V
Vanessa de Oliveira Arnoldi Pellegrini
Researcher at University of São Paulo
Publications - 34
Citations - 458
Vanessa de Oliveira Arnoldi Pellegrini is an academic researcher from University of São Paulo. The author has contributed to research in topics: Enzymatic hydrolysis & Hydrolysis. The author has an hindex of 8, co-authored 27 publications receiving 189 citations. Previous affiliations of Vanessa de Oliveira Arnoldi Pellegrini include Roskilde University & Sao Paulo State University.
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Journal ArticleDOI
Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate
Amanda Bernardes,Vanessa de Oliveira Arnoldi Pellegrini,F Curtolo,Cesar M. Camilo,Bruno Luan Mello,Marcus A. Johns,Janet L. Scott,Francisco Eduardo Gontijo Guimarães,Igor Polikarpov +8 more
TL;DR: It is demonstrated that binding of CBMs to cellulose is non-homogeneous, irreversible and leads to its amorphisation, and effects of CBM-promoted amorphogenesis on cellulose hydrolysis by cellulases are revealed.
Journal ArticleDOI
An overview on progress, advances, and future outlook for biohydrogen production technology
Kamalpreet Kaur Brar,Anelyse Abreu Cortez,Vanessa de Oliveira Arnoldi Pellegrini,K. Amulya,Igor Polikarpov,Sara Magdouli,Manu Kumar,Yung-Hun Yang,Shashi Kant Bhatia,Satinder Kaur Brar +9 more
TL;DR: In this paper , a review aimed to fill the void among technical and applied research and review the current advances in genetic engineering and metabolic pathway developments to improve H 2 productivity is presented.
Journal ArticleDOI
Cellulose nanofibers production using a set of recombinant enzymes
Bruno Roberto Rossi,Vanessa de Oliveira Arnoldi Pellegrini,Anelyse Abreu Cortez,Emanoele Maria Santos Chiromito,Antonio J. F. Carvalho,Lidiane O. Pinto,Camila A. Rezende,Valmor Roberto Mastelaro,Igor Polikarpov +8 more
TL;DR: The results showed that a cooperative action of the set of hydrolytic and oxidative enzymes can be used as a "green" treatment prior to the sonication step to produce nanofibrillated cellulose with advanced properties.
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Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism
Marcelo Vizoná Liberato,Rodrigo L. Silveira,Erica T. Prates,Evandro Ares de Araújo,Vanessa de Oliveira Arnoldi Pellegrini,Cesar M. Camilo,Marco Antonio Seiki Kadowaki,Mario de Oliveira Neto,Alexander Popov,Munir S. Skaf,Igor Polikarpov +10 more
TL;DR: The full-length structure of a cellulase from Bacillus licheniformis is reported, a member of the GH5 subfamily 4 that is entirely dependent on its two ancillary modules (Ig-like module and CBM46) for catalytic activity.
Journal ArticleDOI
Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme
Vanessa de Oliveira Arnoldi Pellegrini,Viviane Isabel Serpa,Andre S. Godoy,Cesar M. Camilo,Amanda Bernardes,Camila A. Rezende,Nei Pereira Junior,João Paulo L. Franco Cairo,Fabio M. Squina,Igor Polikarpov +9 more
TL;DR: In this paper, the authors reported biochemical characterization of the recombinant endoglucanase I from T. harzianum, ThCel7B, and its catalytic core domain.