ArticleFolia microbiologica2008
Phytase from antarctic yeast strain Cryptococcus laurentii AL27.
Article in Folia microbiologica, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 34 citations in OpenAlex.
- Production, purification and characterization of phytase from Pichia kudriavevii FSMP-Y17and its application in layers feed.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity inFrontiers in bioengineering and biotechnology · 2021Article
- Responses of Atlantic cod Gadus morhua head kidney leukocytes to phytase produced by gastrointestinal-derived bacteria.Fish physiology and biochemistry · 2010Article
- Production and chemical characterization of an exopolysaccharide synthesized by psychrophilic yeast strain Sporobolomyces salmonicolor AL₁ isolated from Livingston Island, Antarctica.Folia microbiologica · 2010Article
- Phytase activity in rabbit cecal bacteria.Folia microbiologica · 2009Article
- Production of an exopolysaccharide by Antarctic yeast.Folia microbiologica · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptococcus laurentii strain AL27 demonstrating significant potential for intracellular phytase production was selected by 2-step screening of Antarctic yeasts. The strain showed increased phytase activity in a culture medium with 40 g/L sucrose, KH2PO4 providing 5 mg/L phosphorus, and cultivation temperature of 24 degrees C, which relates it to psychrotrophic microorganisms. The enzyme kinetic characteristics according to sodium phytate were Km = 0.98 mmol/L, vlim = 33.3 micromol g(-1) min(-1). The enzyme had maximum activity at 40 degrees C and acted within a wide pH range: from 2.0 to 5.5, which is of positive significance for its direct inclusion into the feed of monogastric animals.
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Registered trials
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