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<p>Fungal glutaminase is of great importance in different industries fields. Thus, searching for a significantly catalytic <span>l</span>-glutaminase (Glut) with appraising its biochemical properties and biotechnological applications are the main purposes of this work. The Glut from <i>Aspergillus oryzae</i> was purified with a specific activity 258.33 (U/mg of protein), 215-fold and 36.47% yield. The molecular weight of the purified enzyme was 65&#xa0;kDa. The purified enzyme exhibited remarkably improved resistance toward higher temperature in the presence of an exogenous trehalose. The enzyme had a greater affinity towards <span>l</span>-glutamine, <span>l</span>-cysteine, <span>l</span>-proline and <span>l</span>-lysine than <span>l</span>-valine, and <span>l</span>-glycine. The essentiality of arginine, tryptophan, histidine, and cysteine residues in the catalysis process of <span>l</span>-glutaminase was determined. The application of biocatalyst in the reaction mixture has not only remarkably increased <span>l</span>-theanine concentration but also has enhanced glutamic acid production in the presence of 10% compared with 15% NaCl. The deamidation of water insoluble <i>Zea</i> or rice glutelin was approximately 65% and 83% after 44&#xa0;h by the enzymatic treatment. The purified Glut displayed remarkable antitumor activities against lung (A549), liver (HepG2) and human breast (MCF-7) carcinoma. Thus, <span>l</span>-Glut from <i>A. oryzae</i> has the potential to be used in food application and in treatment of various cancer cells.</p>

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Purification and biochemical characterization of l-glutaminase from Aspergillus oryzae with potential biotechnological applications in synthesis of l-theanine and as antitumor agent

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  • 发表日期：

    2025年10月21日

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  • Hamed M. El-Shora,
  • Sally M. Metwally,
  • Nahla T. Elazab,
  • Widad M. Al-Bishri,
  • Gharieb S. El-Sayyad,
  • Reyad M. El-Sharkawy

摘要

Fungal glutaminase is of great importance in different industries fields. Thus, searching for a significantly catalytic l-glutaminase (Glut) with appraising its biochemical properties and biotechnological applications are the main purposes of this work. The Glut from Aspergillus oryzae was purified with a specific activity 258.33 (U/mg of protein), 215-fold and 36.47% yield. The molecular weight of the purified enzyme was 65 kDa. The purified enzyme exhibited remarkably improved resistance toward higher temperature in the presence of an exogenous trehalose. The enzyme had a greater affinity towards l-glutamine, l-cysteine, l-proline and l-lysine than l-valine, and l-glycine. The essentiality of arginine, tryptophan, histidine, and cysteine residues in the catalysis process of l-glutaminase was determined. The application of biocatalyst in the reaction mixture has not only remarkably increased l-theanine concentration but also has enhanced glutamic acid production in the presence of 10% compared with 15% NaCl. The deamidation of water insoluble Zea or rice glutelin was approximately 65% and 83% after 44 h by the enzymatic treatment. The purified Glut displayed remarkable antitumor activities against lung (A549), liver (HepG2) and human breast (MCF-7) carcinoma. Thus, l-Glut from A. oryzae has the potential to be used in food application and in treatment of various cancer cells.