ScholarLens Back to search
2006•Xi'nan Nongye Daxue xuebaoRequires access

PURIFICATION AND CHARACTERIZATION OF PHYTASE FROM ASPERGULLUS NIGER A 3214 AND A. NIGER N 14

Chun Li

Open publisher page 0 citations

Abstract

The phytases of Aspergillus niger A 3214 and its mutant N 14 were purified. Enzymological characterization showed that their optimum pH, optimum temperature and molecular weight were 2.5, 50℃and 47.4 KD, respectively, and their isoelectric point was between 4. 5 and 5. 0. The two phytases retained 80% activity after incubation at 60℃for 10 minutes and 90% activity after treatment for 6 hours with pepsin. K+ , Na+ , Ca 2+ , Mg + and Fe2+ reduced their activity while Zn2+ , Cu2+ and Mn2+ showed no such effects. The Km for sodium phytate and specific activity of A 3214 and N 14 were 0.000 5 and 0.000 4 mol/L and 135 777. 5 and 148 447.5 u/mg, respectively.

About this research paper

What this paper is about

The phytases of Aspergillus niger A 3214 and its mutant N 14 were purified. Enzymological characterization showed that their optimum pH, optimum temperature and molecular weight were 2.5, 50℃and 47.4 KD, respectively, and their isoelectric point was between 4. 5 and 5. 0. The two phytases retained 80% activity after incubation at 60℃for 10 minutes and 90% activity after treatment for 6 hours with pepsin. K+ , Na+ , Ca 2+ , Mg + and Fe2+ reduced their activity while Zn2+ , Cu2+ and Mn2+ showed no such effects. The Km for sodium phytate and specific activity of A 3214 and N 14 were 0.000 5 and 0.000 4 mol/L and 135 777. 5 and 148 447.5 u/mg, respectively.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

The phytases of Aspergillus niger A 3214 and its mutant N 14 were purified. Enzymological characterization showed that their optimum pH, optimum temperature and molecular weight were 2.5, 50℃and 47.4 KD, respectively, and their isoelectric point was between 4. 5 and 5. 0. The two phytases retained 80% activity after incubation at 60℃for 10 minutes and 90% activity after treatment for 6 hours with pepsin. K+ , Na+ , Ca 2+ , Mg + and Fe2+ reduced their activity while Zn2+ , Cu2+ and Mn2+ showed no such effects. The Km for sodium phytate and specific activity of A 3214 and N 14 were 0.000 5 and 0.000 4 mol/L and 135 777. 5 and 148 447.5 u/mg, respectively.

Key concepts: Aspergillus niger, Chemistry, Isoelectric point, Phytase, Nuclear chemistry, Sodium, Food science, Enzyme

Related papers

Related paper 1Related paper 2Related paper 3
Back to paper searchBrowse research topicsOriginal source
PURIFICATION AND CHARACTERIZATION OF PHYTASE FROM ASPERGULLUS NIGER A 3214 AND A. NIGER N 14 — Research Paper | ScholarLens