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The research was aimed to evaluate the effect of biogas liquid waste as a fermentation starter of rice husk to the nutrient content, gross energy and bulk density. The method used laboratory experiment using a completely randomized design (CRD) on factorial pattern (6 x 5) with the level of biogas waste liquid : P0-treatment (0% negative control), P0+ (Cellulomonas sp as positive control), P1 (5%), P2 (10%), P3 (15%), P4 (20%) ml/g, and the incubation time : T0 (0 day control ), T1(7 days), T2 (14 days), T3 (21 days) and T4 (28 days). The variables measured was the content of ash, crude protein, crude fiber, crude fat, gross energy and bulk density. Data were analyzed by analysis of variance (anova) CRD Factorial pattern and if there is a significant difference was followed by Duncan's Multiple Range Test. The results of research was the level of biogas liquid waste and the incubation time provides a significant influence (P

Biodegradation of reactive azo dyes has been an arduous problem for decades. Several efficient biosystems have been proposed for dye degradation, but most of them are dependent on the availability of costly co-substrates such as peptone, yeast extract, and/or glucose. The present study describes the azo dye degradation by a bacterial consortium using glycerol as a sole co-substrate. The consortium was developed from a mixed bacterial culture obtained upon enrichment of soil sediment for Reactive Blue 28 (RB28) decolorization in the presence of glycerol (0.1%; v/v). The consortium with three bacterial species, i.e., Stenotrophomonas acidaminiphila APG1, Cellulomonas sp. APG4, and Pseudomonas stutzeri APG2, designated as “SCP,” decolorized 92% of 100 ppm dye in 96 h. The intricacies of the interactions existing within the members of the consortium were resolved by a simple and unique analysis called “BSocial.” Among all the members, Cellulomonas sp. APG4 exerted a net-positive impact for decolorization (%) on the consortium. The net fitness of the community increased when all the three species were present, and thus, all of them were selected for further analysis. Moreover, APG4 seemed to be central in the reductive decolorization as it possessed the highest reductase activity. The dye degradation by the consortium was demonstrated by UV-Visible spectroscopy, HPTLC, and FTIR spectroscopy of control and decolorized cell-free supernatant. The LC-ESI-MS analysis of metabolites extracted from decolorized cell-free medium led to the identification of degradation products, thus leading us to propose the plausible pathway for degradation of RB28 by bacterial consortium. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s42770-020-00303-3) contains supplementary material, which is available to authorized users.

Cellulomonas sp. strain PS-H5 was isolated from Sekinchan Beach in Selangor, Malaysia, using an ex situ cultivation method. The present work reports a high-quality draft annotated genome sequence of this strain and suggests its potential glycoside hydrolase enzymes for cellulose, hemicellulose, and starch degradations.

AIMS Lignocellulosic biomass deconstruction is a bottleneck for obtaining biofuels and value-added products. Our main goal was to characterize the secretome of a novel isolate, Cellulomonas sp. B6, when grown on residual biomass for the formulation of cost-efficient enzymatic cocktails. METHODS AND RESULTS We identified 205 potential CAZymes in the genome of Cellulomonas sp. B6, 91 of which were glycoside hydrolases (GH). By secretome analysis of supernatants from cultures in either extruded wheat straw (EWS), grinded sugar cane straw (SCR) or carboxymethylcellulose (CMC), we identified which proteins played a role in lignocellulose deconstruction. Growth on CMC resulted in the secretion of two exoglucanases (GH6 and GH48) and two GH10 xylanases, while growth on SCR or EWS resulted in the identification of a diversity of CAZymes. From the 32 GHs predicted to be secreted, 22 were identified in supernatants from EWS and/or SCR cultures, including endo- and exoglucanases, xylanases, a xyloglucanase, an arabinofuranosidase/β-xylosidase, a β-glucosidase and an AA10. Surprisingly, among the xylanases, seven were GH10. CONCLUSIONS Growth of Cellulomonas sp. B6 on lignocellulosic biomass induced the secretion of a diverse repertoire of CAZymes. SIGNIFICANCE AND IMPACT OF THE STUDY Cellulomonas sp. B6 could serve as a source of lignocellulose-degrading enzymes applicable to bioprocessing and biotechnological industries.

To achieve bio-scouring or biological degumming of the flax roving, a kind of eco-friendly techniques, an alkalophilic strain was screened from the rotten wrack around Zhoushan archipelago sea area. It was characterized as Cellulomonas sp and named Cellulomonas sp DA8 by measuring the strain morphology, physiology, biochemistry, and the 16s rDNA sequences. Determination of enzyme activity showed that the activities of petinase and xylanase were obtained, and enzyme activities are stable under 50°C and at pH values in the range of 6.5 to 9.0. It was utilized to scour the flax roving under alkaline conditions, and the result showed that the strain had a good characteristic of scouring, and less strength loss of flax fiber was 14.19%. Scanning electron microscopy (SEM) showed that the gum in the flax fiber was mostly degraded, and the most smooth fiber surface was displayed, compared with fiber untreated and scoured by caustic soda.

Complex formation of multisubstrate analogue inhibitor--2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine (PME-6-thio-Gua) with trimeric purine nucleoside phosphorylase from Cellulomonas sp. was investigated using a stopped-flow spectrofluorimetric approach. Results obtained indicate that, in contrast to binding of guanine, i.e., the transition-state conformation trapping ligand, for which binding at each active site is followed by the enzyme conformational change, association of the ground-state analogue PME-6-thio-Gua is a one-step process.

We present the genome of the cellulose-degrading Cellulomonas sp. strain FA1 isolated from an actively serpentinizing highly alkaline spring. Knowledge of this genome will enable studies into the molecular basis of plant material degradation in alkaline environments and inform the development of lignocellulose bioprocessing procedures for biofuel production.

An objective of this study was to develop high cellulase-producing bacteria by mutagenesis and optimization studies. Among 328 mutant strains of Cellulomonas sp. TSU-03, the mutant M23, NTG mutant, gave the highest value of cellulase activity 2008 U/mg protein) followed by mutant M17 (1884 U/mg protein) in CMC medium. The optimum medium and environmental conditions for cellulase production consisted of 4% wastepaper, 1% NaNO3 under cultivation temperature at 35°C with initial pH and agitation speed at 6 and 100 rpm, respectively. Cellulomonas sp. strain M23 produced the highest cellular growth (28.09 ± 2.28 g/L) and FPase, CMCase as well as, β-glucosidase activities at 325, 2420 and 152 U/mg protein, respectively. Under optimal condition, the cellulase activity achieved from strain M23 is 1.28- and 1.30-fold higher than cellulase from mutant M17 and wild type, respectively. After being subcultured 12 times, the cellulase production of the mutant M23 was stable. The results suggested that Cellulomonas sp. M23 had a good potential for production of cellulase by fermentation using a cultivation medium containing wastepaper as the main substrate. Key words: Mutagenesis, NTG, Ultraviolet, Wastepaper.

Novel 1H-pyrazolo[3,4-b]quinoxalines (flavazoles) 14, 15 and 1-aryl-3-quinoxalinyl-1,2,4-triazole 17 were synthesized from the ester 11 via various hydrazones 12, 13 and 16. In the antibacterial screening test of compounds 12–17, compound 14 showed a relatively high antibacterial activity, wherein the MIC value was 25 μg/ml against Bacillus licheniformis KTCC 21425 and Cellulomonas sp. and 50 μg/ml against Salmonella typhimurium KCTC 1925 and Flavobacterium devolans.

Two-hundred and twenty-five mangrove bacterial strains previously isolated from several mangrove areas in the Philippines were qualitatively screened for cellulase production and 154 were found to be capable of cellulase production. Among them, ten strains showed very strong positive cellulase activities, which were then quantified. Five with the statistically highest activities, specifically, BBCS-11, BBCS-14, BBoB2L2-2, BOrMGS-2, and BOrMGS-3, including Cellulomonas sp. BIOTECH 1240 (control), were further subjected to partial optimization studies. The effects of substrate, pH, incubation temperature and incubation time on cellulase productoin were determined. The cellulase activities (U mL -1 ) of the strains under optimized conditions were: 54.80 (Control); 56.60 (BBCS-11); 66.50 (BBCS-14); 50.33 (BBoB2L2-2); 51.04 (BOrMGS-2); and 48.70 (BOrMGS-3). The promising cellulase producers were previously identified: BBCS-11 as Bacillus cereus; BBCS-14 as Bacillus licheniformis; BOrMGS-2 and BOrMGS-3 as Bacillus pumilus; and BBoB2L2-2 as Bacillus sp.

Cellulose degrading bacteria were isolated from the intestinal fluid of the silver cricket Lepisma Sp. and a culture was developed anoxigenically in the cellulose degrading medium following standard laboratory techniques. The cellulolytic activity of the microbe was examined in a broth culture using Whatman 42 filter paper as the source of insoluble cellulose. Activity was measured spectrophotometrically (620nm) following Anthrone reaction of the culture filtrate and the sugar produced was quantified as a factor of time. The pH optimum was found to be between 7 and 8. Temperature profile optimum was between 30–37°C. The microbes appeared as white colonies on a solid medium. Morphologically the bacterium is a gram-positive nonspore forming rod which was tentatively identified as a new strain of Cellulomonas sp.

This project report summarizes the results of a 3-way collaboration between researchers at Montana State University’s (MSU’s) Center for Biofilm Engineering (CBE) (Drs. Robin Gerlach and Al Cunningham), the WSU/NSF IGERT Center for Multiphase Environmental Research (CMER) at Washington State University (WSU) (Dr. Brent Peyton who recently moved to MSU), and the Idaho National Laboratory (INL) (Drs. William Apel and Frank Roberto). At WSU, removal of uranium (U) from aqueous solution was studied using Cellulomonas sp. strain ES6, under anaerobic, non-growth conditions. The Cellulomonadaceae are environmentally relevant subsurface bacteria, and strain ES6 was isolated from the DOE Hanford subsurface. To better understand the role of the pH buffer in the U immobilization process, both bicarbonate and PIPES buffers were used. Our results show for the first time the strain ES6 has multiple U immobilization mechanisms within one organism. Citations to resulting publications are included in the report.

The reduction of Cr(VI), Fe(III), and U(VI) was studied using three recently isolated environmental Cellulomonas sp. (WS01, WS18, and ES5) and a known Cellulomonas strain ( Cellulomonas flavigena ATCC 482) under anaerobic, non-growth conditions. In all cases, these cultures were observed to reduce Cr(VI), Fe(III), and U(VI). In 100 h, with lactate as electron donor, the Cellulomonas isolates (500 mg/l total cell protein) reduced nitrilotriacetic acid chelated Fe(III) [Fe(III)-NTA] from 5 mM to less than 2.2 mM, Cr(VI) from 0.2 mM to less than 0.001 mM, and U(VI) from 0.2 mM to less than 0.12 mM. All Cellulomonas isolates also reduced Cr(VI), Fe(III), and U(VI) in the absence of lactate, while no metal reduction was observed in either the cell-free or heat-killed cell controls. This is the first report of Cellulomonas sp. reducing Fe(III) and U(VI). Further, this is the first report of Cellulomonas spp. coupling the oxidation of lactate, or other unknown electron donors in the absence of lactate, to the reduction of Cr(VI), Fe(III), and U(VI).

A series of 1,1-difluoro-5-(1 H -9-purinyl)-2-pentenylphosphonic acids, ( E )- 2a,b and ( Z )- 2a,b , as well as the related methano analogues (±) -3a,b and (±) -4a,b were prepared for evaluation of their PNP inhibitory activities. The cyclopopane ring and the hypoxanthine residue were found to increase the profile of inhibitory activity. The IC 50 and K i values of difluoro{(1 R ∗,2 S ∗)-2-[2-(6-oxo-6,9-dihydro-1 H 9-purinyl)ethyl]cyclopropyl}methylphosphonic acid (±) -3b toward PNP purified from Cellulomonas sp. were determined to be 70 nM and 8.8nM, respectively.

α-Mannosidase from Cellulomonas sp. released about 70% of the polymannose chains from yeast external invertase. Native and mannose-depleted yeast invertases were compared with regard to various enzymatic properties. It was found that their catalytic activity and thermal and pH stability were identical. However, the mannose-depleted invertase was more sensitive to proteinases such as pronase and subtilisin. The mannose-depleted invertase was less stable than the native enzyme when incubated with sodium dodecyl sulfate. These results show that the polymannose chains of yeast invertase contribute to the high stability of the enzyme.

Cellulomonas sp. isolated from soil produces a high level of α-mannosidase (α-mannanase) inductively in culture fluid. The enzyme had two different molecular weight forms, and the properties of the high-molecular-weight form were reported previously (Takegawa, K. et al. : Biochim. Biophys. Acta, 991, 431–437, 1989). The low-molecular-weight α-mannosidase was purified to homogeneity by polyacrylamide gel electrophoresis. The molecular weight of the enzyme was over 150,000 by gel filtration. Unlike the high-molecular-weight form, the low-molecular-weight enzyme readily hydrolyzed α-1,2- and α-1,3-linked mannose chains.

The commercially available enzyme purine nucleoside phosphorylase (PNP) from Cellulomonas sp. was purified by ion-­exchange chromatography, partially sequenced and crystallized in two different crystal forms using the hanging-drop vapour-diffusion technique. Crystal form A grows as polyeders and/or cubes in the cubic space group P4232 with unit-cell dimension a = 162.5 A. Crystal form B appears as thick plates in the space group P212121 with unit-cell dimensions a = 63.2, b = 108.3 and c = 117.4 A. Both crystal forms contain three monomers (one trimer) in the asymmetric unit.

The ubiquitous enzyme purine nucleoside phosphorylase (PNP, E.C. 2.4.2.1.) catalyzes the reversible phosphorolysis of naturally occurring purine nucleosides, and many analogues, as follows: $$\beta {\rm{ - purine}}\,{\rm{nucleoside}}\,{\rm{ + }}\,{\rm{orthophosphate}}\, \Leftrightarrow \,{\rm{purine}} + \alpha {\rm{ - D - pentose - }}1{\rm{ - phosphate}}$$

Dissociation constants and stoichiometry of binding for interaction of Cellulomonas sp. purine nucleoside phosphorylase with its substrates: inosine/guanosine, orthophosphate, guanine/hypoxanthine and D-ribose-1-phosphate were studied by kinetic and spectrofluorimetric methods.

A cellulolytic bacterium has been isolated from soil and identified as a Cellulomonas sp. Optimization of media components and environmental factors led to a 17-fold increase in cellulase activity within 40 h. The trace elements Zn2+, Co2+ and Cu2+ caused severe inhibition, which could be reduced by the addition of EDTA. The enzymes endoglucanase, exoglucanase and xylanase were always present irrespective of the carbon source used.

The distribution of glycerol dehydrogenase activity was studied with cell-free extracts of bacteria, yeasts, molds and actinomycetes. High activity was found in 4 strains of bacteria and in 3 strains of molds. The enzymes of bacteria were dependent on NAD+ and those of molds were dependent on NADP+. An isolated gram-positive bacterium, which showed the high activity, was identified as Cellulomonas sp. NT3060. The total and specific activities were associated with growth of this strain and reached the maximum at the early stationary phase. Significant high level activity was detected in cell-free extracts from glycerol and glucose media.

A culture of Cellulomonas sp. and Bacillus subtilis was grown using sugar cane bagasse pith from unburnt sugar cane (UCP) as the source of carbohydrates. The yield and production values were proved to be higher than those obtained with burnt sugar cane (BCP).

Six major components exhibiting endo-1,4-\-d-glucanase activity were partially purified from culture filtrates of a newly isolated Cellulomonas sp. using ion-exchange chromatography. Molecular weights (44,000 to 140,000), pH optima (6.0 to 7.0), temperature optima (40 to 50°C), half-life, energy of activation, Kmand other kinetic parameter investigations indicate the existence of 6 different endoglucanases. Further support for this assumption comes from inhibition studies, whereby glucose inhibited the enzyme activities between 15 and 50% at a concentration of 0.034% (1.65 mM) and cellobiose between 0 and 50% at a concentration of 0.1% (2.92 mM). Of all the metals (Hg2+, Co2+, Cu2+, Ca2+, Mg2+, Zn2+, Fe3+) tested, only Hg2+ exhibited a 55% inhibition at 5.0 mM.

Steady-state continuous culture was used to optimize lean chemically defined media for a Cellulomonas sp. and Bacillus cereus strain T. Both organisms were extremely sensitive to variations in trace-metal concentrations. However, medium optimization by this technique proved rapid, and multifactor screening was easily conducted by using a minimum of instrumentation. The optimized media supported critical dilution rates of 0.571 and 0.467 h −1 for Cellulomonas and Bacillus , respectively. These values approximated maximum growth rate values observed in batch culture.