Producer Streptomyces Sp Research Articles

Genome sequence of the bialaphos producer Streptomyces sp. DSM 41527 and two putative phosphonate antibiotic producers Streptomyces sp. DSM 41014 and DSM 41981 from the DSMZ strain collection.

Streptomyces sp. DSM 41014, DSM 41527, and DSM 41981 are three strains from the DSMZ strain collection. Here, we present the draft genome sequences of DSM 41014, DSM 41527, and DSM 41981 with a size of 9.09 Mb, 8.45 Mb, and 9.23 Mb, respectively.

Bioprospecting of desert actinobacteria with special emphases on griseoviridin, mitomycin C and a new bacterial metabolite producing Streptomyces sp. PU-KB10–4

BackgroundBioprospecting of actinobacteria isolated from Kubuqi desert, China for antibacterial, antifungal and cytotoxic metabolites production and their structure elucidation.ResultsA total of 100 actinobacteria strains were selectively isolated from Kubuqi desert, Inner Mongolia, China. The taxonomic characterization revealed Streptomyces as the predominant genus comprising 37 different species, along with the rare actinobacterial genus Lentzea. The methanolic extracts of 60.8% of strains exhibited potent antimicrobial activities against Staphylococcus aureus, Micrococcus luteus, Bacillus subtilis, Escherichia coli, Salmonella enterica, Saccharomyces cerevisiae and high to mild in vitro cytotoxicity against PC3 (prostate cancer) and A549 (lung carcinoma) cell lines. The metabolomics analysis by TLC, HPLC-UV/vis, HPLC-MS and NMR showed the presence of compounds with molecular weights ranging from 100 to 1000 Da. The scale-up fermentation of the prioritized anti-Gram-negative strain PU-KB10–4 (Streptomyces griseoviridis), yielded three pure compounds including; griseoviridin (1; 42.0 mgL− 1) with 20 fold increased production as compared to previous reports and its crystal structure as monohydrate form is herein reported for the first time, mitomycin C (2; 0.3 mgL− 1) and a new bacterial metabolite 4-hydroxycinnamide (3; 0.59 mgL− 1).ConclusionsThis is the first report of the bioprospecting and exploration of actinobacteria from Kubuqi desert and the metabolite 4-hydroxycinnamide (3) is first time isolated from a bacterial source. This study demonstrated that actinobacteria from Kubuqi desert are a potential source of novel bioactive natural products. Underexplored harsh environments like the Kubuqi desert may harbor a wider diversity of actinobacteria, particularly Streptomyces, which produce unique metabolites and are an intriguing source to develop medicinally valuable natural products.

13-Deoxo-13-iminodutomycin, a new neuroprotective compound from Streptomyces sp. RAP78.

A neuroprotective compound (2) was isolated from the culture broth of the dutomycin (1) producer Streptomyces sp. RAP78. The molecular formula of 2 was established as C44H55NO16 by high-resolution FAB-MS. The structure was determined to be a new dutomycin derivative possessing an acetimidoyl group in place of an acetyl group by NMR spectroscopic analysis. 13-Deoxo-13-iminodutomycin (2) but not dutomycin (1) protected C6 rat glioma cells and N18-RE-105 rat primary retina-mouse neuroblastoma hybrid cells from glutamate-induced toxicity with EC50s of 0.12 µM and 0.72 µM, respectively.

Purification, catalytic, kinetic, thermodynamic characterization and stability profile of alkalophilic lipase from Streptomyces sp. SBLWN_MH2

The current work intended to conduct a full descriptive study on lipase from a potential producer Streptomyces sp. SBLWN_MH2 (MG593538), that was previously isolated, to elucidate its characteristic features in an attempt to introduce a new industrial biocatalyst. The purified enzyme appeared as a single protein band of 24 kDa by SDS-PAGE. Among lipases from the genus Streptomyces, it was the most alkalophilic (optimum pH = 10.7; relative activity at pH 12 = 80%). Thermophilic tendency of the enzyme was clearly observed at optimum temperature 60 °C, and showed more than 96% relative activity at 70 °C. Km and Vmax values were 7.345 mM and 96.52 U/mg. The enzyme showed interested activities with inhibitors and organic solvents which highlighted its promising industrial application. The kinetic parameters of thermal inactivation were determined. The energies of activation and denaturation were 7.74 and 42.95 kJ/mol respectively. The temperature quotient (Q10) was 1.09 between 50 and 60 °C. Changes in enthalpy (ΔH) = 40.18, 40.10 and 40.02 kJ/mol at temperatures 60, 70 and 80 °C respectively. Changes in entropy (ΔS) at the same temperatures were −189.26, −190.24 and −189.73 J/mol.K, respectively while the change in Gibbs free energy (ΔG) was 103.21 kJ/mol at 60 °C with a tendency to increase to 105.35 and 106.99 kJ/mol at 70 and 80 °C respectively indicating the more resistance of enzyme against thermal unfolding at higher temperatures.

Characterization of an L-α,β-diaminopropionic acid polymer with comb-like structure isolated from a poly(ε-L-lysine)-producing Streptomyces sp.

Polymers of basic amino acids function as polycationic compounds under physiological conditions and exhibit intriguing biological properties, such as antimicrobial and antiviral activities, immunopotentiating ability, and DNA-binding activity. Poly(ε-L-lysine) (ε-PL) produced by some strains of Streptomyces spp. is a cationic homopolymer of L-lysine linking between ε-amino and α-carboxylic acid functional groups and has been used as a food preservative based on its biocompatibility and biodegradability. An ε-PL-producing strain of Streptomyces sp. USE-33 was found to secrete a novel polycationic substance into its culture broth along with ε-PL. High-performance liquid chromatography analyses and one- and two-dimensional 1H and 13C nuclear magnetic resonance (NMR) experiments, accompanied by NMR titration studies, revealed that the secreted substance was poly[β-(L-diaminopropionyl-L-diaminopropionic acid)], PAP, characterized by an isopeptide backbone linking between the β-amino and α-carboxylic acid groups of L-α,β-diaminopropionic acid (L-Dpr) with pendent L-Dpr residues. PAP had a molecular weight of 500 to 1400, and copolymers composed of the two amino acids L-Dpr and L-lysine were not detected in the producer strain USE-33. The strain coproduced high levels of the two poly(amino acid)s in the presence of glycerol, citrate, and ammonium sulfate at pH 4.0 in a two-stage cultivation procedure. PAP exhibited strong inhibitory activities against several yeasts and weaker activities against bacteria than ε-PL. PAP may share a number of biological functions with ε-PL, and the use of PAP along with ε-PL has potential as a specific and advanced material for technical applications in various fields.Key points• Novel cationic poly(amino acid) was found in an ε-PL-producing Streptomyces species.• The l-α,β-diaminopropionic acid polymer was characterized by a comb-like structure.• The novel poly(amino acid), PAP, exhibited antibacterial and antifungal activities.

A Study on Media Optimization, Characterization and Purification of L-Asparaginase Producing Streptomyces sp. FSOF Strain Isolated from the Bay of Bengal Coastal Line

The vast marine biodiversity provides abundant opportunities for the isolation and characterization of Streptomyces species with therapeutic applications. The present study is focused on isolation, characterization, media optimization of Streptomyces sp. FSOF strain for production and purification of L-Asparaginase at an economic level. Methods: The isolated strain from the intertidal region of Bay of Bengal coastal region is characterized by physicochemical, genotypic and by phylogenetic methods. The growth medium of Streptomyces FSOF strain is optimized for high enzyme activity and further purified by Ion exchange chromatography. Results and Conclusion: The FSOF isolate exhibited 4.3 IU/ml enzyme activity in m9 broth. The enzyme activity of the FSOF strain is further analyzed in various growth mediums where 5.9 IU/ml activity is observed in tryptic soy broth. The purified L-asparaginase from FSOF isolate exhibited 23.33 IU/mg specific activity with 3.12 fold purification. The 16s rRNA sequence of FSOF isolate is found to have 99.88% similarity with Streptomyces albidoflavius and Streptomyces odorifer strains. The sequence is further deposited in GenBank (accession number MN562193.1) for future analysis. © 2020 iGlobal Research and Publishing Foundation. All rights reserved.

CytA, a reductase in the cytorhodin biosynthesis pathway, inactivates anthracycline drugs in Streptomyces

Antibiotic-producing microorganism can develop strategies to deal with self-toxicity. Cytorhodins X and Y, cosmomycins A and B, and iremycin, are produced as final products from a marine-derived Streptomyces sp. SCSIO 1666. These C-7 reduced metabolites show reduced antimicrobial and comparable cytotoxic activities relative to their C-7 glycosylated counterparts. However, the biosynthetic mechanisms and relevant enzymes that drive C-7 reduction in cytorhodin biosynthesis have not yet been characterized. Here we report the discovery and characterization of a reductase, CytA, that mediates C-7 reduction of this anthracycline scaffold; CytA endows the producer Streptomyces sp. SCSIO 1666 with a means of protecting itself from the effects of its anthracycline products. Additionally, we identified cosmomycins C and D as two intermediates involved in cytorhodin biosynthesis and we also broadened the substrate specificity of CytA to clinically used anthracycline drugs.

Characterization and fermentation optimization of novel thermo stable alkaline protease from Streptomyces sp. Al-Dhabi-82 from the Saudi Arabian environment for eco-friendly and industrial applications

In this study a novel thermo stable alkaline protease producing Streptomyces sp. Al-Dhabi-82was isolated from the soil. The effect of fermentation period on enzyme production by Streptomyces sp. Al-Dhabi-82 was optimized in submerged fermentation. Protease activity was found to be maximum after 5 days of incubation (129.5 ± 7.1 U/ml) and depleted after 6 days of incubation (113.8 ± 4.1 U/ml). Enzyme production increases with the increase in pH up to 9.0 (136.2 ± 3.6 U/ml) and enzyme production depleted significantly at pH 11.0 (67 ± 2.9 U/ml). Maximum production of protease was observed at 40 °C (164 ± 11.1 U/ml). Among the evaluated carbon sources, maltose significantly influenced on protease production (212 ± 14.8 U/ml). The optimum amount of protease (269 ± 10.4 U/ml) produced by Streptomyces sp. Al-Dhabi-82 was observed in the production medium containing yeast extract. Enzyme production was maximum in the presence of 0.15% Ca2+. The specific activity of crude enzyme was 26 U/ mg protein and it increased as 276 U/mg protein after chromatography separation. The molecular weight of purified protease obtained from sephadex G-75 gel filtration chromatography was estimated to be 37 kDa using SDS-PAGE. This enzyme showed high activity at pH 9.0, and lost about 16% activity at pH 10. The optimum temperature for Streptomyces sp. Al-Dhabi-82 protease was 40 °C. The extracellular alkaline protease from Streptomyces sp. Al-Dhabi-82 hydrolyzed chicken feather completely.

Discovery and Biosynthesis of Neoenterocins Indicate a Skeleton Rearrangement of Enterocin.

Two polyketides neoenterocins A (1) and B (2), featuring a neighboring dicarbonyl motif and a furan-containing 5/6 ring system, were isolated from the enterocin producer Streptomyces sp. SCSIO 11863. Heterologous expression, gene disruptions, and isotope feeding experiments indicated that 1 and 2 were derived from the enterocin biosynthetic gene cluster. However, 2 was demonstrated as an artifact from enterocin via a unique skeleton rearrangement.

Complete Genome Sequence of the Putative Phosphonate Producer Streptomyces sp. Strain I6, Isolated from Indonesian Mangrove Sediment.

Streptomyces sp. strain I6 is a novel strain isolated from an Indonesian mangrove sediment sample. Bioinformatic analysis of the genome sequence of Streptomyces sp. I6 revealed 23 biosynthetic gene clusters. One of them encodes the synthesis of a putative phosphonate secondary metabolite, a class of underexplored natural compounds with great pharmaceutical potential.

Ragi Husk as Substrate for Cellulase Production Under Temperature Mediated Solid State Fermentation by <i>Streptomyces</i> Sp

Cellulases have diversity of industrial applications and their cost effective production using agroindustrial wastes by solid state fermentation poses an efficient method. Actinomycetes are considered highly valuable due to their secondary metabolites production and in this study, an attempt was made to optimize the use of ragi husk and refine the process of cellulase production by temperature mediated solid state fermentation. Actinomycetes were isolated from paper mill industry soil and cellulase producing Streptomyces sp was selected for the experiments. Ragi husk was used as substrate for solid state fermentation of cellulase and varying incubation temperatures (20°C, 25°C, 30°C, 35°C and 40°C) was considered to determine its effect on enzyme activity after 6th, 9th and 12th day of fermentation. The carboxymethyl cellualse (CMC-ase) activity was measured and the observations obtained were compared with the standard glucose curve to determine the amount of reducing sugar (µg ml-1) released. Enzyme activity was highest at 35°C and was recorded as 35.14, 45.90 and 59.56 IU ml-1 at the end of 6th, 9th and 12th day of fermentation. Highest amount of reducing sugars at a concentration of 322 µg ml-1 was released at the end of 12th day at 35°C. The results indicated that the enzyme activity was temperature dependent while using ragi husk as growth substrate under solid state fermentation.

Biogenic synthesis of silver nanoparticles using pigment producing Streptomyces sp and Its drug binding assay

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Resistance to Enediyne Antitumor Antibiotics by Sequestration

The enediynes, microbial natural products with extraordinary cytotoxicities, have been translated into clinical drugs. Two self-resistance mechanisms are known in the enediyne producers-apoproteins for the nine-membered enediynes and self-sacrifice proteins for the ten-membered enediyne calicheamicin. Here we show that: (1) tnmS1, tnmS2, and tnmS3 encode tiancimycin (TNM) resistance in its producer Streptomyces sp. CB03234, (2) tnmS1, tnmS2, and tnmS3 homologs are found in all anthraquinone-fused enediyne producers, (3) TnmS1, TnmS2, and TnmS3 share a similar β barrel-like structure, bind TNMs with nanomolar KD values, and confer resistance by sequestration, and (4) TnmS1, TnmS2, andTnmS3 homologs are widespread in nature, including in the human microbiome. These findings unveil an unprecedented resistance mechanism for the enediynes. Mechanisms of self-resistance in producers serve as models to predict and combat future drug resistance in clinical settings. Enediyne-based chemotherapies should now consider the fact that the human microbiome harbors genes encoding enediyne resistance.

Isolation of Chitinase Producing Streptomyces Sp. M1 for Recycling of Fungal Biomass

Isolation of Chitinase Producing Streptomyces Sp. M1 for Recycling of Fungal Biomass

Exploring the biocombinatorial potential of benzoxazoles: generation of novel caboxamycin derivatives

BackgroundThe biosynthesis pathway of benzoxazole compounds caboxamycin and nataxazole have been recently elucidated. Both compounds share one of their precursors, 3-hydroxyanthranilate (two units in the case of nataxazole). In addition, caboxamycin structure includes a salicylate moiety while 6-methylsalycilate is the third scaffold in nataxazole. Pathways cross-talk has been identified in caboxamycin producer Streptomyces sp. NTK937, between caboxamycin and enterobactin pathways, and nataxazole producer Streptomyces sp. Tü6176, between nataxazole and coelibactin pathways. These events represent a natural form of combinatorial biosynthesis.ResultsEleven novel caboxamycin derivatives, and five putative novel derivatives, bearing distinct substitutions in the aryl ring have been generated. These compounds were produced by heterologous expression of several caboxamycin biosynthesis genes in Streptomyces albus J1074 (two compounds), by combinatorial biosynthesis in Streptomyces sp. NTK937 expressing nataxazole iterative polyketide synthase (two compounds) and by mutasynthesis using a nonproducing mutant of Streptomyces sp. NTK937 (12 compounds). Some of the compounds showed improved bioactive properties in comparison with caboxamycin.ConclusionsIn addition to the benzoxazoles naturally biosynthesized by the caboxamycin and nataxazole producers, a greater structural diversity can be generated by mutasynthesis and heterologous expression of benzoxazole biosynthesis genes, not only in the respective producer strains but also in non-benzoxazole producers such as S. albus strains. These results show that the production of a wide variety of benzoxazoles could be potentially achieved by the sole expression of cbxBCDE genes (or orthologs thereof), supplying an external source of salicylate-like compounds, or with the concomitant expression of other genes capable of synthesizing salicylates, such as cbxA or natPK.

Elimination of indigenous linear plasmids in Streptomyces hygroscopicus var. jinggangensis and Streptomyces sp. FR008 to increase validamycin A and candicidin productivities.

Giant linear plasmids, which replicate independently of the chromosomes, widely exist in actinobacteria. Previous studies mostly focused on the replication and evolution of the linear plasmids or the secondary metabolite gene clusters and the resistance gene clusters therein. However, the relationships of the linear plasmids to the productivities of secondary metabolites have not been studied. In this work, we developed a method to eliminate the indigenous linear plasmid pSHJG1 in Streptomyces hygroscopicus var. jinggangensis, and validamycin A titer increased by 12.5% (from 19.16±1.93 to 21.56±2.25g/L) in the high-yielding strain TL01 and 43.7% (from 4.67±0.05 to 6.71±0.21g/L) in the wild-type strain 5008, whereas the cellular growth of the plasmid-cured mutant was reduced. Subsequently, the plasmid-cured mutant was complemented with three structure genes involved in cellular growth in pSHJG1 under the control of a strong PvalA promoter. Among them, the complementation of genes pSHJG1.069 and pSHJG1.072, encoding a putative hydrolase and putative P-loop ATPase, respectively, resulted in the restoration of cellular growth and validamycin A titer. Furthermore, the elimination of indigenous linear plasmid pHZ228 in the candicidin producer Streptomyces sp. FR008 also led to enhanced candicidin production and reduced cellular growth. Because of the wide distribution of indigenous linear plasmids in actinobacteria, the engineering strategy described here could be implemented in a variety of strains for the overproduction of various natural products.

Isolation and Identification of a New Cold and Alkaline Tolerant Antibiotic Producing Streptomyces sp. From Soil

Background: The ever-increasing resistance of microorganisms to pathogens and our inability to control infectious diseases indicate the importance of conducting research to find new antibiotics. Objectives: The aim of the present research was to isolate, identify, and optimize a cold and pH resistant strain of Streptomyces with high antibiotic production capability. Methods: Soil samples were taken from the Telar forests of northern Iran, and the ACS52 strain was identified as a Streptomyces strain based on the morphological, biochemical, and 16S rRNA gene analysis. Antibacterial features of the obtained strain were studied against a wide range of Gram-positive and Gram-negative bacteria using the cross-culture method. In order to evaluate the antibacterial activity of culture product, two seed cultures and three fermentation media were examined. Finally, the effects of various factors such as the type of carbon and nitrogen sources, temperature, pH, and inoculation rate were investigated. Results: Streptomyces sp. ACS52 is a cold-resistant alkalophilic bacterium strain with antibacterial activity against a broad spectrum of pathogenic bacteria. The fermentation medium containing glycerol and ethyl acetate was suitable for the production and extraction of antibacterial compound, respectively. Glycerol and starch as the carbon source, soybean extract as the nitrogen source, temperature of 25°C, pH of 7, and inoculation rate of 10% were found to provide the optimal conditions for the antibacterial activity. Conclusions: The crude extract of Streptomyces sp. ACS52 had high antibacterial activity against a wide spectrum of bacteria and could be of interest due to its features such as ability to grow at low temperatures and alkaline pH levels.

Nitrilase mediated conversion of Indole-3-acetonitrile to Indole-3-acetic acid

Abstract An attempt has been made for the conversion of Indole-3-acetonitrile to Indole-3-acetic acid using whole cells of a thermostable nitrilase producing Streptomyces sp. MTCC 7546 as an enzyme source. The whole cell enzyme activity showed a broad pH range of action with an optimum at 7.5. The optimal temperature for the maximum conversion was 60 °C. The whole cells also showed good thermal stability with half-lives of 8 h at 50 °C, 5 h at 60 °C and 0.5 h at 70 °C, respectively. The Km and Vmax calculated from the Lineweaver plot were 1.3 mM and 28 µM/min. Among different solvents used for assessment on activity, 10% methanol (v/v of reaction mixture) showed maximum nitrilase specific cell activity. TLC, HPLC, FTIR and mass spectroscopy were performed for identification, confirmation as well as quantification of Indole 3-acetic acid.

Optimization, production and characterization of glycolipid biosurfactant from the marine actinobacterium, Streptomyces sp. MAB36

A potential glycolipid biosurfactant producer Streptomyces sp. MAB36 was isolated from marine sediment samples. Medium composition and culture conditions for the glycolipid biosurfactant production by Streptomyces sp. MAB36 were optimized, using two statistical methods: Plackett-Burman design was applied to find out the key ingredients and conditions for the best yield of glycolipid biosurfactant production and central composite design was used to optimize the concentration of the four significant variables, starch, casein, crude oil and incubation time. Fructose and yeast extract were the best carbon and nitrogen sources for the production of the glycolipid biosurfactant. Biochemical characterizations including FTIR and MS studies suggested the glycolipid nature of the biosurfactant. The isolated glycolipid biosurfactant reduced the surface tension of water from 73.2 to 32.4mN/m. The purified glycolipid biosurfactant showed critical micelle concentrations of 36mg/l. The glycolipid biosurfactant was effective at very low concentrations over a wide range of temperature, pH, and NaCl concentration. The purified glycolipid biosurfactant showed strong antimicrobial activity. Thus, the strain Streptomyces sp. MAB36 has proved to be a potential source of glycolipid biosurfactant that could be used for the bioremediation processes in the marine environment.

Optimization of protease production by Streptomyces sp. A6 using statistical approach for reclamation of shellfish waste

Protease producing Streptomyces sp. A6 was isolated from intertidal zone of the coast of Diu (Gujarat, India). Plackett–Burman method was applied to identify important factors (shrimp waste, FeCl3, ZnSO4 and pH) influencing protease production by Streptomyces sp. A6. Further optimization was done by response surface methodology using central composite design. The concentrations of medium components for higher protease production as optimized using the above approach were (g l−1): Shrimp waste, 14; FeCl3, 0.035; ZnSO4, 0.065 and pH, 8.0. This statistical optimization approach led to production of 129.02 ± 2.03 U ml−1 of protease which was 4.96 fold higher compared to that obtained using the unoptimized medium. The protease production was scaled to 3 l in a 5-l bench fermenter using optimized medium which further increased the production by 63.4%. Deproteinization and chitin recovery obtained at the end of fermentation was 85.12 ± 4.7 and 70.58 ± 1.33%, respectively. The present study is the first report on statistical optimization of medium components for production of protease by Streptomyces species using cheaper raw material such as shrimp waste. The study also explored the possibility Streptomyces sp. A6 for reclamation of shrimp wastes.