Cihan University-Erbil Conferences, 4th International Conference on Biological & Health Sciences (CIC-BIOHS’2022)

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In-Vitro Screening of Clostridium Histolyticum Collagenase and Bacillus Polymyxa Metalloprotease Inhibitory Activities in Ninety-Five Medicinal Plant Extracts
Bhimrao V Jaiwal, Ajit B. Patil, Sarwan W. Bradosty, Faiyaz Khudaboddin Shaikh, Manohar V. Padul

Last modified: 2022-08-30

Abstract


Medicinal plants and their different constituents are utilized as therapeutic agents. In present work we report the total phenolics content and screening of ninety five plant extracts for inhibitory activities against Clostridium histolyticum collagenase (ChC) and Bacillus polymyxa metalloprotease (BpM). Total phenolics content from plant methanolic extracts were assessed by using Folin-Ciocalteau assay. Screening of plant extracts for ChC and BpM inhibitory activities was performed by using dot blot assay on X-ray film. G. superba fruit was observed to have the highest phenolics (257.58 ± 0.75 mg GAE /g tissue) content while C. nurvala stem was observed to have the lowest phenolics (0.468 ± 0.003 mg GAE /g tissue) content. Thirty two plants showed ChC inhibitory activities while twenty seven plants showed BpM inhibitory activities. From those plants twenty five plants have common ChC and BpM inhibitory activities. The most of plant Barks were found to have high amount of total phenolics as compared to other plant tissue while the most of plant leaves were found to have low amount of total phenolics. The most of barks were found to exhibit inhibitory activities as compared to other tissue. Only 6 different leaves were found to exhibit inhibitory activity out of 42 different leaves. None of the root extracts exhibited inhibitory activities. In conclusion, the bacterial metalloprotease inhibitory activities of these plant extracts could be explored as significant source for determination of novel drug against human MMPs relevant disorders.

Key Words: Total phenolics, Clostridium histolyticum collagenase, Bacillus polymyxa metalloprotease, G. superba, S. cumini, T. arjuna

 

DOI: http://doi.org/10.24086/biohs2022/paper.727


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