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

• Published in: Journal of basic microbiology Vol. 54; no. 5; pp. 333 - 339
• Main Authors: Benassi, Vivian Machado, Pasin, Thiago Machado, Facchini, Fernanda Dell Antonio, Jorge, João Atílio, de Lourdes Teixeira de Moraes Polizeli, Maria
• Format: Journal Article
• Language: English
• Published: Germany Blackwell Publishing Ltd 01-05-2014
• Subjects: Activation; Aspergillus; Aspergillus - enzymology; Aspergillus - growth & development; Aspergillus phoenicis; Calcium - metabolism; Calcium activation; 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; Glucoamylase; Glucose - metabolism; Hydrogen-Ion Concentration; Hydrolysis; Maltose - metabolism; Manganese - metabolism; Manganese activation; Sodium Acetate - metabolism; Starch - metabolism; Temperature; Activation; Glucoamylase; Manganese activation; Calcium activation; Aspergillus phoenicis
• ISSN: 0233-111X; 1521-4028
• DOI: 10.1002/jobm.201200515

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.