Cloning, expression, and enzyme characterization of an acid heat-stable phytase from Aspergillus fumigatus WY-2.

Abstract:

:A novel thermostable phytase gene was cloned from Aspergillus fumigatus WY-2. It was 1459 bp in size and encoded a polypeptide of 465 amino acids. The gene was expressed in Pichia pastoris GS115 as an extracellular enzyme. The expressed enzyme was purified to homogeneity and biochemically characterized. The purified enzyme had a specific activity of 51 U/mg with an approximate molecular mass of 88 kDa. The optimum pH and temperature for activity were pH 5.5 and 55 degrees C, respectively. After incubation at 90 degrees C for 15 min, it still remained at 43.7% of the initial activity. The enzyme showed higher affinity for sodium phytate than other phosphate conjugates, and the K(m) and K(cat) for sodium phytate were 114 microM: and 102 s(-1), respectively. Incubated with pepsin at 37 degrees C for 2 h at the ratio (pepsin/phytase, wt/wt) of 0.1, it still retained 90.1% residual activity. These exceptional properties give the newly cloned enzyme good potential in animal feed applications.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Wang Y,Gao X,Su Q,Wu W,An L

doi

10.1007/s00284-006-0613-5

subject

Has Abstract

pub_date

2007-07-01 00:00:00

pages

65-70

issue

1

eissn

0343-8651

issn

1432-0991

journal_volume

55

pub_type

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