O
Oscar Romero
Researcher at Pontifical Catholic University of Valparaíso
Publications - 29
Citations - 446
Oscar Romero is an academic researcher from Pontifical Catholic University of Valparaíso. The author has contributed to research in topics: Lipase & Enzyme Reactivation. The author has an hindex of 11, co-authored 29 publications receiving 354 citations. Previous affiliations of Oscar Romero include Polytechnic University of Catalonia & Spanish National Research Council.
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Journal ArticleDOI
Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity
Marco Filice,Oscar Romero,Javier Gutiérrez-Fernández,B. de las Rivas,Juan A. Hermoso,Jose M. Palomo +5 more
TL;DR: A solid-phase strategy using lipase as a biomolecular scaffold to produce a large amount of Cu(2+)-metalloenzyme and creating a heterogeneous artificial metallolipase showing chimeric catalytic activity is proposed.
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Reactivation of covalently immobilized lipase from Thermomyces lanuginosus
Rafael C. Rodrigues,Rafael C. Rodrigues,César A. Godoy,Marco Filice,Juan M. Bolivar,Armand Palau-Ors,Jesús Manuel García-Vargas,Oscar Romero,Oscar Romero,Lorena Wilson,Marco Antônio Záchia Ayub,Roberto Fernandez-Lafuente,Jose M. Guisan +12 more
TL;DR: Results suggested that the opening of the lipase could be a critical step in the inactivation or reactivation of immobilized TLL, and the simple incubation of the partially or fully inactivated enzyme under mild conditions permitted to recover some activity, even in thermal inactivations.
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Reactivation of penicillin acylase biocatalysts: Effect of the intensity of enzyme–support attachment and enzyme load
TL;DR: Full recovery of enzyme activity was obtained with Gx 1 -PGA by reactivation in aqueous medium up to 74 IU/g support, but at higher enzyme loads recovery was significantly impaired because of intense protein–protein interaction during biocatalyst inactivation and reactivation.
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Preparation of an Immobilized Lipase‐Palladium Artificial Metalloenzyme as Catalyst in the Heck Reaction: Role of the Solid Phase
TL;DR: The authors thank Dr. Ramiro Martinez from Novozymes for the generous gift of lipases and Dr. Daminatti from Resindion for the gift of the Sepabeads resin.
Journal ArticleDOI
Enzyme Surface Glycosylation in the Solid Phase: Improved Activity and Selectivity of Candida Antarctica Lipase B
Melissa L. E. Gutarra,Melissa L. E. Gutarra,Oscar Romero,Olga Abian,Fernando Araripe Gonçalves Torres,Denise M. G. Freire,Aline Machado de Castro,Jose M. Guisan,Jose M. Palomo +8 more
TL;DR: Tailor‐made oligosaccharides and polymers were investigated for a specific surface glycosylation of Candida antarctica lipase (fraction B) (CAL‐B) already immobilized on octyl‐Sepharose by interfacial activation and revealed interesting conformational changes in secondary and secondary structures of the protein after modification.