Search

Your search keyword '"P. Bhattacharjee"' showing total 73 results
Start Over "P. Bhattacharjee" Journal archives of microbiology
73 results on '"P. Bhattacharjee"'

8. An up-to-date review of biomedical applications of serratiopeptidase and its biobetter derivatives as a multi-potential metalloprotease.

Author

Hosseini SB, Azizi M, Nojoumi SA, and Valizadeh V

Subjects
Humans, Anti-Inflammatory Agents, Pain drug therapy, Peptide Hydrolases metabolism, Metalloproteases chemistry
Abstract

Serratiopeptidase is a bacterial metalloprotease used in a variety of medical applications. The multidimensional properties of serratiopeptidase make it noticeable as a miraculous enzyme. Anti-coagulant, anti-inflammatory and anti-biofilm activity of serratiopeptidase making it useful in reducing pain and swelling associated with various conditions including arthritis, diabetes, cancer, swelling, pain and also thrombolytic disorders. It breaks down fibrin, thins the fluids formed during inflammation and due to its anti-biofilm activity, can be used in the combination of antibiotics to reduce development of antibiotic resistance. However, some drawbacks like sensitivity to environmental conditions and low penetration into cells due to its large size have limited its usage as a potent pharmaceutical agent. To overcome such limitations, improved versions of the enzyme were introduced using protein engineering in our previous studies. Novel functional serratiopeptidases with shorter length and higher stability have seemingly created a hope for using this enzyme as a more effective therapeutic enzyme. This review explains the structural properties and functional aspects of serratiopeptidase, its main characteristics and properties, pre-clinical and clinical applications of the enzyme, improved qualities of the modified forms, different formulations of the enzyme, and the potential future developments., (© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)

Published
2024
Full Text
View/download PDF

9. GC–MS analysis and molecular docking of bioactive compounds of Camellia sinensis and Camellia assamica.

Author

Pradhan, Surbhi and Dubey, R. C.

Subjects
TEA, MOLECULAR docking, BIOACTIVE compounds, THIN layer chromatography, SIGNAL recognition particle receptor
Abstract

The methanol extract of Camellia sinensis (MES) and acetone extract of Camellia assamica (AEA) were subjected to the thin layer chromatography to separate the bioactive compounds. The antimicrobial activity of all the fractions was carried out against pathogenic microorganisms by the agar-well diffusion method. The most effective bioactive fraction of each plant species was analysed by GC–MS. Fraction L of methanol extract of C. sinensis (MES) and fraction 5 of acetone extract of C. assamica (AEA) were found very effective against selected pathogenic strains. GC–MS analysis of this fraction showed the presence of n-heptadecanol-1 (68.63%) in MES and 2′,6′dihydroxyacetophenone, bis(trimethylsilyl) (17.58%) in AEA with the highest area. The compounds n-heptadecanol-1 and 2′,6′dihydroxyacetophenone, bis(trimethylsilyl) ether were used for docking to analyse its therapeutic potential. The ligand compound n-heptadecanol-1 (HEP) from MES of C. sinensis and 2′,6′dihydroxyacetophenone, bis(trimethylsilyl) ether from AEA of C. assamica were docked with the target protein dihydropteoate synthase (DHPS) active sites of Escherichia coli and Staphylococcus aureus active sites via Auto Dock Vina, thereby forecasting the finest binding position of ligands. AutoDock Vina docked results revealed the involvement of binding energy for the establishment of the protein–ligand structure complex, besides generating an interpretation of all apparent molecular interactions accountable for its activity. Further, the protein–ligand complex of MES, EcDHPS + HEP and SaDHPS + HEP exhibiting the best binding affinity were − 4.8 kcal/mol and − 3.6 kcal/mol. The protein–ligand complex of AEA, i.e., EcDHPS + DHA and SaDHPS + DHA exhibited the best binding affinity of − 4.8 kcal/mol and − 4.8 kcal/mol. [ABSTRACT FROM AUTHOR]

Published
2021
Full Text
View/download PDF

10. The dsRNA mycovirus ChNRV1 causes mild hypervirulence in the fungal phytopathogen Colletotrichum higginsianum.

Author

Olivé, Marta and Campo, Sonia

Subjects
FUNGAL viruses, COLLETOTRICHUM, DOUBLE-stranded RNA, TROPICAL fruit, PHYTOPATHOGENIC fungi, FILAMENTOUS fungi
Abstract

The genus Colletotrichum comprises a large number of filamentous fungi responsible for anthracnose diseases in many tropical and subtropical fruits and vegetables. In particular, Colletotrichum higginsianum infects Brassicaceae species, including Arabidopsis. The C. higginsianum strain IMI349063A is naturally infected with a dsRNA virus, named Colletorichum higginsianum non-segmented virus (ChNRV1). Here, we investigated the biological effect of ChNRV1 in C. higginsianum by comparing strains with and without the virus. ChNRV1 does not have an effect on C. higginsianum growth under salt and cell-wall stress conditions. However, thermal stress reduced C. higginsianum growth rate, this effect being more evident in the wild-type C. higginsianum strain containing the virus. Although ChNRV1 had no effect in conidiation, conidia were narrower when the virus is present. More importantly, ChNRV1 causes a mild increase in C. higginsianum virulence (hypervirulence) when infecting Arabidopsis plants. These findings indicated that, whereas the ChNRV1 mycovirus does not impair growth and conidiation of C. higginsianum, it confers hypervirulence to the fungal host. These findings will help in future research on the effect of mycoviral infection on pathogenic fungi in plant species of agronomical relevance. [ABSTRACT FROM AUTHOR]

Published
2021
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results