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Antimicrobial Insights into a Partially Purified Enzyme Protein Derived from Myrica esculenta

NEHA RAWAT, NEHA PANDEY, AKSHAY KUMAR SHARMA, RITUMBHRA RAJPUT, CHINMOYEE MAHARANA AND AMIT GUPTA
Department of Microbiology, Graphic Era (Deemed to be University), Dehradun-248 002 (Uttarakhand), India
*(e-mail: amit.gupta@jammuuniversity.ac.in; Mobile: 60055 01338)
(Received: August 19, 2025; Accepted: September 29, 2025)

ABSTRACT

Of all industrial enzymes, proteases are the most significant resource of our life. Though new proteases with better physiochemical properties for industrial usage are constantly being researched, the most widely implemented plant proteases are papain, bromelain and ficin. In this study, research was conducted for extracting and employing the required plant protease enzyme from Myrica esculenta leaves (using ammonium sulphate) and evaluating its antibacterial and anti-inflammatory properties towards a handful of pathogenic microbial strains. For this investigation, the total protein content of the collected material was assessed using the colorimetric technique (Bradford test), which was followed by polyacrylamide gel electrophoresis. The partly purified fraction of the recovered enzyme protein had a molecular weight of 31 kDa. The specific partially purified enzyme activity of dialysed M. esculenta protease was 35.20 U/ml. A variety of pH values (4.5, 7.5 and 8.5) was used to calibrate the enzyme’s efficiency for maximum activity. In this study, the partially purified enzyme protein remained actively functional at pH 4.5. Further, the antimicrobial potential was examined against gram-positive and gram-negative bacteria using the disc diffusion method, and also its anti-inflammatory activity against specific antigen. The results of antimicrobial susceptibility and anti-inflammatory activity of the partially purified enzyme protein of leaves were observed at pH 4.5 against bacterial strains and specific antigens were evaluated. This finding demonstrated that the partially purified enzyme protein of M. esculenta leaves appeared to be a viable source for the extraction of proteolytic enzymes.
Key words: Myrica esculenta, plant-derived protease, enzymatic activity, protein purification, antimicrobial activity