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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Production and characteristics comparison of crude beta-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes

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Author(s):
Ribeiro Leite, Rodrigo Simoes [1] ; Alves-Prado, Heloiza Ferreira [2] ; Cabral, Hamilton [3] ; Pagnocca, Fernando Carlos [2] ; Gomes, Eleni [1] ; Da-Silva, Roberto [1]
Total Authors: 6
Affiliation:
[1] Sao Paulo State Univ, UNESP, IBILCE, Lab Biochem & Appl Microbiol, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[2] Sao Paulo State Univ, UNESP, Fac Engn Ilha Solteira, FEIS, BR-15385000 Ilha Solteira, SP - Brazil
[3] Univ Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Pharmaceut Sci, BR-14040903 Ribeirao Preto, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Enzyme and Microbial Technology; v. 43, n. 6, p. 391-395, NOV 6 2008.
Web of Science Citations: 63
Abstract

The purified beta-glucosidase of Aureobasidium pullulans ER-16 is one of more thermostable enzyme reported to date. Considering the unfeasibility of using purified enzyme for industrial application, it was interesting to analyze this property for the crude enzyme. Thermophilic fungus Thermoascus aurantiacus CBMAI-756 and mesophilic A. pullulans ER-16 were cultivated in different hemicellulosic materials on solid-state cultivation for beta-glucosidase production. Wheat bran was most appropriate for beta-glucosidase production by both microorganisms. T. aurantiacus exhibited maximum enzyme production (7.0 U/ml or 70 U/g) at 48-72 h and A. pullulans a maximum (1.3 U/ml or 13 U/g) at 120 h. Maximum activities were at 75 degrees C with optimum pH at 4.5 and 4.0, for T aurantiacus and A. pullulans, respectively. A. pullulans's beta-glucosidase was more pH stable (4.5-10.0 against 4.5-8.0) and more thermostable (90% after 1 h at 75 degrees C against 85% after 1 h at 70 degrees C) than the enzyme from the thermophilic T. aurantiacus. The t((1/2)) at 80 degrees C were 50 and 12.5 min for A. pullulans and T. aurantiascus, respectively. These data confirm the high thermostability of crude beta-glucosidase from A. pullulans. Both beta-glucosidases were strongly inhibited by glucose, but ethanol significantly increased the activity of the enzyme from T. aurantiacus. (C) 2008 Elsevier Inc. All rights reserved. (AU)