Diego E. Sastre
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Diego E. Sastre has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
Beatriz Trastoy
Structural Biology Unit, CIC bioGUNE Technological Park of Bizkaia, Derio, Vizcaya, Spain
1 shared publication- Caterina Gruenwaldt Cunha Marques Netto
Department of Biochemistry Emory University School of Medicine Atlanta Georgia USA
1 shared publication Diego de Mendoza
Instituto de Biología Molecular y Celular de Rosario (IBR), Rosario, Santa Fe, Argentina
1 shared publication- Fernando Cruz Moraes
Department of Chemistry, Federal University of São Carlos (UFSCar), São Carlos 13560-970, Brazil
1 shared publication - Frederico José Gueiros-Filho
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil
1 shared publication - Iago de Assis Modenez
São Carlos Institute of Chemistry, University of São Paulo, São Carlos 13560-970, Brazil
1 shared publication
Latest Publications
- Open Access
- 1 February 2020
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 295 (7) , 2136-2147
Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria
- 1 February 2020
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 295 (7) , 2136-2147
Open AccessMembrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria
- Open Access
Influence of Glutaraldehyde Cross-Linking Modes on the Recyclability of Immobilized Lipase B from Candida antarctica for Transesterification of Soy Bean Oil
Lipase B from Candida antarctica (CAL-B) is largely employed as a biocatalyst for hydrolysis, esterification, and transesterification reactions. CAL-B is a good model enzyme to study factors affecting the enzymatic structure, activity and/or stability after an immobilization process. In this study, we analyzed the immobilization of CAL-B enzyme on different magnetic nanoparticles, synthesized by the coprecipitation method inside inverse micelles made of zwitterionic surfactants, with distinct carbon chain length: 4 (ImS4), 10 (ImS10) and 18 (ImS18) carbons. Magnetic nanoparticles ImS4 and ImS10 were shown to cross-link to CAL-B enzyme via a Michael-type addition, whereas particles with ImS18 were bond via pyridine formation after glutaraldehyde cross-coupling. Interestingly, the Michael-type cross-linking generated less stable immobilized CAL-B, revealing the influence of a cross-linking mode on the resulting biocatalyst behavior. Curiously, a direct correlation between nanoparticle agglomerate sizes and CAL-B enzyme reuse stability was observed. Moreover, free CAL-B enzyme was not able to catalyze transesterification due to the high methanol concentration; however, the immobilized CAL-B enzyme reached yields from 79.7 to 90% at the same conditions. In addition, the transesterification of lipids isolated from oleaginous yeasts achieved 89% yield, which confirmed the potential of immobilized CAL-B enzyme in microbial production of biodiesel.
Open AccessInfluence of Glutaraldehyde Cross-Linking Modes on the Recyclability of Immobilized Lipase B from Candida antarctica for Transesterification of Soy Bean Oil
Lipase B from Candida antarctica (CAL-B) is largely employed as a biocatalyst for hydrolysis, esterification, and transesterification reactions. CAL-B is a good model enzyme to study factors affecting the enzymatic structure, activity and/or stability after an immobilization process. In this study, we analyzed the immobilization of CAL-B enzyme on different magnetic nanoparticles, synthesized by the coprecipitation method inside inverse micelles made of zwitterionic surfactants, with distinct carbon chain length: 4 (ImS4), 10 (ImS10) and 18 (ImS18) carbons. Magnetic nanoparticles ImS4 and ImS10 were shown to cross-link to CAL-B enzyme via a Michael-type addition, whereas particles with ImS18 were bond via pyridine formation after glutaraldehyde cross-coupling. Interestingly, the Michael-type cross-linking generated less stable immobilized CAL-B, revealing the influence of a cross-linking mode on the resulting biocatalyst behavior. Curiously, a direct correlation between nanoparticle agglomerate sizes and CAL-B enzyme reuse stability was observed. Moreover, free CAL-B enzyme was not able to catalyze transesterification due to the high methanol concentration; however, the immobilized CAL-B enzyme reached yields from 79.7 to 90% at the same conditions. In addition, the transesterification of lipids isolated from oleaginous yeasts achieved 89% yield, which confirmed the potential of immobilized CAL-B enzyme in microbial production of biodiesel.