scholarly journals Enhancement of Cellulose Rich Organic Matter Degradation by Inoculation with Streptomyces sp. Strains

2021 ◽  
Vol 26 (02) ◽  
pp. 257-262
Author(s):  
Simonida Djuri
Keyword(s):  
Organic Matter ◽  
Extracellular Enzymes ◽  
Biochemical Characterization ◽  
Cellulose Degradation ◽  
Organic Matter Degradation ◽  
Incubation Experiment ◽  
Cellulose Production ◽  
Streptomyces Sp ◽  
Streptomyces Spp

Microbial degradation of organic matter is a vital part of carbon cycle in nature. Actinobacteria play an important role in the decomposition of cellulose rich organic matter (CROM). Streptomyces spp. are abundant in soil, produce various secondary metabolites and secrete extracellular enzymes. The aim of this research was to isolate and select Streptomyces strains with the best cellulose degradation abilities. Out of total 32 actinobacteria isolates, four Streptomyces strains (CA1, CA10, PA2 and PA7) were subjected to morphological, physiological, biochemical characterization and molecular identification. CROM degradation potential of the strains was investigated on straw and beech briquettes as well as on legume based substrate in in vitro condition. Streptomyces strains CA1 and CA10 showed the best cellulose production and starch hydrolysis abilities, followed by strains PA2 and PA7. Strain CA1 was also positive to production of pectinase enzymes. Streptomyces zaomyceticus CA1 and S. tanashiensis CA10 were used as inoculants, which degraded the raw cellulose from 38.38 to 81.69% in the investigated substrates (straw, beech, legume), during a 30-day incubation experiment. CROM inoculation with the selected Streptomyces strains improved and accelerated its degradation in controlled conditions. © 2021 Friends Science Publishers

scholarly journals Short Communication: In vitro antimicrobial and antimalarial screening of a crude extract of Streptomyces sp. AB8 isolated from Lapindo Mud Volcano Area, Sidoarjo, Indonesia

2021 ◽  
Vol 22 (7) ◽  
Author(s):  
Achmad Arifiyanto ◽  
Endah Setyaningrum ◽  
Nismah Nukmal ◽  
Titik Nur Aeny
Keyword(s):  
Crude Extract ◽  
Short Communication ◽  
Biochemical Characterization ◽  
Culture Media ◽  
Antimalarial Activity ◽  
Mud Volcano ◽  
Broth Culture ◽  
Complete Medium ◽  
Streptomyces Sp

Abstract. Arifiyanto A, Setyaningrum E, Nukmal N, Aeny TN. 2021. Short Communication: In vitro antimicrobial and antimalarial screening of a crude extract of Streptomyces sp. AB8 isolated from Lapindo Mud Volcano Area, Sidoarjo, Indonesia. Biodiversitas 22: 2817-2823. Streptomyces is a potential bacterial genus that has been investigated extensively as a source of natural microbial compounds. Its potential metabolites have been widely developed for pharmaceutical, pathogen control, and other applications in agriculture. This study aimed to determine the ability of the Streptomyces sp AB8 crude extract in inhibiting Plasmodium and pathogenic microbes.  Streptomyces was cultured on Gause synthetic media for 10 days. The fermented broth culture media has dissolved in a 1:1 mixture of ethyl acetate and methanol. Biochemical characterization of this isolate has carried out using the standard methods. In-vitro antimalarial activity assay was performed using a chloroquine-sensitive Plasmodium falciparum strain 3D7. Fresh type O-positive human erythrocytes were suspended at 4 percent hematocrit in a complete medium to maintain culture. The inhibitory concentration (IC50) was determined using probit analysis. The results showed the extract of Streptomyces sp. AB8 contains phenolic and alkaloids. Streptomyces sp. AB8 extract can inhibit Dickeya zeae N-Unila 5, Dickeya zeae N-Unila 10, Aspergillus sp IK3, and Escherichia coli growth. The results also showed that the ICs0 value of extract against P. falciparum 3D7 was 17.56 ug/mL. Further research was needed to determine the types of purified bioactive compounds and their bioactivity.

Influence of selected fibrolytic enzymes on the ensiling characteristics and in vitro rumen degradation of maize silage

2002 ◽  
Vol 2002 ◽  
pp. 213-213
Author(s):  
D. Colombatto ◽  
F. L. Mould ◽  
M. K. Bhat ◽  
R. H. Phipps ◽  
E. Owen
Keyword(s):  
Organic Matter ◽  
Initial Rate ◽  
Fibre Content ◽  
Organic Matter Degradation ◽  
Maize Silage ◽  
Enzyme Preparations ◽  
Fibrolytic Enzymes ◽  
Rumen Degradation

Selected fibrolytic enzyme preparations applied at ensiling have been shown to reduce the fibre contents and to increase the initial rate of in vitro organic matter degradation (OMD) of maize silage (Colombatto et al., 2001). However, there is little information on changes in the fibre content of maize forage during the ensiling process, as affected by enzyme addition. The present study examined the effects of characterised enzyme preparations (Colombatto et al., 2000), derived from mesophilic and thermophilic fungal sources applied at ensiling, on the quality and in vitro rumen degradation characteristics of maize silage, as assessed using the Reading Pressure Technique (RPT, Mauricio et al., 1999).

scholarly journals Associative effects between red clover and kikuyu grass silage: Proteolysis reduction and synergy during in vitro organic matter degradation

2017 ◽  
Vol 231 ◽  
pp. 107-110 ◽  
Author(s):  
Gabriela Cristina Guzatti ◽  
Paulo Gonçalves Duchini ◽  
Gilberto Vilmar Kozloski ◽  
Vincent Niderkorn ◽  
Henrique Mendonça Nunes Ribeiro-Filho
Keyword(s):  
Organic Matter ◽  
Red Clover ◽  
Organic Matter Degradation ◽  
Grass Silage ◽  
Kikuyu Grass

scholarly journals Screening of antibiotic-producing Streptomyces from marine sediments of Bangladesh

2017 ◽  
Vol 10 (4) ◽  
pp. 255
Author(s):  
Shajeda Akter Nishat ◽  
Mohammad Morshad Alam
Keyword(s):  
Antibacterial Agents ◽  
Biochemical Characterization ◽  
Antimicrobial Activities ◽  
Soil Samples ◽  
Streptomyces Species ◽  
Streptomyces Spp ◽  
Spore Mass ◽  
Micro Organisms ◽  
Promising Source

<p>Antimicrobial resistance is a rising concern in the treatment of infectious diseases and the discovery of potential antimicrobial compounds is needed to combat against it. The focus of this study was the in vitro antimicrobial activities of Streptomyces obtained from the soil samples collected from different places of Cox’s Bazar, Bangladesh. A total of 156 isolates was obtained from thirty soil samples using two selective media namely yeast malt agar and starch casein agar. The isolates were morphologically distinct on the basis of spore mass color, reverse slide color, aerial and substrate mycelia formation and production of diffusible pigment. Among the isolates, 12 exhibited good antimicrobial activity against the tested micro-organisms. Isolates were subjected to biochemical characterization and identified as Streptomyces spp. The results suggest that the Streptomyces species could be a promising source for potential antibacterial agents.</p>

The in vivo distribution and dynamics of DNA topoisomerase II in Drosophila embryonic nuclei and chromosomes

1993 ◽  
Vol 51 ◽  
pp. 74-75
Author(s):  
Jason R. Swedlow ◽  
Neil Osheroff ◽  
Tim Karr ◽  
John W. Sedat ◽  
David A. Agard
Keyword(s):  
Topoisomerase Ii ◽  
Biochemical Characterization ◽  
Developmental Cycle ◽  
Dna Topoisomerase Ii ◽  
Chromosomal Distribution ◽  
Dna Topoisomerase ◽  
Ideal System ◽  
Dnase Treatment

DNA topoisomerase II is an ATP-dependent double-stranded DNA strand-passing enzyme that is necessary for full condensation of chromosomes and for complete segregation of sister chromatids at mitosis in vivo and in vitro. Biochemical characterization of chromosomes or nuclei after extraction with high-salt or detergents and DNAse treatment showed that topoisomerase II was a major component of this remnant, termed the chromosome scaffold. The scaffold has been hypothesized to be the structural backbone of the chromosome, so the localization of topoisomerase II to die scaffold suggested that the enzyme might play a structural role in the chromosome. However, topoisomerase II has not been studied in nuclei or chromosomes in vivo. We have monitored the chromosomal distribution of topoisomerase II in vivo during mitosis in the Drosophila embryo. This embryo forms a multi-nucleated syncytial blastoderm early in its developmental cycle. During this time, the embryonic nuclei synchronously progress through 13 mitotic cycles, so this is an ideal system to follow nuclear and chromosomal dynamics.

scholarly journals Degradation Products of Polychlorinated Biphenyls and Their In Vitro Transformation by Ligninolytic Fungi

Toxics ◽  
2021 ◽  
Vol 9 (4) ◽  
pp. 81
Author(s):  
Kamila Šrédlová ◽  
Kateřina Šírová ◽  
Tatiana Stella ◽  
Tomáš Cajthaml
Keyword(s):  
Polychlorinated Biphenyls ◽  
Extracellular Enzymes ◽  
Degradation Products ◽  
Transformation Products ◽  
Irpex Lacteus ◽  
Chlorobenzoic Acid ◽  
Ligninolytic Fungi ◽  
Wide Range ◽  
Pcb Metabolites

Metabolites of polychlorinated biphenyls (PCBs)—hydroxylated PCBs (OH‑PCBs), chlorobenzyl alcohols (CB‑OHs), and chlorobenzaldehydes (CB‑CHOs)—were incubated in vitro with the extracellular liquid of Pleurotus ostreatus, which contains mainly laccase and low manganese-dependent peroxidase (MnP) activity. The enzymes were able to decrease the amount of most of the tested OH‑PCBs by > 80% within 1 h; the removal of more recalcitrant OH‑PCBs was greatly enhanced by the addition of the laccase mediator syringaldehyde. Conversely, glutathione substantially hindered the reaction, suggesting that it acted as a laccase inhibitor. Hydroxylated dibenzofuran and chlorobenzoic acid were identified as transformation products of OH‑PCBs. The extracellular enzymes also oxidized the CB‑OHs to the corresponding CB‑CHOs on the order of hours to days; however, the mediated and nonmediated setups exhibited only slight differences, and the participating enzymes could not be determined. When CB‑CHOs were used as the substrates, only partial transformation was observed. In an additional experiment, the extracellular liquid of Irpex lacteus, which contains predominantly MnP, was able to efficiently transform CB‑CHOs with the aid of glutathione; mono‑ and di-chloroacetophenones were detected as transformation products. These results demonstrate that extracellular enzymes of ligninolytic fungi can act on a wide range of PCB metabolites, emphasizing their potential for bioremediation.

scholarly journals Identification and Biochemical Characterization of High Mobility Group Protein 20A as a Novel Ca2+/S100A6 Target

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 510
Author(s):  
Maho Yamamoto ◽  
Rina Kondo ◽  
Haruka Hozumi ◽  
Seita Doi ◽  
Miwako Denda ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Biochemical Characterization ◽  
S100 Protein ◽  
High Mobility ◽  
Dependent Manner ◽  
Protein Signaling ◽  
Protein Protein Interactions ◽  
High Mobility Group Protein ◽  
Pulldown Assay

During screening of protein-protein interactions, using human protein arrays carrying 19,676 recombinant glutathione s-transferase (GST)-fused human proteins, we identified the high-mobility protein group 20A (HMG20A) as a novel S100A6 binding partner. We confirmed the Ca2+-dependent interaction of HMG20A with S100A6 by the protein array method, biotinylated S100A6 overlay, and GST-pulldown assay in vitro and in transfected COS-7 cells. Co-immunoprecipitation of S100A6 with HMG20A from HeLa cells in a Ca2+-dependent manner revealed the physiological relevance of the S100A6/HMG20A interaction. In addition, HMG20A has the ability to interact with S100A1, S100A2, and S100B in a Ca2+-dependent manner, but not with S100A4, A11, A12, and calmodulin. S100A6 binding experiments using various HMG20A mutants revealed that Ca2+/S100A6 interacts with the C-terminal region (residues 311–342) of HMG20A with stoichiometric binding (HMG20A:S100A6 dimer = 1:1). This was confirmed by the fact that a GST-HMG20A mutant lacking the S100A6 binding region (residues 311–347, HMG20A-ΔC) failed to interact with endogenous S100A6 in transfected COS-7 cells, unlike wild-type HMG20A. Taken together, these results identify, for the first time, HMG20A as a target of Ca2+/S100 proteins, and may suggest a novel linkage between Ca2+/S100 protein signaling and HMG20A function, including in the regulation of neural differentiation.

Functional and Biochemical Characterization of Immunologically Derived Equine Platelet-Activating Factor

1985 ◽  
Vol 22 (4) ◽  
pp. 375-386 ◽  
Author(s):  
H. C. Wimberly ◽  
D. O. Slauson ◽  
N. R. Neilsen
Keyword(s):  
Functional Activity ◽  
Biochemical Characterization ◽  
Platelet Activating Factor ◽  
Biochemical Properties ◽  
Naturally Occurring ◽  
Rabbit Platelets ◽  
Rapid Reaction ◽  
Specific Challenge

Antigen-specific challenge of equine leukocytes induced the non-lytic release of a platelet-activating factor in vitro. The equine platelet-activating factor stimulated the release of serotonin from equine platelets in a dose-responsive manner, independent of the presence of cyclo-oxygenase pathway inhibitors such as indomethacin. Rabbit platelets were also responsive to equine platelet-activating factor. The release of equine platelet-activating factor was a rapid reaction with near maximal secretion taking place in 30 seconds. Addition of equine platelet-activating factor to washed equine platelets stimulated platelet aggregation which could not be inhibited by the presence of aspirin or indomethacin. Platelets preincubated with equine platelet-activating factor became specifically desensitized to equine platelet-activating factor while remaining responsive to other platelet stimuli such as collagen and epinephrine. The following biochemical properties of equine platelet-activating factor are identical to those properties of 1-0-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine (AGEPC): stability upon exposure to air and acid; loss of functional activity after basecatalyzed methanolysis with subsequent acylation that returned all functional activity; and identical relative mobilities on silica gel G plates developed with chloroform:methanol:water (65:35:6, volume/volume). The combined functional and biochemical characteristics of equine platelet-activating factor strongly suggest identity between this naturally occurring, immunologically derived equine factor and AGEPC.

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