Partial purification and physicochemical characterization of glucoamylase from Aspergillus sp. BIOTECH 3104

Issue Date

6-2007

Abstract

Extracellular glucoamylase was partially purified from the culture filtrate of Aspergillus sp. BIOTECH 3104 through ultrafiltration, 90% ammonium sulfate fractionation, DEAE-cellulose ion exchange chromatography and Sephadex G-100 gel filtration. The enzyme was partially purified 21-fold at Sephadex G-100 and showed an estimated MW of 60,000 Da in SDS-PAGE. Its pH and temperature optima were pH 4.5 and 30 °C, respectively. Glucoamylase activity was significantly reduced by Co2+, Fe3+ and EDTA. Addition of 2% SDS and 0.8 M urea denatured the enzyme causing 66% and 89% loss of enzymatic activities, respectively. The use of 1% sodium benzoate and 1% potassium sorbate resulted in reduced loss of activity; with the enzyme retaining 92% and 86% of activity compared with 70% of control after 4 wk of storage at 4 °C.

Source or Periodical Title

Philippine Agricultural Scientist

ISSN

317454

Volume

90

Issue

2

Page

131-136

Document Type

Article

Language

English

Subject

Aspergillus, Chromatography, Denaturation, Glucoamylase, Saccharification

Digital Copy

none

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