Bacillus sp. strain MRS-1: A potential candidate for uranyl biosorption from uranyl polluted sites.

The uranyl tolerance of a metal-resistant Bacillus sp. strain MRS-1, was determined in this current study. This was done due to a rise in anthropogenic activities, such as the production of uranium-based nuclear energy, which contributes to environmental degradation and poses risks to ecosystems and human health. The purpose of the research was to find effective strategies for uranium removal to minimize the contamination. In this paper, the biosorption of uranyl was investigated by batch tests. Bacteria could continue to multiply up to 350 ppm uranyl concentrations, however this growth was suppressed at 400 ppm, that generally accepted as the minimum concentration for bacterial growth inhibition. The optimal conditions for uranyl biosorption were pH 7, 20 °C, and a contact duration of 30 min with living bacteria. According to the findings of an investigation that used isotherm and kinetics models (Langmuir, Freundlich and pseudo second order), Bacillus sp. strain MRS-1 biosorption seemed to be dependent on monolayer adsorption as well as certain functional groups that had a strong affinity for uranyl confirmed by Fourier Transform Infrared Spectroscopy (FTIR) analysis. The shifts/sharping of peaks (1081-3304 cm-1) were prominent in treated samples compared to control one. These functional groups could be hydroxyl, amino, and carboxyl. Our findings showed that Bacillus sp. strain MRS-1 has an elevated uranyl biosorption ability, with 24.5 mg/g being achieved. This indicates its potential as a powerful biosorbent for dealing with uranium contamination in drinking water sources and represents a breakthrough in the cleanup of contaminated ecosystems.

Lead metal biosorption and isotherms studies by metal-resistant Bacillus strain MRS-2 bacterium.

In this study, lead (Pb) biosorption studies in aqueous solution were performed with metal-resistant Bacillus strain MRS-2 (ATCC 55674) bacterium which was previously isolated from wastewater plant. It showed minimum inhibition concentration of 300 ppm Pb on the nutrient agar plates. Pb biosorption using MRS-2 bacteria was investigated under different parameters such as pH, temperature, biomass dosage, initial Pb concentration, contact time, and type of biomass by batch experiments. Pb concentration was analyzed through Inductively coupled plasma-optical emission spectrometry. The rate of biosorption (Q) and Pb biosorption capacity (qe ) were calculated for above mentioned parameters. It was observed that Pb precipitates by itself from the solution at pH 2 and 8 or above without bacteria and precipitation did not increase even in the presence of bacteria. The results showed that the highest biosorption rate and biosorption capacity (mg/g) were observed at pH 7, 25°C, 2-h contact time with live bacteria. The highest biosorption rate was observed at 1.5 g/L biomass dose and 5 ppm initial Pb concentration, whereas the highest Pb biosorption capacity was observed at 0.25 g/L biomass dose and 12.5 ppm initial Pb concentration. It was observed that Pb biosorption by live bacteria occurred through adsorption on cell surface. In this study, the biosorption isotherm analysis favored the Langmuir isotherm model indicating monolayer biosorption. This Bacillus strain showed higher Pb biosorption capacity than most of the previously reported Bacillus strains. In conclusion, this study indicates that the Bacillus MRS-2 strain can be used to remove Pb from industrial wastewaters in an ecofriendly approach.

Skeletal Muscle Protein Composition Adaptations to 10 Weeks of High-Load Resistance Training in Previously-Trained Males.

While high-load resistance training increases muscle hypertrophy, the intramuscular protein responses to this form of training remains largely unknown. In the current study, recreationally resistance-trained college-aged males (N = 15; mean ± SD: 23 ± 3 years old, 6 ± 5 years training) performed full-body, low-volume, high-load [68-90% of one repetition maximum (1RM)] resistance training over 10 weeks. Back squat strength testing, body composition testing, and a vastus lateralis biopsy were performed before (PRE) and 72 h after the 10-week training program (POST). Fiber type-specific cross-sectional area (fCSA), myofibrillar protein concentrations, sarcoplasmic protein concentrations, myosin heavy chain and actin protein abundances, and muscle tissue percent fluid were analyzed. The abundances of individual sarcoplasmic proteins in 10 of the 15 participants were also assessed using proteomics. Significant increases (p < 0.05) in type II fCSA and back squat strength occurred with training, although whole-body fat-free mass paradoxically decreased (p = 0.026). No changes in sarcoplasmic protein concentrations or muscle tissue percent fluid were observed. Myosin heavy chain protein abundance trended downward (-2.9 ± 5.8%, p = 0.069) and actin protein abundance decreased (-3.2 ± 5.3%, p = 0.034) with training. Proteomics indicated only 13 sarcoplasmic proteins were altered with training (12 up-regulated, 1 down-regulated, p < 0.05). Bioinformatics indicated no signaling pathways were affected, and proteins involved with metabolism (e.g., ATP-PCr, glycolysis, TCA cycle, or beta-oxidation) were not affected. These data comprehensively describe intramuscular protein adaptations that occur following 10 weeks of high-load resistance training. Although previous data from our laboratory suggests high-volume resistance training enhances the ATP-PCr and glycolytic pathways, we observed different changes in metabolism-related proteins in the current study with high-load training.

An optimized procedure for isolation of rodent and human skeletal muscle sarcoplasmic and myofibrillar proteins.

Several published protocols exist for isolating contractile or myofibrillar (MF) proteins from skeletal muscle, however, achieving complete resuspension of the myofibril pellet can be technically challenging. We performed several previously published MF isolation methods with the intent of determining which method was most suitable for MF protein isolation and solubilization. Here, we provide an optimized protocol to isolate sarcoplasmic and solubilized MF protein fractions from mammalian skeletal muscle suitable for several downstream assays.

Skeletal Muscle Myofibrillar Protein Abundance Is Higher in Resistance-Trained Men, and Aging in the Absence of Training May Have an Opposite Effect.

Resistance training generally increases skeletal muscle hypertrophy, whereas aging is associated with a loss in muscle mass. Interestingly, select studies suggest that aging, as well as resistance training, may lead to a reduction in the abundance of skeletal muscle myofibrillar (or contractile) protein (per mg tissue). Proteomic interrogations have also demonstrated that aging, as well as weeks to months of resistance training, lead to appreciable alterations in the muscle proteome. Given this evidence, the purpose of this small pilot study was to examine total myofibrillar as well as total sarcoplasmic protein concentrations (per mg wet muscle) from the vastus lateralis muscle of males who were younger and resistance-trained (denoted as YT, n = 6, 25 ± 4 years old, 10 ± 3 self-reported years of training), younger and untrained (denoted as YU, n = 6, 21 ± 1 years old), and older and untrained (denoted as OU, n = 6, 62 ± 8 years old). The relative abundances of actin and myosin heavy chain (per mg tissue) were also examined using SDS-PAGE and Coomassie staining, and shotgun proteomics was used to interrogate the abundances of individual sarcoplasmic and myofibrillar proteins between cohorts. Whole-body fat-free mass (YT > YU = OU), VL thickness (YT > YU = OU), and leg extensor peak torque (YT > YU = OU) differed between groups (p < 0.05). Total myofibrillar protein concentrations were greater in YT versus OU (p = 0.005), but were not different between YT versus YU (p = 0.325). The abundances of actin and myosin heavy chain were greater in YT versus YU (p < 0.05) and OU (p < 0.001). Total sarcoplasmic protein concentrations were not different between groups. While proteomics indicated that marginal differences existed for individual myofibrillar and sarcoplasmic proteins between YT versus other groups, age-related differences were more prominent for myofibrillar proteins (YT = YU > OU, p < 0.05: 7 proteins; OU > YT = YU, p < 0.05: 11 proteins) and sarcoplasmic proteins (YT = YU > OU, p < 0.05: 8 proteins; OU > YT&YU, p < 0.05: 29 proteins). In summary, our data suggest that modest (~9%) myofibrillar protein packing (on a per mg muscle basis) was evident in the YT group. This study also provides further evidence to suggest that notable skeletal muscle proteome differences exist between younger and older humans. However, given that our n-sizes are low, these results only provide a preliminary phenotyping of the reported protein and proteomic variables.

Muscle fiber hypertrophy in response to 6 weeks of high-volume resistance training in trained young men is largely attributed to sarcoplasmic hypertrophy.

Cellular adaptations that occur during skeletal muscle hypertrophy in response to high-volume resistance training are not well-characterized. Therefore, we sought to explore how actin, myosin, sarcoplasmic protein, mitochondrial, and glycogen concentrations were altered in individuals that exhibited mean skeletal muscle fiber cross-sectional area (fCSA) hypertrophy following 6 weeks of high-volume resistance training. Thirty previously resistance-trained, college-aged males (mean ± standard deviation: 21±2 years, 5±3 training years) had vastus lateralis (VL) muscle biopsies obtained prior to training (PRE), at week 3 (W3), and at week 6 (W6). Muscle tissue from 15 subjects exhibiting PRE to W6 VL mean fCSA increases ranging from 320-1600 µm2 was further interrogated using various biochemical and histological assays as well as proteomic analysis. Seven of these individuals donated a VL biopsy after refraining from training 8 days following the last training session (W7) to determine how deloading affected biomarkers. The 15 fCSA hypertrophic responders experienced a +23% increase in mean fCSA from PRE to W6 (p<0.001) and, while muscle glycogen concentrations remained unaltered, citrate synthase activity levels decreased by 24% (p<0.001) suggesting mitochondrial volume decreased. Interestingly, repeated measures ANOVAs indicated that p-values approached statistical significance for both myosin and actin (p = 0.052 and p = 0.055, respectively), and forced post hoc tests indicated concentrations for both proteins decreased ~30% from PRE to W6 (p<0.05 for each target). Phalloidin-actin staining similarly revealed actin concentrations per fiber decreased from PRE to W6. Proteomic analysis of the sarcoplasmic fraction from PRE to W6 indicated 40 proteins were up-regulated (p<0.05), KEGG analysis indicated that the glycolysis/gluconeogenesis pathway was upregulated (FDR sig. <0.001), and DAVID indicated that the following functionally-annotated pathways were upregulated (FDR value <0.05): a) glycolysis (8 proteins), b) acetylation (23 proteins), c) gluconeogenesis (5 proteins) and d) cytoplasm (20 proteins). At W7, sarcoplasmic protein concentrations remained higher than PRE (+66%, p<0.05), and both actin and myosin concentrations remained lower than PRE (~-50%, p<0.05). These data suggest that short-term high-volume resistance training may: a) reduce muscle fiber actin and myosin protein concentrations in spite of increasing fCSA, and b) promote sarcoplasmic expansion coincident with a coordinated up-regulation of sarcoplasmic proteins involved in glycolysis and other metabolic processes related to ATP generation. Interestingly, these effects seem to persist up to 8 days following training.

Quantitative aspects of inorganic nutrient fluxes in the Gazi Bay (Kenya): implications for coastal ecosystems.

Fluxes of dissolved inorganic nutrients: NH4+, NO2-, NO3-, PO4(3-) and Si(OH)4 from nearshore sediments of Gazi Bay were measured in situ within mangrove, seagrass and coral reef biotopes using benthic flux bell-jar chambers of cross-sectional area 0.066 m2 and volume 0.0132 m3. The objectives were: (1) to determine the influence of benthic fluxes, fluvial discharge and seasonal variations on the nutrient budget in the Bay waters; (2) to determine the effect of tidal and spatial variations on nutrient loads in the water column and (3) to establish the relative importance of the nutrient sources with regard to total community production of the Bay. The directly measured fluxes ranged from -270 to +148 micromol NH4+-N/m2/h; -60 to +63 micromol NO2(-)-N/m2/h; -79 to +41 micromol NO3(-)-N/m2/h; -79 to +75 micromol PO4(3-)-P/m2/h and +30 to +350 micromol Si(OH)4-Si/m2/h for and respectively. It was established that benthic fluxes are the major sources of dissolved inorganic NH4+, NO2- and Si(OH)4 while fluvial sources are important for NO3- and PO4(3-) into Gazi Bay waters. Seasonal variations had an appreciable effect on the PO4(3-) fluxes, N:Si ratio, river nutrient discharge, plankton productivity and important environmental factors such as salinity and temperature. Tidal and spatial variations had no significant effect on nutrient concentrations and net fluxes within the water column. The results imply that benthic fluxes are largely responsible for the nutrient dynamics of the nearshore coastal ecosystems especially where direct terrestrial inputs do not contribute significantly to the nutrient budget.