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

Autor: Benassi VM; Departamento de Bioquímica e Imunologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil., Pasin TM, Facchini FD, Jorge JA, Teixeira de Moraes Polizeli Mde L
Jazyk: angličtina
Zdroj: Journal of basic microbiology [J Basic Microbiol] 2014 May; Vol. 54 (5), pp. 333-9. Date of Electronic Publication: 2013 May 17.
DOI: 10.1002/jobm.201200515
Abstrakt: 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.
(© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Databáze: MEDLINE
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