Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in Cyberlindnera jadinii CJ2
| Autor: | Silvia Donzella, Concetta Compagno, Claudia Capusoni, Immacolata Serra |
|---|---|
| Přispěvatelé: | Capusoni, C, Serra, I, Donzella, S, Compagno, C |
| Rok vydání: | 2021 |
| Předmět: |
feed additive
0106 biological sciences 0301 basic medicine Histology Feed additive Biomedical Engineering Bioengineering yeast 01 natural sciences 03 medical and health sciences chemistry.chemical_compound Kluyveromyces marxianus 010608 biotechnology Cyberlindnera jadinii Food science food production chemistry.chemical_classification Phytic acid biology biology.organism_classification phytic acid Torulaspora Yeast 030104 developmental biology Enzyme chemistry phytase Degradation (geology) Phytase TP248.13-248.65 Biotechnology |
| Zdroj: | Frontiers in Bioengineering and Biotechnology, Vol 9 (2021) |
| ISSN: | 2296-4185 |
| DOI: | 10.3389/fbioe.2021.662598 |
| Popis: | Phytic acid is an anti-nutritional compound able to chelate proteins and ions. For this reason, the food industry is looking for a convenient method which allows its degradation. Phytases are a class of enzymes that catalyze the degradation of phytic acid and are used as additives in feed-related industrial processes. Due to their industrial importance, our goal was to identify new activities that exhibit best performances in terms of tolerance to high temperature and acidic pH. As a result of an initial screening on 21 yeast species, we focused our attention on phytases found in Cyberlindnera jadinii, Kluyveromyces marxianus, and Torulaspora delbrueckeii. In particular, C. jadinii showed the highest secreted and cell-bound activity, with optimum of temperature and pH at 50°C and 4.5, respectively. These characteristics suggest that this enzyme could be successfully used for feed as well as for food-related industrial applications. |
| Databáze: | OpenAIRE |
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