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1.
Curr Res Microb Sci ; 6: 100228, 2024.
Article in English | MEDLINE | ID: mdl-38450031

ABSTRACT

In order to comply with the stringent discharge guidelines issued by governmental organizations to protect the ecosystem, the substantial amounts of effluent and sturdy wastes produced by the beer brewing process need to be discarded or handled in the most affordable and secure manner. Huge quantities of waste material released with each brew bestow a significant opportunity for the brewing sector to move towards sustainability. The concept of circular economy and the development of technological advancements in brewery waste processing have spurred interest to valorize brewery waste for implementation in various sectors of medical and food science, industrial science, and many more intriguing fields. Biotechnological methods for valorizing brewery wastes are showing a path towards green chemistry and are feasible and advantageous to environment. The study unfolds most recent prospectus for brewery waste usage and discusses major challenges with brewery waste treatment and valorization and offers suggestions for further work.

2.
Prep Biochem Biotechnol ; 54(4): 573-586, 2024 Apr.
Article in English | MEDLINE | ID: mdl-37729443

ABSTRACT

Four laccase-producing bacteria were found in soil samples from the Similipal Biosphere Reserve in Odisha, according to the current study. The isolates (SLCB1 to SLCB4) were evaluated for their laccase-producing ability in LB broth supplemented with guaiacol. The ABTS assay was performed to assess the laccase activity. The bacterium Mammaliicoccus sciuri shows the highest laccase activity i.e., 0.5125 U/L at the optimized conditions of pH 5.5, temperature 32.5 °C, ABTS concentration of 0.75 µl with an incubation time of 9 d. Laccase activity of M. sciuri grown in Sawdust was significantly increased in comparison to that in other agro wastes. The partially purified laccase enzyme after ammonium sulfate precipitation and dialysis showed a molecular weight of ∼58.5 kDa as determined by SDS-PAGE. A decolorization efficiency of 66.67% was recorded for the dye crystal violet after 1 h treatment with dialyzed laccase enzyme compared with phenol red, brilliant blue, and methylene blue.


Subject(s)
Benzothiazoles , Coloring Agents , Laccase , Sulfonic Acids , Coloring Agents/chemistry , Laccase/chemistry , Gentian Violet , Soil , Temperature , Hydrogen-Ion Concentration
3.
In Silico Pharmacol ; 12(1): 5, 2024.
Article in English | MEDLINE | ID: mdl-38148755

ABSTRACT

The human respiratory syncytial virus (RSV) creates a pandemic every year in several countries in the world. Lack of target therapeutics and absence of vaccines have prompted scientists to create novel vaccines or small chemical treatments against RSV's numerous targets. The matrix (M) protein and fusion (F) glycoprotein of RSV are well characterized and attractive drug targets. Five bioactive compounds from Alnus japonica (Thunb.) Steud. were taken into consideration as lead compounds. Drug-likeness characters of them showed the drugs are non-toxic and non-mutagenic and mostly lipophobic. Molecular docking reveals that all bioactive compounds have better binding and better inhibitory effect than ribavirin which is currently used against RSV. Praecoxin A appeared as the best lead compound between them. It creates 7 different types of bonds with amino acids of M protein and 5 different types of bonds with amino acids of F protein. Van der Waals interactions highly influenced the binding energies. Molecular dynamic simulations represent the non-deviated and less fluctuating nature of praecoxin A. Principal Component Analysis showed praecoxin A complex with RSV matrix protein is more stable than ribavirin complex. This study will help to develop a new drug to inhibit RSV. All ligands were minimized through semi-empirical PM3 process with MOPAC. Toxicity was tested by ProTox-II server. Molecular docking studies were carried out using AutoDock 4.2. Molecular dynamics simulations for 100 ns were carried out through GROMACS 5.12 MD and GROMOS96 43a1 force field. The graphs were produced by GROMACS's XMGrace program.

4.
J Biomol Struct Dyn ; : 1-23, 2023 Dec 21.
Article in English | MEDLINE | ID: mdl-38126200

ABSTRACT

Cellulases are enzymes that aid in the hydrolysis of cellulosic fibers and have a wide range of industrial uses. In the present in silico study, sequence alignment between cellulases from different Bacillus species revealed that most of the residues are conserved in those aligned enzymes. Three dimensional structures of cellulase enzymes from 23 different Bacillus species have been predicted and based on the alignment between the modeled structures, those enzymes have been categorized into 7 different groups according to the homology in their conformational folds. There are two structural contents in Gr-I cellulase namely ß1-α2 and ß3-α5 loops which varies greatly according to their static position. Molecular docking study between the B. albus cellulase and its various cellulosic substrates including xylanoglucan oligosaccharides revealed that residues viz. Phe154, Tyr258, Tyr282, Tyr285, and Tyr376 of B. albus cellulase are significantly involved in formation stacking interaction during enzyme-substrate binding. Residue interaction network and binding energy analysis for the B. albus cellulase with different cellulosic substrates depicted the strong affinity of XylGlc3 substrate with the receptor enzyme. Molecular interaction and molecular dynamics simulation studies exhibited structural stability of enzyme-substrate complexes which are greatly influenced by the presence of catalytic promiscuity in their substrate binding sites. Screening of B. albus in carboxymethylcellulose (CMC) and xylan supplemented agar media revealed the capability of the bacterium in degrading both cellulose and xylan. Overall, the study demonstrated B. albus cellulase as an effective biocatalyst candidate with the potential role of catalytic promiscuity for possible applications in biofuel industries.Communicated by Ramaswamy H. Sarma.

5.
Indian J Microbiol ; 63(4): 604-620, 2023 Dec.
Article in English | MEDLINE | ID: mdl-38031614

ABSTRACT

Manganese peroxidase (MnP), a microbial ligninolytic enzyme which plays significant role in lignin and melanoidin degradation has gained much attention in the field of industry. In the present study, 15 ligninolytic bacteria were isolated from the soil sample of Similipal Biosphere Reserve (SBR) and screened for MnP activity. The most efficient MnP-producing bacterium HNB5 was evaluated for alkali lignin and maillard reaction products (MRPs) degradation and identified as Enterobacter wuhouensis using 16S rRNA sequencing. This bacterium exhibited the highest MnP activity of 2.6 U mL-1 min-1 in un-optimized conditions. Further, optimization using response surface methodology E. wuhouensis showed increased MnP activity of 4.11 U mL-1 min-1 at pH 6.3, temperature 37 °C, substrate concentration 1.05%, and time 144 h. In both FT-IR and UV-Vis spectrophotometry analyses of control and bacterium degraded MRPs, the reduction in Maillard product colour was correlated with shifting absorption peaks. Also, the GC-MS analysis data showing a change in functional group revealed the rise of novel peaks caused due to the degradation of MRPs complex. The phytotoxicity study was conducted for bacterial degraded MRPs medium revealed that toxicity of the medium decreased after bacterial treatment. The findings of the current study suggest that the manganese MnP produced by E. wuhouensis isolated from SBR soil sample may be employed for bioremediation purposes to degrade MRPs.

6.
Crit Rev Biotechnol ; : 1-21, 2023 Jul 16.
Article in English | MEDLINE | ID: mdl-37455422

ABSTRACT

Lignin is a complex of organic polymers that are abundantly present in the plant cell wall which considered of emerging substrates for various kinds of value-added industrial products. Lignin has potential use for the production of green nanomaterials, which exhibit improved or different properties corresponding to their parent polymers. Nano lignin has received significant interest in recent years due to its applications in numerous fields. Lignin, the abundant and limited functionality has challenges for its potential uses. Creating advanced functional lignin-derived material like lignin nanoparticles (LNPs) which significantly alter the biological process has great potential for its applications. In the fields of biotechnology, several lignin extraction processes from various raw materials and diverse synthesis techniques, including acid precipitation, dialysis, solvent shifting/solvent exchange, antisolvent precipitation, homogenization, water-in-oil (W/O) microemulsion, ultra-sonication, interfacial crosslinking, polymerization, and biological pathway can be employed to produce LNPs. The scientific community has recently become more concerned about the transformation of lignin to lignin nanomaterials, including nanoparticles, nanocapsules, nanofibers, nanotubes, and nanofilms. Recent research has shown that lignin nanoparticles (LNPs) are: non-toxic at adequate amounts (both in vitro and in vivo), are economical, and can be biodegradable by bacteria and fungi. In promising studies, LNPs have been investigated for their potential applications in gene delivery systems, drug carriers, biocatalysts, tissue engineering, heavy metal absorbers, encapsulation of molecules, supercapacitors, hybrid nanocomposites, and other applications. This current review addresses the recent advances in the synthesis of LNPs, their advanced application in different areas, future perspectives, and challenges associated with lignin-based nanomaterials.

7.
Bioresour Technol ; 379: 129045, 2023 Jul.
Article in English | MEDLINE | ID: mdl-37044152

ABSTRACT

Lignin, a highly heterogeneous polymer of lignocellulosic biomass, is intricately associated with cellulose and hemicellulose, responsible for its strength and rigidity. Lignin decomposition is carried out through certain enzymes derived from microorganisms to promote the hydrolysis of lignin. Analyzing multi-omics data helps to emphasize the probable value of fungal-produced enzymes to degrade the lignocellulosic material, which provides them an advantage in their ecological niches. This review focuses on lignin biodegrading microorganisms and associated ligninolytic enzymes, including lignin peroxidase, manganese peroxidase, versatile peroxidase, laccase, and dye-decolorizing peroxidase. Further, enzymatic catalysis, lignin biodegradation mechanisms, vital factors responsible for lignin modification and degradation, and the design and selection of practical metabolic pathways are also discussed. Highlights were made on metabolic pathway engineering, different aspects of omics analyses, and its scope and applications to ligninase enzymes. Finally, the advantages and essential steps of successfully applying metabolic engineering and its path forward have been addressed.


Subject(s)
Lignin , Metabolic Engineering , Lignin/metabolism , Peroxidases/genetics , Peroxidases/metabolism , Laccase/genetics , Laccase/metabolism , Metabolic Networks and Pathways
8.
J Basic Microbiol ; 63(7): 759-780, 2023 Jul.
Article in English | MEDLINE | ID: mdl-37026418

ABSTRACT

Among 24 isolated cellulolytic bacteria from Similipal Biosphere Reserve, the most efficient isolate was recognized as a strain of Bacillus albus. This strain of B. albus was evaluated for cellulase production and the cellulase activity was measured in submerged fermentation using substrate carboxymethyl cellulose (CMC). Different nutritional (carbon, nitrogen, and metal-ion sources) and physical variables (pH, temperature, substrate concentration, and incubation time) during the growth of B. albus were optimized to obtain maximum cellulase activity. The highest cellulase activity of 5.79 U/mL for B. albus was observed at pH 6.75, temperature 37.5°C, CMC concentration 8.5 g/L, and 42 h incubation time. Further, supplementation of glucose as a subsidiary carbon source, yeast extract, peptone as nitrogen sources, and MgSO4 and MnSO4 as metal-ion sources enhance the cellulase activity of B. albus. The purified enzyme was reported to have a molecular weight of ∼54 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A zymogram analysis evidenced the cellulase activity of the purified enzyme fractions obtained from diethylaminoethyl cellulose chromatography. The purified cellulase was reported to have an optimum pH and temperature of 7.0°C and 50°C, respectively with a capacity of retaining its 60% residual activity within pH 6.0-8.0 and temperature 30-40°C, respectively. The metal ions, K+ and Na+ were the activators, while Pb2+ and Hg2+ were the inhibitors for the purified cellulase. The purified cellulase showed Km and Vmax values of 0.38 M and 8.19 U/mL, respectively, in presence of the substrate CMC and also simultaneous consumption of both hexose and pentose sugars.


Subject(s)
Cellulase , Hydrogen-Ion Concentration , Metals , Temperature , Carbon , Nitrogen
9.
Comp Clin Path ; 32(2): 179-189, 2023.
Article in English | MEDLINE | ID: mdl-36687210

ABSTRACT

In the last 3 years of the pandemic situation, SARS-CoV-2 caused a significant number of deaths. Infection rates for symptomatic and asymptomatic patients are higher than that for death. Eventually, researchers explored that the major deaths are attributed to several comorbidity factors. The confounding factors and gender-associated infection/death rate are observed globally. This suggests that SARS-CoV-2 selects the human system recognizing the internal comorbid environment. This article explored the influences of hypertension, diabetes, cardiovascular, and renovascular disorders in COVID-19 severity and mortality. Brief mechanistic layouts have been presented here, indicating some of the comorbidity as the critical determinant in the COVID-19 pathogenesis and related mortality.

10.
J Biomol Struct Dyn ; 41(12): 5757-5775, 2023.
Article in English | MEDLINE | ID: mdl-35838062

ABSTRACT

Laccase is a delignifying enzyme that belongs to the oxidoreductase family, and it has long been investigated as a pretreatment agent in biofuel production. In this study, amino acid sequences of five bacterial laccases from Bifidobacterium breve, Klebsiella pneumonia, Pseudodesulfovibrio hydrargyri, Pseudomonas aeruginosa and Veillonella rodentium have been retrieved from UniProtKB for sequence alignment, phylogenetic analysis using MEGA 7.0 and 3 D structure prediction by homology modeling in SWISS-MODEL. Multiple sequence alignment between all the bacterial laccase sequences revealed a similar structural fold, although the overall protein sequence varied greatly with the substrate binding sites. Further molecular docking in AutoDock Vina and MD stimulation (MDS) in GROMACS for those modelled enzymes were performed considering both apo and ligand bound structures considering both apo and its ligand bound form. Investigation of molecular interaction utilizing docking of five bacterial laccases with three substrates (ABTS, DMP and Guaiacol) revealed that ABTS with K. pneumoniae laccase had the highest binding energy of -7.00 kcal/mol. In the current MDS investigation, bacterial laccases demonstrated greater binding and substrate energy in the ligand bound complex than in the apo form for ABTS, DMP and Guaiacol. In most cases of bacterial laccase, MDS revealed that DMP bound complex was more stable within an average RMSD value lower than 0.5 nm throughout 100 ns time scale. Thus, in silico studies undertaken in this work will be useful in determining the stable enzyme-substrate complex which further might improve the enzymatic catalysis of bacterial laccases for lignin breakdown and biofuel generation.


Subject(s)
Laccase , Lignin , Lignin/chemistry , Lignin/metabolism , Molecular Docking Simulation , Laccase/genetics , Laccase/chemistry , Laccase/metabolism , Phylogeny , Ligands , Biofuels , Molecular Dynamics Simulation , Bacteria/metabolism , Sequence Analysis , Guaiacol , Substrate Specificity
11.
Expert Rev Vaccines ; 21(6): 825-842, 2022 06.
Article in English | MEDLINE | ID: mdl-35313785

ABSTRACT

INTRODUCTION: Since its inception, Coronavirus disease-19 (COVID-19), caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), has claimed a significant number of lives around the world. AREA COVERED: COVID-19 vaccine development involves several vaccine platforms, including traditional live-attenuated or killed viral particles, viral vectors or DNA, and mRNA-based vaccines. The efficacy and effectiveness (EV) of these vaccines must be assessed in order to determine the extent to which they can protect us against infection. Despite the fact that some affluent countries attempted to vaccinate the majority of their inhabitants, children and pregnant women were first excluded. EXPERT OPINION: While the severity of COVID-19 is less severe in children, the COVID-19-related complications are more severe.SARS-CoV-2 infection is also dangerous for pregnant women. The key to limiting disease spread is early discovery, isolation, and the development of safe and efficient vaccinations. As a result, the purpose of this study is to highlight the current development of various COVID-19 vaccine platforms for different groups of people at higher risk of COVID-19, with a special focus on children, pregnant and lactating women, as well as structural and pathogenicity elements of SARS CoV-2.


Subject(s)
COVID-19 , COVID-19/prevention & control , COVID-19 Vaccines/adverse effects , Child , Female , Humans , Lactation , Pregnancy , SARS-CoV-2 , Vaccination
12.
J Genet Eng Biotechnol ; 20(1): 2, 2022 Jan 03.
Article in English | MEDLINE | ID: mdl-34978643

ABSTRACT

BACKGROUND: Lignin is a complex polymer of phenyl propanoid units found in the vascular tissues of the plants as one of lignocellulose materials. Many bacteria secrete enzymes to lyse lignin, which can be essential to ease the production of bioethanol. Current research focused on the study of ligninolytic bacteria capable of producing lignin peroxidase (LiP) which can help in lignin biodegradation and bioethanol production. Ligninolytic bacterial strains were isolated and screened from the soil samples of Simlipal Biosphere Reserve (SBR), Odisha (India), for the determination of their LiP activity. Enzymatic assay and optimization for the LiP activity were performed with the most potent bacterial strain. The strain was identified by morphological, biochemical, and molecular methods. RESULTS: In this study, a total of 16 bacteria (Simlipal ligninolytic bacteria [SLB] 1-16) were isolated from forest soils of SBR using minimal salt medium containing lignin. Out of the 16 isolates, 9 isolates showed decolourization of methylene blue dye on LB agar plates. The bacterial isolates such as SLB8, SLB9, and SLB10 were able to decolourize lignin with 15.51%, 16.80%, and 33.02%, respectively. Further enzyme assay was performed using H2O2 as substrate and methylene blue as an indicator for these three bacterial strains in lignin containing minimal salt medium where the isolate SLB10 showed the highest LiP activity (31.711 U/mg). The most potent strain, SLB10, was optimized for enhanced LiP enzyme activity using response surface methodology. In the optimized condition of pH 10.5, temperature 30 °C, H2O2 concentration 0.115 mM, and time 42 h, SLB10 showed a maximum LiP activity of 55.947 U/mg with an increase of 1.76 times from un-optimized condition. Further chemical optimization was performed, and maximum LiP activity as well as significant dye-decolourization efficiency of SLB10 has been found in bacterial growth medium supplemented individually with cellulose, yeast extract, and MnSO4. Most notably, yeast extract and MnSO4-supplemented bacterial culture medium were shown to have even higher percentage of dye decolourization compared to normal basal medium. The bacterial strain SLB10 was identified as Bacillus mycoides according to morphological, biochemical, and molecular (16S rRNA sequencing) characterization and phylogenetic tree analysis. CONCLUSION: Result from the present study revealed the potential of Bacillus mycoides bacterium isolated from the forest soil of SBR in producing LiP enzyme that can be evaluated further for application in lignin biodegradation and bioethanol production. Scaling up of LiP production from this potent bacterial strain could be useful in different industrial applications.

13.
J Biomol Struct Dyn ; 40(20): 10239-10249, 2022.
Article in English | MEDLINE | ID: mdl-34182880

ABSTRACT

In December 2019, COVID-19 epidemic was reported in Wuhan, China, and subsequently the infection has spread all over the world and became pandemic. The death toll associated with the pandemic is increasing day by day in a high rate. Herein, an effort has been made to identify the potentiality of commercially available drugs and also their probable derivatives for creation of better opportunity to make more powerful drugs against coronavirus. This study involves the in-silico interactions of dexamethasone and its derivatives against the multiple proteins of SARS-CoV-2 with the help of various computational methods. Descriptor parameters revealed their non-toxic effect in the human body. Ultimately docking studies and molecular dynamic simulation on those target protein by dexamethasone and its derivatives showed a high binding energy. Dexamethasone showed -9.8 kcal/mol and its derivative D5 showed -12.1 kcal/mol binding energy. Those scores indicate that dexamethasone has more therapeutic effect on SARS CoV-2 than other currently used drugs. Derivatives give the clue for the synthesis of a novel drug to remove SARS CoV-2. Until then, dexamethasone will be used as a potential inhibitor of SARS CoV-2.Communicated by Ramaswamy H. Sarma.


Subject(s)
COVID-19 , Humans , SARS-CoV-2 , Molecular Dynamics Simulation , Dexamethasone/pharmacology , Molecular Docking Simulation , Protease Inhibitors
14.
Article in English | MEDLINE | ID: mdl-34870149

ABSTRACT

The rapid spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) - coronavirus disease 2019 (COVID-19) has raised a severe global public health issue and creates a pandemic situation. The present work aims to study the molecular -docking and dynamic of three pertinent medicinal plants i.e. Eurycoma harmandiana, Sophora flavescens and Andrographis paniculata phyto-compounds against SARS-COV-2 papain-like protease (PLpro) and main protease (Mpro)/3-chymotrypsin-like protease (3CLpro). The interaction of protein targets and ligands was performed through AutoDock-Vina visualized using PyMOL and BIOVIA-Discovery Studio 2020. Molecular docking with canthin-6-one 9-O-beta-glucopyranoside showed highest binding affinity and less binding energy with both PLpro and Mpro/3CLpro proteases and was subjected to molecular dynamic (MD) simulations for a period of 100ns. Stability of the protein-ligand complexes was evaluated by different analyses. The binding free energy calculated using MM-PBSA and the results showed that the molecule must have stable interactions with the protein binding site. ADMET analysis of the compounds suggested that it is having drug-like properties like high gastrointestinal (GI) absorption, no blood-brain barrier permeability and high lipophilicity. The outcome revealed that canthin-6-one 9-O-beta-glucopyranoside can be used as a potential natural drug against COVID-19 protease.

15.
Chemosphere ; 282: 131135, 2021 Nov.
Article in English | MEDLINE | ID: mdl-34470171

ABSTRACT

Hexavalent chromium is a highly toxic element generated due to indiscriminate chromite mining in Sukinda, Odisha. In the present research investigation a relatively higher Cr(VI) resistant (900 mg L-1) bacterium CWB-54 was isolated from the chromite mine water. Based on the biochemical and molecular analysis the strain (CWB-54) was identified as Exiguobacterium mexicanum. When this bacterium was grown at 35 °C, 100 rpm, pH~8.0, and fructose as an electron donor, it could reduce the total hexavalent chromium (100 mg L-1) supplemented in the medium within 33 h of incubation period. Though experiment was carried out to study the effect of Mn, Ni, Cd, Hg and Zn on Cr(VI) reduction by the strain E. mexicanum it has been observed that in the presence of Cd and Hg, Cr(VI) reduction drastically decreased. Characterization of Cr(VI) reduced product by SEM-EDX and TEM analysis revealed intracellular and extracellular Cr(III) deposition in the bacterium, which is assumed to be Cr(OH)3 precipitate in nanometric size. But the extracellular chromate reductase enzyme production is found to be negligible as compared to the intracellular enzyme production. The increased concentration of Cr(VI) above (1000 mg L-1) also showed the genotoxic effect on the DNA. Several reports have been published on Exiguobacterium sp. on different scientific aspect but the current report on the reduction of toxic Cr(VI) by a new species E. mexicanum is a novel one which established the potentiality of this microorganism for a broad area of application.


Subject(s)
Exiguobacterium , Soil , Biodegradation, Environmental , Chromium , Oxidation-Reduction
16.
Bioresour Technol ; 340: 125710, 2021 Nov.
Article in English | MEDLINE | ID: mdl-34365301

ABSTRACT

The inherent resistance of lignocellulosic biomass makes it impervious for industrially important enzymes such as cellulases to hydrolyze cellulose. Further, the competitive absorption behavior of lignin and hemicellulose for cellulases, due to their electron-rich surfaces augments the inappropriate utilization of these enzymes. Hence, modification of the surface charge of the cellulases to reduce its non-specific binding to lignin and enhance its affinity for cellulose is an urgent necessity. Further, maintaining the stability of cellulases by the preservation of their secondary structures using immobilization techniques will also play an integral role in its industrial production. In silico approaches for increasing the catalytic activity of cellulase enzymes is also significant along with a range of substrate specificity. In addition, enhanced productivity of cellulases by tailoring the related genes through the process of genetic engineering and higher cellulase recovery after saccharification seems to be promising areas for efficient and large-scale enzyme production concepts.


Subject(s)
Cellulase , Cellulases , Cellulases/genetics , Genetic Engineering , Hydrolysis , Lignin
17.
Biotechnol Prog ; 37(1): e3078, 2021 01.
Article in English | MEDLINE | ID: mdl-32902193

ABSTRACT

Recently, a corona virus disease (COVID-19) caused by a novel corona virus (sevier acute respiratory syndrome corona virus 2; SARS-CoV-2), rapidly spread throughout the world. It has been resulted an unprecedented public health crisis and has become a global threat. WHO declared it as a pandemic due to rapid transmission and severity of the disease. According to WHO, as of 22nd of August 2020, the disease spread over 213 countries of the world having 22,812,491 confirmed cases and 795,132 deaths recorded worldwide. In the absence of suitable antiviral drugs and vaccines, the current pandemic has created an urgent need for accurate diagnostic tools that would be helpful for early detection of the patients. Many tests including classical and high-throughput techniques have developed and obtained U.S. Food and drug administration (FDA) approval. However, efforts are being made to develop new diagnostic tools for detection of the disease. Several molecular diagnostic tests such as real-time-polymerase chain reaction, real-time isothermal loop-mediated amplification (RT-LAMP), full genome analysis by next-generation sequencing, clustered regularly interspaced short palindromic repeats technique and microarray-based assays along with other techniques such as computed tomography scan, biomarkers, biosensor, nanotechnology, serological test, enzyme-linked immunosorbent assay (ELISA), isolation of viral strain in cell culture are currently available for diagnosis of COVID-19 infection. This review provides a brief overview of promising high-throughput techniques currently used for detection of SARS-CoV-2, along with their scope and limitations that may be used for effective control of the disease.


Subject(s)
COVID-19 Testing/methods , COVID-19/diagnosis , Enzyme-Linked Immunosorbent Assay/methods , Molecular Diagnostic Techniques/methods , SARS-CoV-2/isolation & purification , COVID-19/epidemiology , COVID-19/virology , Humans , Pandemics , Sensitivity and Specificity
18.
Curr Pharm Biotechnol ; 22(9): 1164-1191, 2021.
Article in English | MEDLINE | ID: mdl-33032507

ABSTRACT

BACKGROUND: Nowadays, medicines derived from natural sources have drawn much attention as potential therapeutic agents in the suppression and treatment of cancer because of their low toxicity and fewer side effects. OBJECTIVE: The present review aims to assess the currently available knowledge on the ethnomedicinal uses and pharmacological activities of bioactive compounds obtained from medicinal mushrooms towards cancer treatment. METHODS: A literature search has been conducted for the collection of research papers from universally accepted scientific databases. These research papers and published book chapters were scrutinized to retrieve information on ethnomedicinal uses of mushrooms, different factors involved in cancer cell proliferation, clinical and in silico pharmaceutical studies made for possible treatments of cancer using mushroom derived compounds. Overall, 241 articles were retrieved and reviewed from the year 1970 to 2020, out of which 98 relevant articles were finally considered for the preparation of this review. RESULTS: This review presents an update on the natural bioactive substances derived from medicinal mushrooms and their role in inhibiting the factors responsible for cancer cell proliferation. Along with it, the present review also provides information on the ethnomedicinal uses, solvents used for extraction of anti-cancer metabolites, clinical trials, and in silico studies that were undertaken towards anticancer drug development from medicinal mushrooms. CONCLUSION: The present review provides extensive knowledge on various anti-cancer substances obtained from medicinal mushrooms, their biological actions, and in silico drug designing approaches, which could form a basis for the development of natural anti-cancer therapeutics.


Subject(s)
Agaricales/chemistry , Biological Products/therapeutic use , Neoplasms/drug therapy , Agaricales/metabolism , Antineoplastic Agents/chemistry , Antineoplastic Agents/isolation & purification , Antineoplastic Agents/pharmacology , Antineoplastic Agents/therapeutic use , Biological Products/chemistry , Biological Products/pharmacology , Cell Cycle Checkpoints/drug effects , Cell Survival/drug effects , Fungal Polysaccharides/chemistry , Fungal Polysaccharides/isolation & purification , Fungal Polysaccharides/pharmacology , Fungal Polysaccharides/therapeutic use , Humans , Medicine, Traditional , Terpenes/chemistry , Terpenes/isolation & purification , Terpenes/pharmacology , Terpenes/therapeutic use
19.
J Genet Eng Biotechnol ; 18(1): 81, 2020 Dec 11.
Article in English | MEDLINE | ID: mdl-33306167

ABSTRACT

BACKGROUND: Xylanase has long been recognized as a widely used industrially important enzyme. There are some bacterial species already reported to produce xylanase which have potent xylanolytic activity towards the use of this enzyme in the production of bioethanol from lignocellulosic biomass. In this view, an efficient xylanolytic bacterial strain was isolated and screened from the soil sample of Simlipal Biosphere Reserve. Enzymatic assay for the xylanase activity was evidenced from the most potent bacterial strain, and the culture condition was optimized for obtaining the maximum enzyme activity. The most potent xylanolytic strain was also identified using biochemical and molecular methods. RESULTS: Nineteen xylanolytic bacteria (SXB1-SXB19) were isolated from Simlipal forest soil samples following dilution plate technique using corn cob xylan-enriched nutrient agar medium and screened for their xylanase-producing ability. Among these isolates, SXB19 showed maximum xylanolytic potential with a halozone size of 2.5 cm as evident in the formation of prominent yellow patches surrounding its growth in xylan-enriched nutrient agar plate. In unoptimized condition, SXB19 showed the highest enzymatic activity of 22.5 IU/ml among the 19 bacterial strains. In order to optimize the culture conditions for maximizing the xylanase production, Box-Behnken design of response surface methodology (RSM) was used. Four variables such as incubation time, pH, substrate (corn cob xylan) concentration, and temperature were considered for the RSM optimization study. From the results, it is evident that in an optimized condition of incubation time 36 h, pH 6.0, xylan concentration 0.5%, and temperature 42.5 °C, the enzyme activity reached a maximum of 152 IU/ml with nearly 6.75 times increase from the unoptimised condition. Besides, xylanase production from SXB19 was considerable in the presence of xylan followed by starch, nitrogen source such as urea followed by yeast extract, and mineral ion sources such as KCl followed by MgSO4 and ZnSO4. From different biochemical tests, 16S rRNA gene sequencing, and phylogenetic analysis, the bacterial strain SXB19 was identified as Pseudomonas mohnii. CONCLUSION: The isolation of Pseudomonas mohnii, a potent xylanolytic bacterium from Simlipal, is a new report which opens up an opportunity for industrial production of xylanase for bioethanol production and other applications.

20.
Front Nutr ; 7: 117, 2020.
Article in English | MEDLINE | ID: mdl-32850938

ABSTRACT

Both pectin and pectinase are vitally imperative biomolecules in the biotechnological sector. These molecules are a feasible non-toxic contrivance of nature with extensive applicative perception. Understanding pectic substances and their structure, unique depolymerization, and biochemical properties such as a catalytic mechanism and the strong interrelationship among these molecules could immensely enhance their applicability in industries. For instance, gaining knowledge with respect to the versatile molecular heterogeneity of the compounds could be considered as the center of concern to resolve the industrial issues from multiple aspects. In the present review, an effort has been made to orchestrate the fundamental information related to structure, depolymerization characteristics, and classification of pectin as well as the types and biochemical properties of pectinase. Furthermore, various production methods related to the optimization of the product and its significant contribution to the pharmaceutical industry (either pectinase or derived pectic substances) are described in this article.

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