Abstract:
:An extracellular acid phosphatase isolated from the culture of a wild strain Aspergillus niger, producing the dephosphorylating 3-phytase, was obtained in a homogeneous form by sequential application of ultrafiltration through PS 50 membrane, gel filtration on Sephadex G-100 and ion exchange chromatography on DEAE-Sepharose CL 6B and CM-Sepharose CL 6B. The enzyme showed a maximum catalytic value in a strongly acidic range (pH 2.0-2.4) with pHopt 2.1 and topt 66 degrees C. The acid phosphatase showed a wide substrate specificity and a high affinity for sodium phytate, 2.5x higher than with 4-nitrophenyl phosphate. This property of the acid phosphatase demonstrated that it is a potent 3-phytase at pH 2.1 and is of great significance for a practical application of the dephosphorylating complex--its addition to the diets of monogastric animals in view of the low pH values in the digestive tract.
journal_name
Folia Microbiol (Praha)journal_title
Folia microbiologicaauthors
Gargova S,Sariyska M,Angelov A,Stoilova Idoi
10.1007/BF02931618subject
Has Abstractpub_date
2006-01-01 00:00:00pages
541-5issue
6eissn
0015-5632issn
1874-9356journal_volume
51pub_type
杂志文章abstract::The ability of six bifidobacterial strains (3 of human origin and 3 isolates from fermented milk products) to utilize glucose, lactose, melezitose, sucrose, raffinose, and stachyose was determined. Dairy-related bifidobacterial strains were identified as Bifidobacterium animalis (2 strains) or as B. pseudolongum (1 st...
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journal_title:Folia microbiologica
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更新日期:2010-07-01 00:00:00
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