Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach
| Autor: | Cassamo Ussemane Mussagy, Juliana Cristina Bassan, Bárbara Ribeiro Ferrari, Valéria de Carvalho Santos-Ebinuma, Ariela Veloso de Paula, Daniela Remonatto |
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| Přispěvatelé: | Universidade Estadual Paulista (UNESP), Universidade de São Paulo (USP) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Montmorillonite KSF
TP1-1185 Vermiculite Catalysis Hydrolysis Immobilization Adsorption lipase Kaolinite Physical and Theoretical Chemistry Lipase QD1-999 Aspergillus japonicus biology Chemistry Chemical technology Environmentally friendly Yield (chemistry) immobilization biology.protein montmorillonite KSF Nuclear chemistry |
| Zdroj: | Scopus Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP Catalysts Volume 11 Issue 10 Catalysts, Vol 11, Iss 1173, p 1173 (2021) |
| Popis: | Made available in DSpace on 2022-04-28T19:44:55Z (GMT). No. of bitstreams: 0 Previous issue date: 2021-10-01 Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that pre-sented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50◦ C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process. Department of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP) Department of Pharmaceutical-Biochemical Technology School of Pharmaceutical Sciences University of São Paulo Department of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP) CAPES: 2017/11482-7 FAPESP: 2017/11482-7 CAPES: 2018/06908-8 FAPESP: 2018/06908-8 CAPES: 2019/15493-9 FAPESP: 2019/15493-9 CAPES: 2020/08655-0 FAPESP: 2020/08655-0 CAPES: 2020/09592-1 FAPESP: 2020/09592-1 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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