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Abstract <p>Proteolysis, the process by which proteins are broken down into smaller polypeptides or single amino acids, is catalyzed by enzymes known as proteases. In this study, bacteria isolated from marine sediments were screened for protease production on skim milk agar medium. Out of 8 isolates, VITSDPB8 exhibited distinct zones of hydrolysis around its colonies indicating higher protease activity. This strain was closely related to <i>Rossellomorea aquimaris</i>. The enzyme activity was optimized by varying pH, temperature, and carbon and nitrogen sources. Enhanced protease activity (277 U/mL/min) was achieved under the optimized conditions: glucose as the carbon source, skim milk as the nitrogen source, pH 9.0, and a temperature of 42°C. The protease was extracted and subsequently purified, with the molecular weight of the purified enzyme determined to be approximately 45 kDa. The efficacy of the enzyme was evaluated for various applications. When applied as a purified extract, it successfully removed blood stains within 20 min. Additionally, after 60 min of incubation, the enzyme thoroughly digested the blood clots. The enzyme extract also exhibited notable antimicrobial activity against <i>Salmonella typhi</i> and <i>Klebsiella pneumonia</i>. These findings demonstrate that <i>R. aquimaris</i> VITSDPB8 has significant potential for protease production. This enzyme is promising bioactive compound for use in the medicinal applications.</p>

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Optimization and Purification of Protease Produced by Rossellomorea aquimaris Isolated from Marine Sediments and Exploring Their Diverse Biological Applications

  • 期刊论文

  • 发表日期：

    2025年6月15日

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  • P. M. Sebastian,
  • G. Sanjana,
  • D. Mundrikeri,
  • K. V. B. Rao

摘要

Abstract

Proteolysis, the process by which proteins are broken down into smaller polypeptides or single amino acids, is catalyzed by enzymes known as proteases. In this study, bacteria isolated from marine sediments were screened for protease production on skim milk agar medium. Out of 8 isolates, VITSDPB8 exhibited distinct zones of hydrolysis around its colonies indicating higher protease activity. This strain was closely related to Rossellomorea aquimaris. The enzyme activity was optimized by varying pH, temperature, and carbon and nitrogen sources. Enhanced protease activity (277 U/mL/min) was achieved under the optimized conditions: glucose as the carbon source, skim milk as the nitrogen source, pH 9.0, and a temperature of 42°C. The protease was extracted and subsequently purified, with the molecular weight of the purified enzyme determined to be approximately 45 kDa. The efficacy of the enzyme was evaluated for various applications. When applied as a purified extract, it successfully removed blood stains within 20 min. Additionally, after 60 min of incubation, the enzyme thoroughly digested the blood clots. The enzyme extract also exhibited notable antimicrobial activity against Salmonella typhi and Klebsiella pneumonia. These findings demonstrate that R. aquimaris VITSDPB8 has significant potential for protease production. This enzyme is promising bioactive compound for use in the medicinal applications.