A novel glucoamylase activated by manganese and calcium produced in submerged fermentation by Aspergillus phoenicis

J Basic Microbiol. 2014 May;54(5):333-9. doi: 10.1002/jobm.201200515. Epub 2013 May 17.

Abstract

This study investigates the production of glucoamylase from Aspergillus phoenicis in Machado Benassi (MB) medium using 1% maltose as carbon source. The maximum amylase activity was observed after four days of cultivation, on static conditions at 30 °C. Glucoamylase production was induced by maltose and inhibited by different glucose concentrations. The optimum of temperature and pH were 60-65 °C, and 4.5 or 5.0 to sodium acetate and Mcllvaine buffers, respectively. It was observed that the enzyme was totally stable at 30-65 °C for 1 h, and the pH range was 3.0-6.0. The enzyme was mainly activated by manganese (176%), and calcium (130%) ions. The products of starch hydrolysis were analyzed by thin layer chromatography and after 3 h, only glucose was detected, characterizing the amylolytic activity as a glucoamylase.

Keywords: Activation; Aspergillus phoenicis; Calcium activation; Glucoamylase; Manganese activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus / enzymology*
  • Aspergillus / growth & development*
  • Calcium / metabolism*
  • Chromatography, Thin Layer
  • Culture Media / chemistry
  • Enzyme Activators / metabolism*
  • Enzyme Inhibitors / metabolism
  • Fermentation
  • Glucan 1,4-alpha-Glucosidase / isolation & purification*
  • Glucan 1,4-alpha-Glucosidase / metabolism*
  • Glucose / metabolism
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Maltose / metabolism
  • Manganese / metabolism*
  • Sodium Acetate / metabolism
  • Starch / metabolism
  • Temperature

Substances

  • Culture Media
  • Enzyme Activators
  • Enzyme Inhibitors
  • Manganese
  • Sodium Acetate
  • Maltose
  • Starch
  • Glucan 1,4-alpha-Glucosidase
  • Glucose
  • Calcium