<p>Alcohol dehydrogenases (ADHs) are key enzymes in microbial ethanol metabolism and ethanol detection with significant relevance in industrial bioprocessing and synthetic biology. The study focuses on enhancing the activation of <i>Magnusiomyces capitatus</i> ADHs specific to ethanol for ethanol conversion and detection. This was achieved by evaluating its specific alcohol dehydrogenase (ADH) activity under varying growth conditions by following a systematic one-factor-at-a-time (OFAT) approach and a central composite rotatable design (CCRD). Using the OFAT method, the most critical factor for improving specific ADH activity were identified as glucose, ammonium sulphate, zinc sulphate, and pH, which was further optimized using the CCRD. The specific ADH activity of <i>M. capitatus</i> in the developed medium was 489.28 ± 0.31 mU mg<sup>− 1</sup> of protein, which was greater than that of cells cultured in basal ethanol medium. Furthermore, the volatile compounds (VOCs) generated during ethanol oxidation under aerobic conditions were analyzed by GC-MS, validating the metabolic flexibility of <i>M. capitatus</i> under optimal circumstances. These findings offer new insights into the systems-level metabolic behavior of <i>M. capitatus</i> under ethanol stress and highlight its potential as a microbial platform for future biomanufacturing and enzymatic conversion processes with potential applications in biosensing and industrial bioprocessing.</p>

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Metabolic adaptation and alcohol dehydrogenase induction in Magnusiomyces capitatus through systematic bioprocess tuning

  • Dhanasekaran Subashri,
  • Kalyanasundaram Sundaragnanam,
  • Abbas Ali Abdul Rahuman,
  • Pambayan Ulagan Mahalingam

摘要

Alcohol dehydrogenases (ADHs) are key enzymes in microbial ethanol metabolism and ethanol detection with significant relevance in industrial bioprocessing and synthetic biology. The study focuses on enhancing the activation of Magnusiomyces capitatus ADHs specific to ethanol for ethanol conversion and detection. This was achieved by evaluating its specific alcohol dehydrogenase (ADH) activity under varying growth conditions by following a systematic one-factor-at-a-time (OFAT) approach and a central composite rotatable design (CCRD). Using the OFAT method, the most critical factor for improving specific ADH activity were identified as glucose, ammonium sulphate, zinc sulphate, and pH, which was further optimized using the CCRD. The specific ADH activity of M. capitatus in the developed medium was 489.28 ± 0.31 mU mg− 1 of protein, which was greater than that of cells cultured in basal ethanol medium. Furthermore, the volatile compounds (VOCs) generated during ethanol oxidation under aerobic conditions were analyzed by GC-MS, validating the metabolic flexibility of M. capitatus under optimal circumstances. These findings offer new insights into the systems-level metabolic behavior of M. capitatus under ethanol stress and highlight its potential as a microbial platform for future biomanufacturing and enzymatic conversion processes with potential applications in biosensing and industrial bioprocessing.