Use este identificador para citar ou linkar para este item:
https://repositorio.ufrn.br/handle/123456789/29601| Título: | Liquefied petroleum gas as solvent medium for the treatment of immobilized inulinases |
| Autor(es): | Silva, Marceli Fernandes Golunski, Simone Maria Rigo, Diane Mossi, Vinícius Luccio, Marco Di Mazutti, Marcio A. Pergher, Sibele Berenice Castellã Oliveira, Débora Oliveira, J. Vladimir Treichel, Helen |
| Palavras-chave: | Inulinase;Compressed fluid LPG |
| Data do documento: | Fev-2013 |
| Editor: | Wiley |
| Referência: | SILVA, Marceli Fernandes; GOLUNSKI, Simone Maria; RIGO, Diane; MOSSI, Vinícius; LUCCIO, Marco Di; MAZUTTI, Marcio A.; PERGHER, Sibele Berenice Castellã; OLIVEIRA, Débora; OLIVEIRA, J. Vladimir; TREICHEL, Helen. Liquefied petroleum gas as solvent medium for the treatment of immobilized inulinases. Journal Of Chemical Technology & Biotechnology, [s.l.], v. 88, n. 2, p. 280-286, fev. 2013. ISSN 1097-4660. Disponível em: https://onlinelibrary.wiley.com/doi/abs/10.1002/jctb.3827. Acesso em: 14 jul. 2020. https://doi.org/10.1002/jctb.3827. |
| Resumo: | BACKGROUND: The main goal of this work is to assess the influence of pressurized liquefied petroleum gas (LPG) treatment on the enzymatic activity of immobilized inulinases. The effects of process variables were evaluated through 23 experimental design. RESULTS: Inulinase from Klyveromyces marxianus NRRL Y‐7571 presented an increase of 163% in residual activity using LPG at 30 bar during 1 h exposure using a depressurization rate of 20 bar min−1. For Aspergillus niger commercial inulinase, an increment of 129% in residual activity was observed at 30 bar for 1 h treatment at the highest depressurization rate (20 bar min−1). Enzymatic activities changed significantly depending on the enzyme source and the experimental treatment conditions investigated, such as exposure time, depressurization rate and pressure. CONCLUSION: Hence, compressed LPG appears to be a promising technique with practical relevance as a preparation step to improve enzyme activity, thus helping the development of new biotransformation processes. © 2012 Society of Chemical Industry |
| URI: | https://repositorio.ufrn.br/jspui/handle/123456789/29601 |
| ISSN: | 1097-4660 |
| Aparece nas coleções: | IQ - Artigos publicados em periódicos |
Arquivos associados a este item:
Não existem arquivos associados a este item.
Os itens no repositório estão protegidos por copyright, com todos os direitos reservados, salvo quando é indicado o contrário.