Titre:	Optimization and partial purification of beta‑galactosidase production by Aspergillus niger isolated from Brazilian soils using soybean residue
Auteur(s):	Martarello, Raquel Dall’Agnol Cunha, Luana Cardoso, Samuel Leite Freitas, Marcela Medeiros de Silveira, Dâmaris Fonseca‑Bazzo, Yris Maria Homem de Mello, Mauricio Ferreira Filho, Edivaldo Ximenes Batista, Pérola de Oliveira Magalhães Dias
metadata.dc.identifier.orcid:	http://orcid.org/0000-0001-8011-6940
Assunto::	Fungos Enzimas Purificação Resíduos agroindustriais
Date de publication:	2019
Editeur:	Springer Open
Référence bibliographique:	MARTARELLO, Raquel Dall’Agnol et al. Optimization and partial purification of beta‑galactosidase production by Aspergillus niger isolated from Brazilian soils using soybean residue. AMB Express, v. 9, p. 2-13, 2019. DOI: https://doi.org/10.1186/s13568-019-0805-6. Disponível em: https://amb-express.springeropen.com/articles/10.1186/s13568-019-0805-6. Acesso em:
Abstract:	β-Galactosidases are widely used for industrial applications. These enzymes could be used in reactions of lactose hydrolysis and transgalactosylation. The objective of this study was the production, purification, and characterization of an extracellular β-galactosidase from a filamentous fungus, Aspergillus niger. The enzyme production was optimized by a factorial design. Maximal β-galactosidase activity (24.64 U/mL) was found in the system containing 2% of a soybean residue (w/v) at initial pH 7.0, 28 °C, 120 rpm in 7 days. ANOVA of the optimization study indicated that the response data on temperature and pH were significant (p < 0.05). The regression equation indicated that the R2 is 0.973. Ultrafiltration at a 100 and 30 kDa cutoff followed by gel filtration and anion exchange chromatography were carried out to purify the fungal β-galactosidase. SDS-PAGE revealed a protein with molecular weight of approximately 76 kDa. The partially purified enzyme showed an optimum temperature of 50 °C and optimum pH of 5.0, being stable under these conditions for 15 h. The enzyme was exposed to conditions approaching gastric pH and in pepsin’s presence, 80% of activity was preserved after 2 h. These results reveal a A. niger β-galactosidase obtained from residue with favorable characteristics for food industries.
Licença::	© The Author(s) 2019. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
Collection(s) :	Artigos publicados em periódicos e afins

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