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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.)

Influence of Different Substrates on the Production of a Mutant Thermostable Glucoamylase in Submerged Fermentation

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Author(s):
Pavezzi, Fabiana Carina [1, 2] ; Jacomassi Carneiro, Andreia A. [1, 2] ; Bocchini-Martins, Daniela Alonso [1] ; Alves-Prado, Heloiza Ferreira [3] ; Ferreira, Henrique [4] ; Martins, Paula M. [4, 2] ; Gomes, Eleni [1] ; da Silva, Roberto [1]
Total Authors: 8
Affiliation:
[1] UNESP Sao Paulo State Univ, Biochem & Appl Microbiol Lab, BR-15054000 Sao Paulo - Brazil
[2] UNESP Sao Paulo State Univ, Inst Biol, Sao Paulo - Brazil
[3] UNESP Sao Paulo State Univ, Food & Tecnol Dept DFTASE, Sao Paulo - Brazil
[4] UNESP Sao Paulo State Univ, Univ Pharmaceut Sci, Dept Biol, Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Applied Biochemistry and Biotechnology; v. 163, n. 1, p. 14-24, JAN 2011.
Web of Science Citations: 8
Abstract

Three mutations, Ser54 -> Pro, Thr314 -> Ala, and His415 -> Tyr, were identified in Aspergillus awamori glucoamylase gene expressed by Saccharomyces cerevisiae. The mutant glucoamylase (GA) was substantially more thermostable than a wild-type GA at 70 A degrees C, with a 3.0 KJ mol(-1) increase in the free energy of thermo-inactivation. The effect of starch from different botanical sources on the production of this GA was measured in liquid fermentation using commercial soluble starch, cassava, potato, and corn as the carbon source. The best substrate for GA production was the potato starch showing an enzymatic activity of 6.6 U/mL. The commercial soluble starch was also a good substrate for the enzyme production with 6.3 U/mL, followed by cassava starch and corn starch with 5.9 and 3.0 U/mL, respectively. These results showed a significant difference on GA production related to the carbon source employed. The mutant GA was purified by acarbose-Sepharose affinity chromatography; the estimated molecular mass was 100 kDa. The mutant GA exhibited optimum activity at pH 4.5 and an optimum temperature of 65 A degrees C. (AU)

FAPESP's process: 07/07930-2 - Termostable mutant glucoamylases from the fungus Aspergillus awamori expressed in Saccharomyces cerevisiae: sequences of the gene, production and purification of the enzyme obtained by submerged fermentation
Grantee:Fabiana Carina Pavezzi
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 07/08083-1 - Evaluation of the prebiotic activity of gluco-oligosaccharides obtained from beta-glucans of Agaricus blazei
Grantee:Andréia Aparecida Jacomassi Carneiro
Support Opportunities: Scholarships in Brazil - Doctorate