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A novel glucoamylase activated by manganese and calcium produced in submerged fermentation by Aspergillus phoenicis
Author(s) -
Benassi Vivian Machado,
Pasin Thiago Machado,
Facchini Fernanda Dell Antonio,
Jorge João Atílio,
de Lourdes Teixeira de Moraes Polizeli Maria
Publication year - 2014
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201200515
Subject(s) - maltose , chemistry , hydrolysis , starch , amylase , fermentation , manganese , calcium , enzyme , sodium , enzyme assay , chromatography , sodium acetate , biochemistry , organic chemistry
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.