Development and biotechnological application of a novel endoxylanase family GH10 identified from sugarcane soil metagenome.

Autor: Thabata M Alvarez, Rosana Goldbeck, Camila Ramos dos Santos, Douglas A A Paixão, Thiago A Gonçalves, João Paulo L Franco Cairo, Rodrigo Ferreira Almeida, Isabela de Oliveira Pereira, George Jackson, Junio Cota, Fernanda Büchli, Ana Paula Citadini, Roberto Ruller, Carla Cristina Polo, Mario de Oliveira Neto, Mário T Murakami, Fabio M Squina

Publikováno v: PLoS ONE, Vol 8, Iss 7, p e70014 (2013)

Metagenomics has been widely employed for discovery of new enzymes and pathways to conversion of lignocellulosic biomass to fuels and chemicals. In this context, the present study reports the isolation, recombinant expression, biochemical and structu

Externí odkaz: https://doaj.org/article/6ba7edef13b94d51aa5fc11616cb4f8e

Identification of a cold-adapted and metal-stimulated β-1,4-glucanase with potential use in the extraction of bioactive compounds from plants

Autor: Ricardo Rodrigues de Melo, Letícia Maria Zanphorlin, Plínio Salmazo Vieira, Mário T. Murakami, Gabriela F. Persinoti, Evandro Antônio de Lima, Roberto Ruller, Amanda Silva de Sousa, Priscila Oliveira de Giuseppe

Publikováno v: International Journal of Biological Macromolecules. 166:190-199

Cold-adapted endo-β-1,4-glucanases hold great potential for industrial processes requiring high activity at mild temperatures such as in food processing and extraction of bioactive compounds from plants. Here, we identified and explored the specific

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a4809374e3cccfc46210bb12c102f0
https://doi.org/10.1016/j.ijbiomac.2020.10.137

Luciferase isozymes from the Brazilian Aspisoma lineatum (Lampyridae) firefly: origin of efficient pH-sensitive lantern luciferases from fat body pH-insensitive ancestors

Autor: Atílio Tomazini, Mariele C. Carvalho, Danilo T. Amaral, Vadim R. Viviani, Mário T. Murakami

Publikováno v: Photochemical & Photobiological Sciences. 19:1750-1764

Firefly luciferases usually emit green-yellow bioluminescence at physiological pH values. However, under acidic conditions, in the presence of heavy metals and, at high temperatures they emit red bioluminescence. To understand the structural origin o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3c22d5f482d62b321e0415be413daad
https://doi.org/10.1039/d0pp00272k

Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

Autor: Camila R. Santos, Evandro Antônio de Lima, Sinkler E. T. Gonzalez, Fabio C. Gozzo, Lucelia Cabral, Rosa Lorizolla Cordeiro, Plínio Salmazo Vieira, Pedro A. C. R. Costa, Mariane Noronha Domingues, Marcele P. Martins, Fernanda Mandelli, Renan A. S. Pirolla, Munir S. Skaf, Erica T. Prates, Beatriz P. Souza, Mário T. Murakami, Atílio T. Junior, Thamy Lívia Ribeiro Corrêa, Gabriela Felix Persinoti

Publikováno v: Nature Chemical Biology. 16:920-929

The fundamental and assorted roles of β-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. In this work, the selectivity and modes of act

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c85effa75822f63f87975ac611602d7a
https://doi.org/10.1038/s41589-020-0554-5

Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans

Autor: Marcele P. Martins, Mariana A. B. Morais, Gabriela F. Persinoti, Rafael H. Galinari, Li Yu, Yoshihisa Yoshimi, Fernanda B. Passos Nunes, Tatiani B. Lima, Shayla F. Barbieri, Joana L. M. Silveira, Vincent Lombard, Nicolas Terrapon, Paul Dupree, Bernard Henrissat, Mário T. Murakami

Publikováno v: Martins, M P, Morais, M A B, Persinoti, G F, Galinari, R H, Yu, L, Yoshimi, Y, Passos Nunes, F B, Lima, T B, Barbieri, S F, Silveira, J L M, Lombard, V, Terrapon, N, Dupree, P, Henrissat, B & Murakami, M T 2022, ' Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans ', Acta Crystallographica Section D: Biological Crystallography, vol. 78, no. 11, pp. 1358-1372 . https://doi.org/10.1107/S2059798322009561
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2022, 78 (11), pp.1358-1372. ⟨10.1107/S2059798322009561⟩

International audience; Glycoside hydrolase family 5 (GH5) harbors diverse substrate specificities and modes of action, exhibiting notable molecular adaptations to cope with the stereochemical complexity imposed by glycosides and carbohydrates such a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffb34d1fd43c9a2230e1d9ded097768a
https://orbit.dtu.dk/en/publications/b865f68e-b3c0-4417-8051-6100ce204459