Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Fernanda Dell Antonio Facchini"'
Autor:
Ana Claudia Vici, Andrezza Furquim da Cruz, Fernanda Dell Antonio Facchini, Caio Cesar Carvalho, Marita Giminez Pereira, Raquel eFonseca-Maldonado, Richard John Ward, Benevides Costa Pessela, Gloria eFernadez-Lorente, Fernando Araripe Gonçalves Torres, João Atílio Jorge, Maria De Lourdes Teixeira De Moraes Polizeli
Publikováno v:
Frontiers in Microbiology, Vol 6 (2015)
Lipases (EC 3.1.1.3) comprise a biotechnologically important group of enzymes because they are able to catalyze both hydrolysis and synthesis reactions, depending on the amount of water in the system. One of the most interesting application of lipase
Externí odkaz:
https://doaj.org/article/422f1dbd3ca840e2b1de0eb6ed275a81
Autor:
Marco Filice, Benevides C. C. Pessela, Jose M. Guisan, Gloria Fernández-Lorente, Maria de Lourdes Teixeira de Moraes Polizeli, Marita Gimenez Pereira, Fernanda Dell Antonio Facchini, Ana Claudia Vici
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Catalysts, Vol 8, Iss 2, p 84 (2018)
Catalysts; Volume 8; Issue 2; Pages: 84
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
instname
Catalysts, Vol 8, Iss 2, p 84 (2018)
Catalysts; Volume 8; Issue 2; Pages: 84
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
This article belongs to the Special Issue Immobilized Biocatalysts.
Fusarium verticillioides lipases were purified in a “cascade” method using octadecyl Sepabeads and octyl Sepharose resins, which led to the isolation of two proteins with li
Fusarium verticillioides lipases were purified in a “cascade” method using octadecyl Sepabeads and octyl Sepharose resins, which led to the isolation of two proteins with li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf1460fb7e1e0a1fd02169c7bda40c41
http://hdl.handle.net/10261/192566
http://hdl.handle.net/10261/192566
Autor:
Ana Claudia Vici, Aline M. Polizeli, Fernanda Dell Antonio Facchini, Jose M. Guisan, Maria de Lourdes Teixeira de Moraes Polizeli, Gloria Fernández-Lorente, Benevides C. C. Pessela, João Atílio Jorge, Marita Gimenez Pereira
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Digital.CSIC. Repositorio Institucional del CSIC
instname
Universidade de São Paulo (USP)
instacron:USP
Digital.CSIC. Repositorio Institucional del CSIC
instname
Lipase from Hypocrea pseudokoningii was purified using the support Octyl-Sepharose. This adsorption resulted in a 3-fold increase in activity of the immobilized enzyme. Following, still on this support, the lipase was enriched in surface amino groups
Autor:
João Atílio Jorge, Gloria Fernández-Lorente, Luiz Estevam Cavenage Filó, J. M. Guisan, Ana Claudia Vici, Marita Gimenez Pereira, Fernanda Dell Antonio Facchini, Benevides C. C. Pessela, Maria de Lourdes Teixeira de Moraes Polizeli, Aline M. Polizeli
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
instname
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Hypocrea pseudokoningii purified lipase was immobilized on hydrophobic supports (phenyl-sepharose, butyl-sepharose, octyl-sepharose, Hexyl Toyopearl, Lewatit, Purolite, Decaoctyl sepabeads) and ionic supports (Duolite, DEAE-agarose, PEI-agarose, MANA
Autor:
Benevides C. C. Pessela, Fernanda Dell Antonio Facchini, Marita Gimenez Pereira, Paulo Ricardo Heinen, Ana Claudia Vici, Susana Velasco-Lozano, Aline M. Polizeli, Jose M. Guisan, Maria de Lourdes Teixeira de Moraes Polizeli, Sonia Moreno-Pérez, Mariana Cereia, Gloria Fernández-Lorente, João Atílio Jorge
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules; Volume 22; Issue 9; Pages: 1448
Molecules, Vol 22, Iss 9, p 1448 (2017)
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
instname
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules; Volume 22; Issue 9; Pages: 1448
Molecules, Vol 22, Iss 9, p 1448 (2017)
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
This article belongs to the Special Issue Lipases and Lipases Modification.
Enzyme immobilization can promote several advantages for their industrial application. In this work, a lipase from Hypocrea pseudokoningii was efficiently linked to four
Enzyme immobilization can promote several advantages for their industrial application. In this work, a lipase from Hypocrea pseudokoningii was efficiently linked to four
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e5f2d7db79ef6a00a68dbadaa036970
http://hdl.handle.net/10261/194046
http://hdl.handle.net/10261/194046
Autor:
Fernanda Dell Antonio Facchini, Maria de Lourdes Teixeira de Moraes Polizeli, Vivian Machado Benassi, João Atílio Jorge, Thiago Machado Pasin
Publikováno v:
Journal of Basic Microbiology. 54:333-339
This study investigates the production of glucoamylase from Aspergillus phoenicis in Machado Benassi (MB) medium using 1% maltose as carbon source. The maximum amylase activity was observed after four days of cultivation, on static conditions at 30
Autor:
Marita Gimenez Pereira, Ana Claudia Vici, Andressa Tironi Vieira, Antonio Carlos Ferreira Batista, Taila Angélica da Silva, Fernanda Dell Antonio Facchini, M.F. de Oliveira, Maria de Lourdes Teixeira de Moraes Polizeli, João Atílio Jorge
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Revista Brasileira de Engenharia de Biossistemas, Vol 10, Iss 1, Pp 01-13 (2016)
Universidade de São Paulo (USP)
instacron:USP
Revista Brasileira de Engenharia de Biossistemas, Vol 10, Iss 1, Pp 01-13 (2016)
The application of lipases in various fields has been notably increased in the last few decades and qualitative/quantitative improvements need to be done. However, many methodologies of screening are described in order to find a good lipase producer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddf2f2f2611841d37b18f58cd88dce7a
Autor:
Luiz Alexandre Pedro de Freitas, Ricardo Andrade Reis, Ana Claudia Vici, Maria de Lourdes Teixeira de Moraes Polizeli, Vivian Machado Benassi, João Atílio Jorge, Fernanda Dell Antonio Facchini, Héctor Francisco Terenzi
Publikováno v:
Bioprocess and Biosystems Engineering. 34:1027-1038
Fibrolytic enzyme production by Aspergillus japonicus C03 was optimized in a medium containing agro-industrial wastes, supplemented with peptone and yeast extract. A 2(3) full factorial composite and response surface methodology were used to design t
Autor:
Maria de Lourdes Teixeira de Moraes Polizeli, João Atílio Jorge, Victor Ricardo Amin Reis, Fernanda Dell Antonio Facchini, Ricardo Andrade Reis, Héctor Francisco Terenzi, Ana Claudia Vici
Publikováno v:
Bioprocess and Biosystems Engineering. 34:347-355
Solid-state fermentation obtained from different and low-cost carbon sources was evaluated to endocellulases and endoxylanases production by Aspergillus japonicus C03. Regarding the enzymatic production the highest levels were observed at 30 °C, usi
Autor:
Filipe Vasconcelos, Eleni Gomes, Lara Durães Sette, Letícia Maria Zanphorlin, Andre Rodrigues, Fernanda Dell Antonio Facchini, Gustavo Orlando Bonilla-Rodriguez, Rafaella Costa Bonugli-Santos
Publikováno v:
The Journal of Microbiology. 48:331-336
Thermophilic fungi produce thermostable enzymes which have a number of applications, mainly in biotechnological processes. In this work, we describe the characterization of a protease produced in solidstate (SSF) and submerged (SmF) fermentations by