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In this study, in silico SARS-CoV-2 inhibitory potential of 19 marine algal polycyclic aromatic compounds plus three commercial anti-viral drug were validated comparatively against three target proteins. Among 19 marine algal compounds apigenin-7-O-neohesperidoside,dieckol, luteolin-7-rutinoside, oxoglyantrypine, hydroxypentafuhalol A, and pseudopentafuhalol B exhibited good binding affinity of toward all three screened targets (Mpro, RdRp, and spike protein) of SARS-CoV-2 shortlisted for further In silico virtual screening analysis. Complete docking interaction analysis indicates that apigenin-7-O-neohesperidoside, dieckol, luteolin-7-rutinoside compounds display very excellent binding and inhibitory potential against the all three screened targets of SAR-CoV-2 among 19 screened marine algal compounds than standard anti-viral drugs. DFT analysis affirms the essential Homo-Lumo orbital energies of apigenin-7-O-neohesperidoside to inhibit targets of SARS-CoV-2. Further in silico analysis confirmed three chosen marine algal compounds are showing their excellent pharmacokinetic and molecular electrostatic potentials (MEPs) toward targets of SARS-CoV-2. MD simulation analysis of three chosen marine algal compounds possesses best simulation trajectories toward the binding pocket of target proteins essential to inhibit SARS-CoV-2 multiplication comparatively standard anti-viral drugs possess lesser binding affinity. However, further human clinical trials are necessary to justify their clinical pertinence. [ABSTRACT FROM AUTHOR]

Background: An eco-friendly treatment of industrial effluents is a major environmental concern of the modern world in the face of stringent environmental legislations. By keeping in mind the extensive industrial applications of ligninolytic enzymes, this study was performed to purify, and immobilize the manganese peroxidase (MnP) produced from an indigenous strain of Ganoderma lucidum. The present study was also focused on investigating the capability of immobilized MnP for decolorization of dye containing textile effluents. Results: A large magnitude of an indigenous MnP (882±13.3 U/mL) was obtained from white rot fungal strain G. lucidum in solid state bio-processing of wheat straw under optimized fermentation conditions (moisture, 50%; substrate, 5 g; pH, 5.5; temperature, 30°C; carbon source, 2% fructose; nitrogen source, 0.02% yeast extract; C: N ratio, 25:1; fungal spore suspension, 5 mL and fermentation time period, 4 days). After ammonium sulfate fractionation and Sephadex-G-100 gel filtration chromatography, MnP was 4.7-fold purified with specific activity of 892.9 U/mg. G. lucidum MnP was monomeric protein as evident by single band corresponding to 48 kDa on native and denaturing SDS-PAGE. The purified MnP (2 mg/mL) was immobilized using a sol-gel matrix of tetramethoxysilane (TMOS) and proplytrimethoxysilane (PTMS). The oxidation of MnSO4 for up to 10 uninterrupted cycles demonstrated the stability and reusability of the immobilized MnP. Shelf life profile revealed that enzyme may be stored for up to 60 days at 25°C without losing much of its activity. To explore the industrial applicability of MnP produced by G. lucidum, the immobilized MnP was tested against different textile effluents. After 4 h reaction time, the industrial effluents were decolorized to different extents (with a maximum of 99.2%). The maximally decolorized effluent was analyzed for formaldehyde and nitroamines and results showed that the toxicity parameters were below the permissible limits. Conclusions: In conclusion, G. lucidum MnP was immobilized by sol-gel matrix entrapment with an objective to enhance its practical efficiencies. The MnP was successfully entrapped into a sol- gel matrix of TMOS and PTMS with an overall immobilization efficiency of 93.7%. The sol- gel entrapped MnP seems to have prospective capabilities which can be useful for industrial purposes, especially for bioremediation of industrial effluents. [ABSTRACT FROM AUTHOR]

Ziziphus jujuba plant belongs to Rhamnaceous family and grows mainly in Europe, southern and eastern Asia, and Australia. Recent phytochemical investigation of plants provided some information on their biological effects, such as the hepatoprotective, immunostimulating, anti-obesity, anti-inflammatory, and anti-cancer properties. The current study investigated 34 phytocompounds from Z. jujuba and three anti-cancer drugs against three lung cancer target proteins. Drug likeliness screening revealed that two compounds dodecanoic acid and 7,9-di-tert-butyl-1-oxaspiro[4,5]deca-6,9-diene-2,8-dione possess zero violation, and compound azelaic acid possesses single violation against five drug rules. Molecular docking study reveals that 34 phytocompounds from Z. jujuba and three anti-cancer drugs showed docking score values in the range of −3.9 to −10.2 kcal/mol and −7.2 to −9.0 kcal/mol against three significant lung cancer target proteins. Furthermore, in silico screening top scored three phytocompounds campesterol, stigmast-5-en-3-ol, 7,9-di-tert-butyl-1-oxaspiro[4,5]deca-6,9-diene-2,8-dione and three anti-cancer drugs etoposide, paclitaxel, and doxorubicin utilized. Pharmacokinetic profile of three phytocompounds from Z. jujuba showed excellent absorption, distribution, metabolism, excretion, and toxicity profile than standard drugs. Furthermore, bioactivity and density functional theory analysis showed that phytocompounds from Z. jujuba possess better bioactivity scores and molecular electrostatic potentials than standard drugs. Molecular dynamics simulation results revealed that campesterol with CDK2 (PDB ID 1GII) and MDM2/P53 (4HFZ) target proteins possess better simulation trajectories and binding affinity than standard drugs. Further clinical trials of compounds (campesterol, stigmast-5-en-3-ol, 7,9-di-tert-butyl-1-oxaspiro[4,5]deca-6,9-diene-2,8-dione) are needed to check clinical pertinence toward lung cancer target proteins to commercialize these novel drug molecule in the drug industry. [ABSTRACT FROM AUTHOR]

The present study is to identify polycyclic aromatic bioactive phytocompounds from Eclipta alba against breast cancer target protein through in silico approach. Among 52 phytocompounds ecliptalbine, wedelolactone, ursolic acid and beta amyrin they have exhibited strong binding affinity against all three screened breast cancer target proteins such as matrix metallo protein (PDB ID 1RM8), estrogen receptor (PDB ID 3ERT) and progesterone receptor (PDB ID 4OAR). In drug likeliness 11 phytocompounds showed zero violations against all five drug likeliness rule, whereas all three anticancer drugs showed three minimal violations against the drug likeliness rule. Docking score of all screened compounds lies in the range of −4.3 Kcal/mol to −9.4 Kcal/mol in that ecliptalbine and ursolic acid show maximal binding affinity with all screened target proteins of breast cancer. Phytocompound ecliptalbine, wedelolactone and ursolic acid has shown excellent simulation trajectories with two screened target proteins in MDS analysis. Further compound ecliptalbine shown good phracokinetic and DFT scores which affirm that reason behind the good binding affinity with breast cancer target proteins. MMGBSA analysis also affirms the excellent binding affinity of ecliptalbine with breast cancer target proteins (–51.42 and −72.74 Kcal/mol) than the standard drug score. Finally ethanolic leaf extract of Eclipta alba showed excellent In vitro antioxidant (DPPH-IC50 83.40 µg/ml and ABTS–IC50 48.80 µg/ml) and cytotoxic potential (IC50 97.20 µg/ml) against triple-negative breast cancer cells (MDA-MB-231). Further these drug candidates can be validated through in vitro and preclinical studies to discover novel drug for breast cancer therapeutics. [ABSTRACT FROM AUTHOR]

In the present study, in silico PLpro inhibitory potential of 28 polyphenolic compounds was validated, which possesses in vivo inhibitory potential against different SARS-CoV-2 replication enzymes. Among 28 polyphenolic compounds amentoflavone, tiliroside, papyriflavanol A and indinavir exhibited good binding affinity of toward PLpro has been considered for further virtual screening processes. Comprehensive analysis indicates that amentoflavone, tiliroside, and papyriflavanol A phenolic compounds demonstrate very high stability and higher inhibiting potential to bind with the Thr158 and Leu162 dyad of PLpro among 28 phenolic compounds. Further ADME and DFT analysis of amentoflavone, and papyrifalvanol A reveal that possess excellent pharmacokinetic and molecular electrostatic potentials. MD simulation and MM-GBSA analysis of amentoflavone, tiliroside, and one anti-viral drug indinavir toward PLpro (PDB ID 6W9C) result revealed that phenolic compounds amentoflavone, tiliroside possess excellent simulation trajectories toward the binding pocket of PLpro essential to inhibit SARS-CoV-2 multiplication. Further MM-GBSA analysis affirm that PLpro-amentoflavone complex exhibit high MMGBSA score of −106.56Kcal/mol. However, further human clinical trials are essential to justify their clinical pertinence. [ABSTRACT FROM AUTHOR]

Trametes versicolor IBL-04 was used for biodegradation of Remazol Brilliant Yellow 3-GL (RBY3-GL) reactive textile dye in Kirk's basal salts medium. During the initial screening study, the maximum decolorization (93.5%) of RBY3-GL was achieved in 7 days' shaking incubation period at pH 4 and 30 °C. Different physical and nutritional factors were statistically optimized to enhance the efficiency of T. versicolor IBL-04 for maximum decolorization. Under optimal conditions T. versicolor IBL-04 completely decolorized (100%) the RBY3-GL in 2 days of incubation with negligible adsorption on fungal mycelia. Laccase was the major enzyme (938.3 U/mL) secreted by T. versicolor IBL-04 along with comparatively lower activities of MnP. In this article and for the first time, a statistical correlation has been successfully investigated between the ligninolytic enzymes from an indigenously isolated white rot fungi, T. versicolor IBL-04, and the degradation of RBY3-GL. [ABSTRACT FROM AUTHOR]

In the present study, we developed a novel ligninolytic enzymes based pre-treatment method for lignocellulosic wheat straw to depolymerize lignin and expose the cellulose polymers to produce bio-ethanol. Wheat straw was pre-treated with ligninolytic enzymes extract produced from Ganoderma lucidum under optimum solid state fermentation conditions. The pre-treated biomass was further subjected to the enzymatic hydrolysis by the crude unprocessed cellulases (β-1,4 endoglucanase, 53.5 ± 1.24 U/mL; (β-1,4 exoglucanase, 41.3 ± 1.31 U/mL; (β-1,4 glucosidase, 46.8 ± 1.43 U/mL; and xylanase 39 ± 2.2 U/mL) produced by Trichoderma harzaianum. Under optimal conditions for enzymatic saccharification, 10% (w/v) of pre-treated biomass was hydrolyzed completely and converted to 72.5 and 2.4 g/L of glucose and xylose, respectively. Initial time screening Sequential Saccharification and Fermentation (SSF) of the concentrated enzymatic hydrolyzate (10%, w/v) by Saccharomyces cereuisiae produced 22.6 g/L ethanol in a fermented medium after 72 h of temperature controlled incubation at 37 °C. For maximum ethanol production, different physical and nutritional parameters like pH, temperature, substrate level and inoculum sizes were optimized. Under optimal conditions ethanol production of 33.5 g/L was obtained from ligninolytic treated residual (wheat straw) biomass. [ABSTRACT FROM AUTHOR]

A novel manganese peroxidase (MnP) was isolated from an indigenous fungal species Schizophyllum commune strain IBL-06 that was grown in pre-optimized solid state culture using banana stalk as substrate. The MnP was purified by (NH4)2SO4 fractionation, dialysis and Sephadex G-100 gel filtration chromatography to achieve 1.8 fold purification with 22% enzyme yield and 506 U/mg specific activity. A homogenous single band of 40 kDa for purified MnP was obtained after gel documentation of Native-PAGE that was further confirmed on SDS-PAGE. Characterization of MnP revealed that the pH and temperature optima of S. commune IBL-06 MnP were 5 and 40°C, respectively. S. commune MnP showed high substrate (MnSO4) affinity and catalytic efficiency with corresponding kinetic constants Km and Vmax values of 0.4 mM and 410 mM/min, respectively. The purified enzyme was activated by CuSO4 and MnSO4 and inhibited by CaCl2, EDTA, TEMED, β- Marcaptoethanol, AgNO3 and Pb(NO3)2 (most inhibitory). [ABSTRACT FROM AUTHOR]

Background: In serious consideration of the worldwide environmental issues associated with the extensive use of the textile dyes and effluents generated thereof, the scientists across the world are in search for potential treatment technologies for their treatment. In such scenario the ligninolytic enzymes provide a potential alternative because they are cost effective, eco-friendly and can be applied to wide range of dye containing industrial effluents. Results: Laccase produced from Pleurotus ostreatus IBL-02 during decolorization of the reactive textile dye Drimarene brilliant red K-4BL (DBR K-4BL) was purified and immobilized by hydrophobic gel entrapment. The crude laccase was 4.2-fold purified with specific activity of 573.52 U/mg after passing through the DEAE-Sepharose ion exchange and Sephadex-G-100 chromatography columns. P. ostreatus IBL-02 laccase was found to be a homogenous monomeric protein as evident by single band corresponding to 67 kDa on native and sodium dodesylsulfate polyacrylamide gel electrophoresis (PAGE). The laccase was immobilized by entrapment in Sol-gel matrix of trimethoxysilane (T) and proplytetramethoxysilane (P) prepared using different T:P molar ratios. The free and immobilized laccases were compared to investigate the effect of immobilization on catalytic efficiency and thermo-stability features. Laccase immobilized in the Sol-gel of 1:5 T:P ratio was optimally active and thermo-stable fraction at pH 5, 60°C with half-life of 3 h and 50 min. Laccases immobilized in 1:2 and 1:5 T:P ratio gels had significantly higher Km (83 and100mM) and Vmax (1000 and 1111 mM/mg) values as compared to free laccase. After 5 h reaction time varying decolorization percentages with a maximum of 100% were achieved for different dyes and effluents. Conclusions: In summary, P. ostreatus IBL-02 laccase was immobilized by entrapping in a Sol-gel matrix with an objective to enhance its catalytic and stability properties. Sol-gel entrapped laccase presented potential efficiency as a biocatalyst when applied for decolorization of different dyes and effluents. The main benefits of the Sol-gel matrix immobilization processes are the eco-friendly approach, chemical free and energy saving reaction conditions. [ABSTRACT FROM AUTHOR]

A study was conducted to purify and characterize a novel protease produced from Aspergillus niger using different lignocellulosic agro-based by-products including corncobs, wheat bran, and rice bran as substrates under SSF. Maximum protease activity was recorded on wheat bran fermented culture media after the 3rd day of incubation. The optimal conditions found for protease production using wheat bran were cultivation period (3 days), substrate concentration (10 g), pH (7), incubation temperature (45°C), inoculum size (4 mL), and 3% surfactant Tween-80 (2 mL). A purification fold of 2.41 with 29 U/mg specific activity and 70.73 % recovery was achieved after purification. Purified protease from A. niger had a molecular weight of 47 kDa on SDS-PAGE. The enzyme activity profile showed that purified protease was optimally active at pH 7 and 45°C as optimum values. A. niger protease was reasonably stable in the pH range 5-8 and 35-60°C for up to 1 h incubation. Protease was activated by various metal ions/inhibitors tested, Mn2+, Cd2+, Mg2+, Cu2+, PMSF, Pepstatin and Iodoacetic acid at 1 mM, proving the enzyme as metalloprotease, whereas an inhibitory effect was shown by certain agents including EDTA and SDS. The purified protease was compatible with five local detergents with up to 25 days of shelf life at room temperature. The maximum production of protease in the presence of a cheaper substrate at low concentration and its potential as a detergent additive for improved washing makes the strain and its enzymes potentially useful for industrial purposes, especially for the detergent and laundry industry. [ABSTRACT FROM AUTHOR]