Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Enrique J. Mammarella"'
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Akademický článek
Engineering the l-Arabinose Isomerase from Enterococcus Faecium for d-Tagatose Synthesis
Autor: Marylane de Sousa, Ricardo M. Manzo, José L. García, Enrique J. Mammarella, Luciana R. B. Gonçalves, Benevides C. Pessela
Publikováno v: Molecules, Vol 22, Iss 12, p 2164 (2017)
l-Arabinose isomerase (EC 5.3.1.4) (l-AI) from Enterococcus faecium DBFIQ E36 was overproduced in Escherichia coli by designing a codon-optimized synthetic araA gene. Using this optimized gene, two N- and C-terminal His-tagged-l-AI proteins were prod
Externí odkaz: https://doaj.org/article/d84bc9f4f4314d028a6a4d4fe1c28030
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3
Immobilization of Carboxypeptidase A into Modified Chitosan Matrixes by Covalent Attachment
Autor: Horacio Bonazza, Enrique J. Mammarella, Roberto Julio Ceruti, Wellington Sabino Adriano, Guillermo Adrian Sihufe, Ricardo Martín Manzo
Publikováno v: Applied Biochemistry and Biotechnology. 185:1029-1043
Carboxypeptidase A (CPA) is a metalloexopeptidase that catalyzes the hydrolysis of the peptide bonds that are adjacent to the C-terminal end of a polypeptide chain. The enzyme preferentially cleaves over C-terminal L-amino acids with aromatic or bran
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8249bd2d6378f13b11492678626a5088
https://doi.org/10.1007/s12010-018-2708-4
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4
Immobilized enzymes and their implications
Autor: Sofia Municoy, German Abel Islan, Ricardo Martín Manzo, Maximiliano Luis Cacicedo, Enrique J. Mammarella, Martín G. Bellino, Martín F. Desimone, Guillermo R. Castro, Horacio Bonazza
Publikováno v: Biomass, Biofuels, Biochemicals : Advances in Enzyme Technology
The main goal of enzyme immobilization is the re-use of enzymes for many reaction cycles and extended periods of time. Many novel strategies were developed during the last 20 years. The most common are thec arrier-bound technologies employing synthet
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8dc6d96be6ca5e1c7d8afd414e3f95b
https://www.sciencedirect.com/science/article/pii/B9780444641144000078
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6
One-Step Immobilization and Stabilization of a Recombinant Enterococcus faecium DBFIQ E36 L-Arabinose Isomerase for D-Tagatose Synthesis
Autor: Enrique J. Mammarella, Benevides C. C. Pessela, Vânia Maria Maciel Melo, Ricardo Martín Manzo, Marylane de Sousa, André S L M Antunes, Denise Cavalcante Hissa, Luciana Rocha Barros Gonçalves, José Luis García
Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
Repositório Institucional da Universidade Federal do Ceará (UFC)
Universidade Federal do Ceará (UFC)
instacron:UFC
A recombinant L-arabinose isomerase from Enterococcus faecium DBFIQ E36 was immobilized onto multifunctional epoxide supports by chemical adsorption and onto a chelate-activated support via polyhistidine-tag, located on the N-terminal (N-His-L-AI) or
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe3c9d40795d4de6e9ff2f1e77956236
https://pubmed.ncbi.nlm.nih.gov/30430344
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7
Operational and Thermal Stability Analysis of Thermomyces lanuginosus Lipase Covalently Immobilized onto Modified Chitosan Supports
Autor: Horacio L, Bonazza, Ricardo M, Manzo, José C S, Dos Santos, Enrique J, Mammarella
Publikováno v: Applied biochemistry and biotechnology. 184(1)
The aim of this paper was to evaluate different strategies of chitosan activation using cross-linking reagent like glycidol, epichlorohydrin, and glutaraldehyde for Thermomyces lanuginosus lipase (TLL) immobilization. Operational activity and stabili
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2768e8ea8762e82a87884083b54e1319
https://pubmed.ncbi.nlm.nih.gov/28664524
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8
Engineering the L-Arabinose somerase from Enterococcus faecium for D-tagatose synthesis
Autor: Enrique J. Mammarella, José Luis García, Ricardo Martín Manzo, Benevides C. C. Pessela, Marylane de Sousa, Luciana Rocha Barros Gonçalves
Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Molecules, Vol 22, Iss 12, p 2164 (2017)
Molecules; Volume 22; Issue 12; Pages: 2164
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
L-Arabinose isomerase (EC 5.3.1.4) (l-AI) from Enterococcus faecium DBFIQ E36 was overproduced in Escherichia coli by designing a codon-optimized synthetic araA gene. Using this optimized gene, two N- and C-terminal His-tagged-l-AI proteins were prod
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3083c29c8596085a45b12456cd21a071
http://hdl.handle.net/10261/194069
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9
Improving the properties of chitosan as support for the covalent multipoint immobilization of chymotrypsin
Autor: Enrique J. Mammarella, Dasciana S. Rodrigues, Dany B. Mendonça, Wellington Sabino Adriano, Raquel L. C. Giordano
Changing gel structure and immobilization conditions led to a significant improvement in the covalent multipoint attachment of chymotrypsin on chitosan. The use of sodium alginate, gelatin, or κ-carrageenan, activation with glutaraldehyde, glycidol,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a754e31ab9d6af770bd6ce74d36141f
http://pubs.acs.org/doi/abs/10.1021/bm8002754
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