Aspergillus niger pH 2.1 optimum acid phosphatase with high affinity for phytate

. 2006 ; 51 (6) : 541-5.

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid17455790

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.

Zobrazit více v PubMed

Nature. 1970 Aug 15;227(5259):680-5 PubMed

Anal Biochem. 1981 May 15;113(2):313-7 PubMed

Folia Microbiol (Praha). 1998;43(4):323-38 PubMed

Arch Tierernahr. 1999;52(1):15-27 PubMed

Biosci Biotechnol Biochem. 1997 Sep;61(9):1512-7 PubMed

Appl Environ Microbiol. 1998 Nov;64(11):4446-51 PubMed

Biochem Biophys Res Commun. 1994 Aug 30;203(1):182-9 PubMed

World J Microbiol Biotechnol. 1993 Jan;9(1):117-9 PubMed

J Mol Biol. 1999 May 21;288(5):965-74 PubMed

Prep Biochem. 1987;17(1):63-91 PubMed

Prep Biochem. 1987;17(4):397-422 PubMed

Folia Microbiol (Praha). 2003;48(6):767-70 PubMed

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...