Enhanced acido-thermophilic invertase production via a derepressed mutant of Pichia kudriavzevii in batch cultures

Invertase, a crucial enzyme involved in sucrose hydrolysis, finds extensive applications in various industrial processes, including food and biofuel production. This study focuses on the optimization of acido-thermophilic invertase production using a derepressed mutant strain of Pichia kudriavzevii in batch cultures. The development of an efficient and cost-effective process for invertase production is essential to meet the increasing demands of industrial applications. Notably, the maximum specific invertase production rate (qP) reached 247.3 IU/g cells h, with an invertase yield (YP/S) of 150 IU/g substrate utilized at 40 °C. A detailed exploration of temperature-dependent specific growth and product formation rates unveiled the organism’s thermophilic characteristics. The determined K m and V max values were significantly lower compared to those of other yeast species and a reference P. kudriavzevii strain. The enzyme exhibited both acidophilic and thermophilic properties at optimized pH (3.0–5.0) and temperature (50 °C), respectively. Based on kinetic and thermodynamic attributes, the invertase derived from the mutant demonstrated comparability to acido-thermophilic enzymes previously documented in the literature. The study provides valuable insights into the genetic and environmental factors influencing acido-thermophilic invertase production in P. kudriavzevii . The application of a derepressed mutant offers a promising strategy for enhancing enzyme yields in batch cultures. This research contributes to the development of sustainable and economically viable processes for industrial-scale invertase production, addressing the growing demand for this enzyme in various biotechnological applications.