commodities in the world, being applied in feed crops and food, pharmaceutical industries in different ways. Soy is rich in isoflavones that in aglycone forms have exhibited significant anti-obesity and anti-lipogenic effects. Obesity is a global problem as several diseases have been related to this worldwide epidemic. The aim of this work was to verify the effect of free and immobilized β-glucosidase, testing Lentikats, and sol-gel as carriers. Moreover, we wanted to examine if the different types of hydrolysis would generate extracts with distinct biological activity concerning lipid accumulation, PPAR-α regulation, and TNF-α, IL-6, and IL-10 concentrations using in vitro assays. Our results show that all formulations of β-glucosidase could hydrolyze soy isoflavones. Thus, after 24 h of incubation, daidzein content increased 2.6-, 10.8-, and 12.2-fold; and genistein content increased 11.7, 11.4, and 11.4 times with the use of free enzyme, Lentikats®, and sol-gel immobilized enzyme, respectively. Moreover, both methodologies for enzyme immobilization led to promising forms of biocatalysts for application in the production of soy extracts rich in isoflavones aglycones, which are expected to bring about health benefits. A mild lipogenic effect was observed for some concentrations of extracts, as well as a slight inhibition in PPAR-α expression, although no significant differences were noticeable in the cytokines TNF-α, IL-10, and IL-6 as compared with the control.

Olive oil and table olives are rich sources of biophenols, which provides a unique taste, aroma and potential health benefits. Specifically, green olive drupes are enriched with oleuropein, a bioactive biophenol secoiridoid. Olive oil contains hydrolytic derivatives such as hydroxytyrosol, oleacein and elenolate from oleuropein as well as tyrosol and oleocanthal from ligstroside. Biophenol secoiridoids are categorized by the presence of elenoic acid or its derivatives in their molecular structure. Medical studies suggest that olive biophenol secoiridoids could prevent cancer, obesity, osteoporosis, and neurodegeneration. Therefore, understanding the biomolecular dynamics of oleuropein can potentially improve olive-based functional foods and nutraceuticals. This review provides a critical assessment of oleuropein biomolecular mechanism and computational mapping that could contribute to nutrigenomics.

Olive oil and table olives are rich sources of biophenols, which provides a unique taste, aroma and potential health benefits. Specifically, green olive drupes are enriched with oleuropein, a bioactive biophenol secoiridoid. Olive oil contains hydrolytic derivatives such as hydroxytyrosol, oleacein and elenolate from oleuropein as well as tyrosol and oleocanthal from ligstroside. Biophenol secoiridoids are categorized by the presence of elenoic acid or its derivatives in their molecular structure. Medical studies suggest that olive biophenol secoiridoids could prevent cancer, obesity, osteoporosis, and neurodegeneration. Therefore, understanding the biomolecular dynamics of oleuropein can potentially improve olive-based functional foods and nutraceuticals. This review provides a critical assessment of oleuropein biomolecular mechanism and computational mapping that could contribute to nutrigenomics.

Current cellulosic biomass hydrolysis is based on the one-time use of cellulases. Cellulases immobilized on magnetic nanocarriers offer the advantages of magnetic separation and repeated use for continuous hydrolysis. Most immobilization methods focus on only one type of cellulase. Here, we report co-immobilization of two types of cellulases, β-glucosidase A (BglA) and cellobiohydrolase D (CelD), on sub-20 nm superparamagnetic nanoparticles. The nanoparticles demonstrated 100% immobilization efficiency for both BglA and CelD. The total enzyme activities of immobilized BglA and CelD were up to 67.1% and 41.5% of that of the free cellulases, respectively. The immobilized BglA and CelD each retained about 85% and 43% of the initial immobilized enzyme activities after being recycled 3 and 10 times, respectively. The effects of pH and temperature on the immobilized cellulases were also investigated. Co-immobilization of BglA and CelD on MNPs is a promising strategy to promote synergistic action of cellulases while lowering enzyme consumption.

Water quality modeling intends to represent a water body in order to assess their status and project the effects of different measures taken for their protection. This paper presents the results obtained from the Qual2kw model implementation in the first 50 kilometers of the Aburrá-Medellín River, in their most critical conditions of water quality, which correspond to low flow rates. After the model calibration, three recovery scenarios (short-term, medium-term and long-term) were evaluated. In the first scenario the sanitation only improved in some streams, in accordance with the Plan of Sanitation and Management of Discharges that was considered. Medium and long-term scenarios, with the operation of the new Water Waste Treatment Plant (WWTP) of the Bello municipality and an increase in the sewage collection, were considered. The obtained results show the positive impact of the operation of the WWTP of Bello in the balance of BOD5, dissolved oxygen and nitrogen.

Bifidobacterium pseudocatenulatum IPLA 36007 acts on isoflavone glycosides, releasing their corresponding aglycones. This strain-specific activity might be a key step in making isoflavones bioavailable and harnessing their oestrogenic activity. To investigate the molecular mechanisms involved in this activity, four glycosyl hydrolaseencoding genes in the IPLA 36007 genome (AW18_01575, AW18_09810, AW18_08145, and AW18_08090) were selected, synthesized with heterologous promoter and terminator signals (r-β-gluA, r-β-gluB, r-β-gluD and r-β-gluE, respectively), cloned into Escherichia coli, overexpressed as His-tagged proteins, and the enzymes purified and characterized. All four enzymes-GluA His , GluB His , GluD His and GluE His-proved to have β-glucosidase activity and deglycosylated (although at different rates) the isoflavone glycosides daidzin and genistin, releasing the corresponding aglycone moieties daidzein and genistein. GluD His and GluE His were also shown to hydrolyse β-glucosyl disaccharides such as cellobiose and gentiobiose, while GluA His and GluB His did not. Differences in activity were recorded for the four βglucosidases at different pHs and temperatures under otherwise similar assay conditions, suggesting they have complementary activities under different environmental conditions. Two of the recombinant genes, r-β-gluA, and r-β-gluD, were cloned and expressed in the model lactic acid bacterium Lactococcus lactis, suggesting the β-glucosidase activity could be transferred to other starter and probiotic organisms. B. pseudocatenulatum IPLA 36007 contains additional β-glucosidases to those studied in this work, indicating a high level of redundancy for this enzymatic activity. Knowledge of glycoside-degrading enzymes should facilitate the development of novel, more effective or more selective prebiotics or functional foods for the promotion of 3 bifidobacterial numbers in the human gut. It might also be of interest in the development of novel probiotics with specific health-promoting activities.

β-Glucosidases (EC 3.2.1.21) split β-glucosidic linkages at the non-reducing end of glucosides and oligosaccharides to release β-D-glucose. One of the important functions of plant β-glucosidase is deglucosylation of inactive glucosides of phytohormones to regulate levels of active hormones. Tuberonic acid is a jasmonate-related compound that shows tuber-inducing activity in the potato. We have identified two enzymes, OsTAGG1 and OsTAGG2, that have hydrolytic activity towards tuberonic acid β-D-glucoside in rice (Oryza sativa L.). The expression of OsTAGG2 is upregulated by wounding and by methyl jasmonate, suggesting that this isozyme is involved in responses to biotic stresses and wounding, but the physiological substrate of OsTAGG2 remains ambiguous. In this study, we produced recombinant OsTAGG2 in Pichia pastoris (rOsTAGG2P), and investigated its substrate specificity in detail. From 1 L of culture medium, 2.1 mg of purified recombinant enzyme was obtained by ammonium sulfate precipitation and Ni-chelating column chromatography. The specific activity of rOsTAGG2P (182 U/mg) was close to that of the native enzyme (171 U/mg), unlike recombinant OsTAGG2 produced in Escherichia coli, which had approximately 3-fold lower specific activity than the native enzyme. The optimum pH and temperature for rOsTAGG2P were pH 3.4 and 60°C. After pH and heat treatments, the enzyme retained its original activity in a pH range of 3.4-9.8 and below 55°C. Native OsTAGG2 and rOsTAGG2P showed 4.5-4.7-fold higher activities towards salicylic acid β-D-glucoside, an inactive storage-form of salicylic acid, than towards tuberonic acid β-D-glucoside (TAG), although OsTAGG2 was originally isolated from rice based on TAG-hydrolytic activity.

In the context of environmentally-friendly bleaching in paper pulp manufacturing, an enzymatic procedure was developed for the isolation of residual lignins from eucalypt pulp. The method was based on the hydrolysis and complete solubilization of pulp cellulose using a combination of Trichoderma cellulase and Aspergillus ␤-glucosidase, followed by lignin purification using Bacillus protease (for hydrolysis of contaminating cellulase) and extraction of lignin with dimethylacetamide (DMAC) and NaOH. This method was applied to both unbleached and totally chlorine free bleached eucalypt kraft pulps. The different fractions obtained were analyzed by Fourier-transform infrared spectroscopy and pyrolysis-gas chromatography/mass spectrometry to evaluate the effect of the different isolation steps, and optimize the lignin isolation procedure. Depending of the type of pulp and its delignification degree most of the lignin was recovered from the cellulase hydrolyzate or the non-hydrolyzable residue. High-purity lignins were obtained from pulps by a new isolation procedure that included double solvent purification after combining the two fractions from protease treatment. This method is being used to analyze the effect of chlorine-free reagents (including enzymes) in clean bleaching sequences.

This study determined the influence of pulp maceration and b-glucosidase on mango wine physico-chemical properties and volatile profiles. The distinction in pH, sugars and organic acids among different treatments was not statistically significant. All wine samples reached around 8% (v/v) ethanol from about 16% (w/v) of sugars. The wine with pulp contact contained about ten times higher a-terpinolene and up to three times higher acetate esters than the wine without pulp contact, but mitigated the production of medium-chain fatty acids and relative ethyl esters by up to six times. b-glucosidase enhanced terpenols by up to ten times and acetate esters by up to three times. Furthermore, enzyme treatment mitigated, by up to five times, the formation of medium-chain fatty acids and ethyl esters to moderate levels. Sensory evaluation showed pulp contact, and b-glucosidase not only improved the intensity and complexity of wine aroma but balanced odour attributes.

A cellulase producing bacterium (E3 strain) was isolated from fecal matter of elephant and identified as Bacillus sp. using 16S rDNA sequenced based molecular phylogenetic approach. While studying the effect of substrates like Carboxymethyl cellulose (CMC), avicel, starch, maltose, sucrose, glucose, fructose, galactose and lactose on cellulase production, it was found that CMC was best carbon source induced cellulase production followed by lactose in this bacterial strain. A positive synergistic effect of lactose with CMC was also observed with enhancement of 5-6 times in cellulase production. The optimum cellulase production was recorded with 1% CMC and 1% lactose when added individually in the Omeliansky's medium. The results showed that addition lactose with CMC greatly enhances the production and activity of various cellulase enzymes. The optimal fermentation conditions for the biosynthesis of cellulase by this strain were found to be temperature: 37˚C, pH 7.0. The nitrogen source NH 4 Cl at 0.15% was optimum for cellulase production by this bacterium.

The term regulon has been coined in the genetic model plant Arabidopsis thaliana, denoting a structural and physiological defense apparatus defined genetically through the identification of the penetration (pen) mutants. The regulon is composed partially by the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) syntaxin PEN1. PEN1 has homology to a Saccharomyces cerevisae gene that regulates a Secretion (Sec) protein, Suppressor of Sec 1 (Sso1p). The regulon is also composed of the b-glucosidase (PEN2) and an ATP binding cassette (ABC) transporter (PEN3). While important in inhibiting pathogen infection, limited observations have been made regarding the transcriptional regulation of regulon genes until now. Experiments made using the model agricultural Glycine max (soybean) have identified co-regulated gene expression of regulon components. The results explain the observation of hundreds of genes expressed specifically in the root cells undergoing the natural process of defense. Data regarding additional G. max genes functioning within the context of the regulon are presented here, including Sec 14, Sec 4 and Sec 23. Other examined G. max homologs of membrane fusion genes include an endosomal bromo domain-containing protein1 (Bro1), syntaxin6 (SYP6), SYP131, SYP71, SYP8, Bet1, coatomer epsilon (e-COP), a coatomer zeta (z-COP) paralog and an ER to Golgi component (ERGIC) protein. Furthermore, the effectiveness of biochemical pathways that would function within the context of the regulon ave been examined, including xyloglucan xylosyltransferase (XXT), reticuline oxidase (RO) and galactinol synthase (GS). The experiments have unveiled the importance of the regulon during defense in the root and show how the deposition of callose relates to the process.

The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes...

A gene (<i>PSTG2</i>) coding for a novel β-glucosidase belonging to glycoside hydrolase family 3 was identified in the vicinity of the previously identified β-glucosidase gene [sesaminol triglucoside (STG)-hydrolyzing β-glucosidase, PSTG1] in the genome of <i>Paenibacillus</i> sp. strain KB0549. Compared with PSTG1, recombinant PSTG2 more specifically acted on the β-1,2-glucosidic linkage of the STG molecule to transiently accumulate a larger amount of 6-<i>O</i>-(β-D-glucopyranosyl)-β-D-glucopyranosylsesaminol.

A cellulase producing bacterium (E3 strain) was isolated from fecal matter of elephant and identified as Bacillus sp. using 16S rDNA sequenced based molecular phylogenetic approach. While studying the effect of substrates like Carboxymethyl cellulose (CMC), avicel, starch, maltose, sucrose, glucose, fructose, galactose and lactose on cellulase production, it was found that CMC was best carbon source induced cellulase production followed by lactose in this bacterial strain. A positive synergistic effect of lactose with CMC was also observed with enhancement of 5-6 times in cellulase production. The optimum cellulase production was recorded with 1% CMC and 1% lactose when added individually in the Omeliansky's medium. The results showed that addition lactose with CMC greatly enhances the production and activity of various cellulase enzymes. The optimal fermentation conditions for the biosynthesis of cellulase by this strain were found to be temperature: 37˚C, pH 7.0. The nitrogen source NH 4 Cl at 0.15% was optimum for cellulase production by this bacterium.

Immobilization is an exciting alternative to improve the stability of enzymatic processes. However, part of the applied covalent strategies for immobilization uses specific conditions, generally alkaline pH, where some enzymes are not stable. Here, a new generation of heterofunctional supports with application at neutral pH conditions was proposed. New supports were developed with different bifunctional groups (i.e., hydrophobic or carboxylic/metal) capable of adsorbing biocatalysts at different regions (hydrophobic or histidine richest place), together with a glutaraldehyde group that promotes an irreversible immobilization at neutral conditions. To verify these supports, a multi-protein model system (E. coli extract) and four enzymes (Candida rugosa lipase, metagenomic lipase, β-galactosidase and β-glucosidase) were used. The immobilization mechanism was tested and indicated that moderate ionic strength should be applied to avoid possible unspecific adsorption. The use of different supports allowed the immobilization of most of the proteins contained in a crude protein extract. In addition, different supports yielded catalysts of the tested enzymes with different catalytic properties. At neutral pH, the new supports were able to adsorb and covalently immobilize the four enzymes tested with different recovered activity values. Notably, the use of these supports proved to be an efficient alternative tool for enzyme immobilization at neutral pH.

Background: On-site cellulase production using locally available lignocellulosic biomass (LCB) is essential for cost-effective production of 2 nd-generation biofuels. Cellulolytic enzymes (cellulases and hemicellulases) must be produced in fed-batch mode in order to obtain high productivity and yield. To date, the impact of the sugar composition of LCB hydrolysates on cellulolytic enzyme secretion has not been thoroughly investigated in industrial conditions. Results: The effect of sugar mixtures (glucose, xylose, inducer) on the secretion of cellulolytic enzymes by a glucose-derepressed and cellulase-hyperproducing mutant strain of Trichoderma reesei (strain CL847) was studied using a small-scale protocol representative of the industrial conditions. Since production of cellulolytic enzymes is inducible by either lactose or cellobiose, two parallel mixture designs were performed separately. No significant difference between inducers was observed on cellulase secretion performance, probably because a common induction mechanism occurred under carbon flux limitation. The characteristics of the enzymatic cocktails did not correlate with productivity, but instead were rather dependent on the substrate composition. Increasing xylose content in the feed had the strongest impact. It decreased by 2-fold cellulase, endoglucanase, and cellobiohydrolase activities and by 4-fold β-glucosidase activity. In contrast, xylanase activity was increased 6-fold. Accordingly, simultaneous high β-glucosidase and xylanase activities in the enzymatic cocktails seemed to be incompatible. The variations in enzymatic activity were modelled and validated with four fed-batch cultures performed in bioreactors. The overall enzyme production was maintained at its highest level when substituting up to 75% of the inducer with non-inducing sugars. Conclusions: The sugar substrate composition strongly influenced the composition of the cellulolytic cocktail secreted by T. reesei in fed-batch mode. Modelling can be used to predict cellulolytic activity based on the sugar composition of the culture-feeding solution, or to fine tune the substrate composition in order to produce a desired enzymatic cocktail.

Soybeans and soy-based products contain isoflavones which can be used for nutraceutical and medical applications. In soybeans and in unfermented soy foods, isoflavones are normally present as glycosides. Isoflavone glycosides can be enzymatically converted to isoflavone aglycones, thus releasing the sugar molecule. The effective absorption of isoflavones in humans requires the bioconversion of isoflavone glycosides to isoflavone aglycones through the activity of the enzyme β-glucosidase. The objective was to assess the capacity of 42 bacterial strains (belonging to Lactobacillus, Streptococcus and Enterococcus) to produce β-glucosidase activity. The strain that showed the highest β-glucosidase activity (Lactobacillus plantarum 128/2) was then used for the optimization of the bioconversion of genistin and daidzin present in commercial soymilk to their aglycone forms genistein and daidzein. The contribution of process parameters (temperature, inoculum size, time) to the efficiency of ...

Three strains of Aspergillus niger were retrieved from culture collection of the Department of Microbiology, University of Karachi, Karachi, Pakistan and were studied for their ability to produce cellulases. Cultivation at different temperatures and in presence of various carbon sources revealed that all the three strains produced more amounts of endoglucanase, β- glucosidase and filter-paperase activities at 35o C; carboxymethyl cellulose promotes the production of filter paperase and endoglucanase activities whereas salicin induced β-glucosidase activity. Experiments on growth and enzyme production kinetics showed that generation time and hence volumetric rate of biomass production is influenced by the carbon source used in the medium; simple carbon source, such as glucose favored the growth of all the strains. Cellulases from all the strains showed optimum activity at temperature >50o C and under acidic range of pH, while melting temperature was 64- 65o C. These findings affir...

The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes...

The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes...

Glucose isomerase was immobilized by itself and coimmobilized with cellulase and fl-glucosidase using a polyurethane foam (Hypol | FHP 2002). Approximately 50% of the enzyme added was immobilized. The immobilized enzyme was active at pH values as low as 6.8. When immobilized alone, the Km for Mg 2 § increased by 5.5fold and the Km for fructose increased 62%. The half-life of the immobilized glucose isomerase was approximately 160 h of continuous hydrolysis, with a substantial (about 35-40%) amount of activity remaining even after 1000 h. When all three enzymes were immobilized together, the system was found capable of functioning at pH 7.0 to produce fructose from both soluble and insoluble cellulose substrates. At this pH, the glucose:fructose ratio was 70:30. The advantageous properties of the foam as a support for enzyme immobilization and the efficiency of the one-step conversion process outlined combine to make this system appear valuable for use in high fructose syrup production.

Water quality modeling intends to represent a water body in order to assess their status and project the effects of different measures taken for their protection. This paper presents the results obtained from the Qual2kw model implementation in the first 50 kilometers of the Aburrá-Medellín River, in their most critical conditions of water quality, which correspond to low flow rates. After the model calibration, three recovery scenarios (short-term, medium-term and long-term) were evaluated. In the first scenario the sanitation only improved in some streams, in accordance with the Plan of Sanitation and Management of Discharges that was considered. Medium and long-term scenarios, with the operation of the new Water Waste Treatment Plant (WWTP) of the Bello municipality and an increase in the sewage collection, were considered. The obtained results show the positive impact of the operation of the WWTP of Bello in the balance of BOD5, dissolved oxygen and nitrogen.

Water quality modeling intends to represent a water body in order to assess their status and project the effects of different measures taken for their protection. This paper presents the results obtained from the Qual2kw model implementation in the first 50 kilometers of the Aburrá-Medellín River, in their most critical conditions of water quality, which correspond to low flow rates. After the model calibration, three recovery scenarios (short-term, medium-term and long-term) were evaluated. In the first scenario the sanitation only improved in some streams, in accordance with the Plan of Sanitation and Management of Discharges that was considered. Medium and long-term scenarios, with the operation of the new Water Waste Treatment Plant (WWTP) of the Bello municipality and an increase in the sewage collection, were considered. The obtained results show the positive impact of the operation of the WWTP of Bello in the balance of BOD5, dissolved oxygen and nitrogen.

El nitrógeno es un elemento biogénico constituyente de moléculas orgánicas que desempeñan funciones vitales para toda célula [1]. Su origen proviene de la mineralización de la materia orgánica, de la disolución de rocas sedimentarias y del intercambio con el nitrógeno ...

The term regulon has been coined in the genetic model plant Arabidopsis thaliana, denoting a structural and physiological defense apparatus defined genetically through the identification of the penetration (pen) mutants. The regulon is composed partially by the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) syntaxin PEN1. PEN1 has homology to a Saccharomyces cerevisae gene that regulates a Secretion (Sec) protein, Suppressor of Sec 1 (Sso1p). The regulon is also composed of the b-glucosidase (PEN2) and an ATP binding cassette (ABC) transporter (PEN3). While important in inhibiting pathogen infection, limited observations have been made regarding the transcriptional regulation of regulon genes until now. Experiments made using the model agricultural Glycine max (soybean) have identified co-regulated gene expression of regulon components. The results explain the observation of hundreds of genes expressed specifically in the root cells undergoing the natural process of defense. Data regarding additional G. max genes functioning within the context of the regulon are presented here, including Sec 14, Sec 4 and Sec 23. Other examined G. max homologs of membrane fusion genes include an endosomal bromo domain-containing protein1 (Bro1), syntaxin6 (SYP6), SYP131, SYP71, SYP8, Bet1, coatomer epsilon (e-COP), a coatomer zeta (z-COP) paralog and an ER to Golgi component (ERGIC) protein. Furthermore, the effectiveness of biochemical pathways that would function within the context of the regulon ave been examined, including xyloglucan xylosyltransferase (XXT), reticuline oxidase (RO) and galactinol synthase (GS). The experiments have unveiled the importance of the regulon during defense in the root and show how the deposition of callose relates to the process.

In streams and rivers, the first organisms which directly receive and respond to nutrients are primary producers (algae, macrophytes) and microbial heterotrophs (bacteria, fungi) since they rely on available inorganic nutrients from the water column. The aim of the present study was to analyze the response of the epipelic microbial biofilm in a Pampean stream submitted to a continuous input of inorganic nutrients (nitrogen and phosphorus). For this purpose, we measured the effects of moderate nutrient addition during 14 mo on the epipelic biofilm community of a meso-eutrophic stream that runs through the Pampean plain. The effects of nutrient enrichment were tested by analyzing the difference in algal and bacterial biomass and 2 extracellular enzymatic activities (β-glucosidase, phosphatase) at an enriched reach compared with those measured at an unmodified upstream reach. Overall, the response of the epipelon of this Pampean stream produced a slow and delayed effect on algal biomass increases, which might result in a delayed effect on the increase of bacterial densities. Neither phosphatase activity nor β-glucosidase activity exhibited significant changes due to nutrient addition. This may be due to the fact that the phosphatase activities measured were basal activities, uninhibited by enrichment, and that the epipelic β-glucosidase activity was regulated more by substrate availability than by any nutrient imbalance. Although changes are slow, if some of these changes were to become chronic, they would affect the functioning and services of the whole stream ecosystem.

Current lye processing for debittering California black table olives produces large amounts of caustic wastewater and destroys many of the beneficial phenolic compounds in the fruit. Herein, we propose using enzyme treatment in place of lye, potentially reducing the amount and causticity of wastewater produced. By specifically targeting the bitterness-causing compound, oleuropein, retention of other beneficial phenolics may be possible. A β-glucosidase from Streptomyces sp. was identified from a screen of 22 glycosyl hydrolases to completely degrade oleuropein in 24 h. Computational modeling was performed on this enzyme, and mutation C181A was found to improve the rate of catalysis by 3.2-fold. This mutant was tested in the context of the olive fruit and leaf extract. Degradation was observed in the olive leaf extract but not in the fruit matrix, suggesting that enzyme fruit penetration is a limiting factor. This work discovers and begins the refinement process for an enzyme that has the catalytic properties for debittering olives and provides direction for future engineering efforts required to make a product with commercial value.

A gene (<i>PSTG2</i>) coding for a novel β-glucosidase belonging to glycoside hydrolase family 3 was identified in the vicinity of the previously identified β-glucosidase gene [sesaminol triglucoside (STG)-hydrolyzing β-glucosidase, PSTG1] in the genome of <i>Paenibacillus</i> sp. strain KB0549. Compared with PSTG1, recombinant PSTG2 more specifically acted on the β-1,2-glucosidic linkage of the STG molecule to transiently accumulate a larger amount of 6-<i>O</i>-(β-D-glucopyranosyl)-β-D-glucopyranosylsesaminol.

In recent years, the interest to find alternative extraction methods has increased. Extraction of natural phenolics by enzymes produced during solid-state fermentation (SSF) is a useful and novel technique environmentally friendly. On the other hand, agro-industrial wastes are an excellent source of natural antioxidants as phenolics. The aim of the work was to evaluate the increase of antioxidant compounds extraction from agro-industrial wastes after SSF and to relate it to the production of lignocellulolytic enzymes. Several filamentous fungi were evaluated as candidates to increase the extraction of antioxidant compounds by solid-state fermentation of wineries, olive mill and brewery wastes. Fermented and unfermented agro-industrial wastes were extracted with water and lignocellulolytic enzymes, total phenolic compounds and antioxidant activity were determined in the extract. The maximum xylanase and cellulase activities were achieved by A. ibericus strains using brewer´s spent grain (BSG) as substrate and ranged from 300 to 313 U xylanase/g and 51-62 U cellulase/g. The best producer of β-glucosidase was A. niger CECT2088 using BSG as substrate (94 ± 4 U/g). The results of extraction of phenolic compounds revealed a higher extraction by SSF in olive mill wastes followed by winery wastes. In the same form, the maximum increase of antioxidant activity was achieved by SSF of exhausted olive pomace by Rhizopus oryzae MUM 10.260, increasing 12.9-fold in relation to unfermented waste. In addition, the production of enzymes, the extraction of phenolic compounds and the increase of antioxidant activity were related by principal component analysis. The first component grouped the BSG along with maximum enzymes production, the second component related positively the production of enzymes and the extraction of phenolic compounds and the increase of antioxidant activity. SSF proved to be an innovative environmentally friendly process that can improve the extraction of antioxidant compounds and simultaneously to produce lignocellulolytic enzymes from different agro-industrial wastes.

Cellulose is the most abundant biopolymer in biosphere and the major constituent of plant biomass. Cellulose polymer is made up of β-glucose units linked by β-glucosidic bonds. Cellulase is an enzymatic system that catalyzes the hydrolysis of cellulose polymer to glucose monomers. This enzymatic system consists of three individual enzymes namely endoglucanase, exoglucanase and β-glucosidase which act synergistically to degrade cellulose molecules into glucose. Cellulases are produced by bacteria, fungi, plants, and animals and used in many industrial applications such as textile industries, laundry and detergent industries, paper and pulp industry, animal feeds, and biofuels production. β-Glucosidase is a diverse group of enzymes with wide distribution in bacteria, fungi, plants and animals and has the potential to be utilized in various biotechnological processes such as biofuel production, isoflavone hydrolysis, flavor enhancement and alkyl/aryl β-D-glucoside and oligosaccharides ...

Cellulose is the most abundant biopolymer in biosphere and the major constituent of plant biomass. Cellulose polymer is made up of β-glucose units linked by β-glucosidic bonds. Cellulase is an enzymatic system that catalyzes the hydrolysis of cellulose polymer to glucose monomers. This enzymatic system consists of three individual enzymes namely endoglucanase, exoglucanase and β-glucosidase which act synergistically to degrade cellulose molecules into glucose. Cellulases are produced by bacteria, fungi, plants, and animals and used in many industrial applications such as textile industries, laundry and detergent industries, paper and pulp industry, animal feeds, and biofuels production. β-Glucosidase is a diverse group of enzymes with wide distribution in bacteria, fungi, plants and animals and has the potential to be utilized in various biotechnological processes such as biofuel production, isoflavone hydrolysis, flavor enhancement and alkyl/aryl β-D-glucoside and oligosaccharides ...

Olive oil and table olives are rich sources of biophenols, which provides a unique taste, aroma and potential health benefits. Specifically, green olive drupes are enriched with oleuropein, a bioactive biophenol secoiridoid. Olive oil contains hydrolytic derivatives such as hydroxytyrosol, oleacein and elenolate from oleuropein as well as tyrosol and oleocanthal from ligstroside. Biophenol secoiridoids are categorized by the presence of elenoic acid or its derivatives in their molecular structure. Medical studies suggest that olive biophenol secoiridoids could prevent cancer, obesity, osteoporosis, and neurodegeneration. Therefore, understanding the biomolecular dynamics of oleuropein can potentially improve olive-based functional foods and nutraceuticals. This review provides a critical assessment of oleuropein biomolecular mechanism and computational mapping that could contribute to nutrigenomics.

A cellulase producing bacterium (E3 strain) was isolated from fecal matter of elephant and identified as Bacillus sp. using 16S rDNA sequenced based molecular phylogenetic approach. While studying the effect of substrates like Carboxymethyl cellulose (CMC), avicel, starch, maltose, sucrose, glucose, fructose, galactose and lactose on cellulase production, it was found that CMC was best carbon source induced cellulase production followed by lactose in this bacterial strain. A positive synergistic effect of lactose with CMC was also observed with enhancement of 5-6 times in cellulase production. The optimum cellulase production was recorded with 1% CMC and 1% lactose when added individually in the Omeliansky's medium. The results showed that addition lactose with CMC greatly enhances the production and activity of various cellulase enzymes. The optimal fermentation conditions for the biosynthesis of cellulase by this strain were found to be temperature: 37˚C, pH 7.0. The nitrogen source NH 4 Cl at 0.15% was optimum for cellulase production by this bacterium.

RESUMEN Selección de cepas de bacterias ácido lácticas que degradan oleuropeína aisladas en la fermentación de aceitunas verdes marroquíes. Un total de 177 cepas de bacterias ácido lácticas (LAB) fueron aisladas en las primeras etapas de la fermentación de aceitunas verdes marroquíes Picholine, incluyendo Lactobacillus plantarum (44.63%), Lactobacillus pentosus (25.99%), Lactobacillus brevis (9.61%) y Pediococcus pentosaceus (19.77%). Todos los aislados fueron evaluados mediante su tolerancia a extractos de hojas de olivo y oleuropeína. La mayoría de los aislados (85,3%) degradaron oleuropeína, cuando fueron evaluados usando oleuropeína o 5-Bromo-4-cloro-3-indolil β-D-glucuronido (X-Gluc) como sustrato. La capacidad de biodegradación de las cepas seleccionadas para cada especie fue confirmada mediante análisis por HPLC.

A successful lignocellulosic ethanol production process needs to address the technological impediments such as cost-competitiveness and sustainability of the process. Effective biomass utilization requires a repertoire of enzymes including various accessory enzymes. Developing an enzyme preparation with defined hydrolytic activities can circumvent the need for supplementing cellulases with accessory enzymes for enhanced hydrolysis. With this objective, mixture design approach was used in the present study to enhance glycoside hydrolase production of a fungal isolate, Aspergillus terreus CM20, by determining the proportion of different lignocellulosic components as enzyme inducers in the culture medium. A mixture of paddy straw and wheat straw (1.42:1.58) resulted in improved cellulolytic activities. The precipitated crude enzyme showed higher CMCase (365.03 18 IU g-1), FPase (161.48 IU g-1), avicelase (15.46 IU g-1), β-glucosidase (920.92 IU g-1) and xylanase (9627.79 IU g-1) activi...

The control and infected leaf samples of blast resistant and susceptible rice genotypes were evaluated for activities of defence-related enzymes viz., total phenol content, chitinase, phenylalanine ammonia lyase (PAL), β-glycosidase, antioxidative enzymes, superoxide dismutase, peroxidase and ascorbate peroxidase. The level of total phenol content and the activity profile of chitinase, PAL and β-glycosidase significantly increased in both blast-resistant and susceptible rice genotypes with comparatively higher level induction Tetep, NLR-20104 and Swarnadhan the blast-resistant genotypes. The antioxidative enzymes were comparatively higher in the leaf samples of blast-resistant genotypes recording highest increase in NLR-20104 and KJT-5. The constitutive levels of total phenols and activity of defence-related and antioxidative enzymes in the control leaf samples differed among the genotypes and were even higher in the two blast susceptible genotypes (EK-70 and Chimansal). However, th...

Water quality modeling intends to represent a water body in order to assess their status and project the effects of different measures taken for their protection. This paper presents the results obtained from the Qual2kw model implementation in the first 50 kilometers of the Aburrá-Medellín River, in their most critical conditions of water quality, which correspond to low flow rates. After the model calibration, three recovery scenarios (short-term, medium-term and long-term) were evaluated. In the first scenario the sanitation only improved in some streams, in accordance with the Plan of Sanitation and Management of Discharges that was considered. Medium and long-term scenarios, with the operation of the new Water Waste Treatment Plant (WWTP) of the Bello municipality and an increase in the sewage collection, were considered. The obtained results show the positive impact of the operation of the WWTP of Bello in the balance of BOD5, dissolved oxygen and nitrogen.