Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in

Cyberlindnera jadinii feed additive food production phytase phytic acid yeast

Journal

Frontiers in bioengineering and biotechnology
ISSN: 2296-4185
Titre abrégé: Front Bioeng Biotechnol
Pays: Switzerland
ID NLM: 101632513

Informations de publication

Date de publication:
2021
Historique:
received: 01 02 2021
accepted: 29 03 2021
entrez: 10 6 2021
pubmed: 11 6 2021
medline: 11 6 2021
Statut: epublish

Résumé

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

Identifiants

pubmed: 34109165
doi: 10.3389/fbioe.2021.662598
pmc: PMC8181137
doi:

Types de publication

Journal Article

Langues

eng

Pagination

662598

Informations de copyright

Copyright © 2021 Capusoni, Serra, Donzella and Compagno.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Claudia Capusoni (C)

Department of Food, Environmental and Nutritional Sciences, University of Milan, Milan, Italy.

Immacolata Serra (I)

Department of Food, Environmental and Nutritional Sciences, University of Milan, Milan, Italy.

Silvia Donzella (S)

Department of Food, Environmental and Nutritional Sciences, University of Milan, Milan, Italy.

Concetta Compagno (C)

Department of Food, Environmental and Nutritional Sciences, University of Milan, Milan, Italy.

Classifications MeSH