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<p>This study focuses on the isolation, processing, and development of a protease from ginger rhizomes (<i>Zingiber officinale</i>). The protease was extracted using centrifugation, ammonium sulfate precipitation, and dialysis, followed by freeze-drying and incorporation into a wheat bran carrier. Proteolytic activity was qualitatively confirmed using a skim milk agar plate assay and quantitatively assessed by measuring tyrosine release from a caseinate substrate under controlled pH and temperature conditions. The enzyme’s activity was optimal at pH 4–8 and temperatures between 40&#xa0;°C and 70&#xa0;°C, demonstrating stability across a broad range of conditions. Protein concentration in the extract was determined using the Bradford assay, with Bovine Serum Albumin (BSA) as a standard. The protease exhibited significant hydrolytic activity, indicating its potential to enhance protein digestion. Furthermore, this enzyme maintained efficacy under conditions that simulate the avian digestive environment. These findings highlight the feasibility of utilizing ginger-derived proteases as sustainable and effective additives in animal feed, contributing to improved nutrient utilization and digestion. The study underscores the need for further exploration into optimizing extraction processes and industrial-scale production for broader applications.</p>

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Isolation, characterization, and development of phyto-protease from ginger (Zingiber officinale) rhizome

  • 期刊论文

  • 发表日期：

    2026年3月30日

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  • Muhammad Shahkar Uzair,
  • Asad Sultan,
  • Shabana Naz,
  • Rifat Ullah Khan,
  • Vincenzo Tufarelli,
  • Ibrahim A. Alhidary

摘要

This study focuses on the isolation, processing, and development of a protease from ginger rhizomes (Zingiber officinale). The protease was extracted using centrifugation, ammonium sulfate precipitation, and dialysis, followed by freeze-drying and incorporation into a wheat bran carrier. Proteolytic activity was qualitatively confirmed using a skim milk agar plate assay and quantitatively assessed by measuring tyrosine release from a caseinate substrate under controlled pH and temperature conditions. The enzyme’s activity was optimal at pH 4–8 and temperatures between 40 °C and 70 °C, demonstrating stability across a broad range of conditions. Protein concentration in the extract was determined using the Bradford assay, with Bovine Serum Albumin (BSA) as a standard. The protease exhibited significant hydrolytic activity, indicating its potential to enhance protein digestion. Furthermore, this enzyme maintained efficacy under conditions that simulate the avian digestive environment. These findings highlight the feasibility of utilizing ginger-derived proteases as sustainable and effective additives in animal feed, contributing to improved nutrient utilization and digestion. The study underscores the need for further exploration into optimizing extraction processes and industrial-scale production for broader applications.