Publications by authors named "Natalia N Gessler"

In this study, we first thoroughly assayed the response of the key enzymes of energy metabolism and the antioxidant system in yeast at extreme pH. The activity of the tricarboxylic acid cycle enzymes, namely NAD-dependent isocitrate dehydrogenase, aconitate hydratase, NAD-dependent malate dehydrogenase, and fumarate hydratase, NADPH-producing enzymes of glucose-6-P dehydrogenase and NADP-dependent isocitrate dehydrogenase, and the enzymes of the glutathione system was assessed. All the enzymes that were tested showed a significant induction contrary to some decrease in the aconitate hydratase activity with acidic and alkaline stress.

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In this study, we used the Manchurian golden breed of quails. We assessed the efficacy of the food additives of the phytase from encapsulated in the recombinant yeast, which was supplied at a concentration of 500 phytase activity units per kg of the feed. One hundred fifty one-day-old quails were distributed into six treatment groups.

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The review describes the advances in the phytase immobilization for the past decade and their biotechnological applications. Different approaches for phytase immobilization are described including the process using organic and inorganic matrices and microbial cells, as well as nanostructures of various nature. Moreover, the immobilization of phytase-producing microbial cells and the use of cross-linked phytase aggregates have been under consideration.

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In the ascomycete fungus Neurospora crassa blue-violet light controls the expression of genes responsible for differentiation of reproductive structures, synthesis of secondary metabolites, and the circadian oscillator activity. A major photoreceptor in Neurospora cells is WCC, a heterodimeric complex formed by the PAS-domain-containing polypeptides WC-1 and WC-2, the products of genes white collar-1 and white collar-2. The photosignal transduction is started by photochemical activity of an excited FAD molecule noncovalently bound by the LOV domain (a specialized variant of the PAS domain).

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