Results 31 to 40 of about 132,531 (238)

Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion

Biotechnology for Biofuels, 2018
Background Lignocellulose is highly recalcitrant to enzymatic deconstruction, where the recalcitrance primarily results from chemical linkages between lignin and carbohydrates.
Jenny Arnling Bååth, Scott Mazurkewich, Rasmus Meland Knudsen, Jens-Christian Navarro Poulsen, Lisbeth Olsson, Leila Lo Leggio, Johan Larsbrink   +6 more
doaj   +1 more source

Metagenomics approach to identify lignocellulose-degrading enzymes in the gut microbiota of the Chinese bamboo rat cecum

Electronic Journal of Biotechnology, 2021
Background: Lignocellulose is considered a renewable organic material, but the industrial production of biofuel from lignocellulose is challenging because of the lack of highly active hydrolytic enzymes.
Ding-Ping Bai, Xin-Yu Lin, Yu-Qiong Hu, Zhen-Zhen Chen, Lu Chen, Yi-Fan Huang, Xiao-Hong Huang, Jian Li   +7 more
doaj   +1 more source

Carbohydrate-Active Enzymes [PDF]

, 2020
Jean-Luc Wertz, Magali Deleu, Séverine Coppée, Aurore Richel   +3 more
  +5 more sources

Crystal structure and functional characterization of an oligosaccharide dehydrogenase from Pycnoporus cinnabarinus provides insights into fungal breakdown of lignocellulose

Biotechnology for Biofuels, 2021
Background Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the “Auxiliary Activity” family 3 (AA3) of the Carbohydrate-Active enZymes ...
Gabriele Cerutti, Elena Gugole, Linda Celeste Montemiglio, Annick Turbé-Doan, Dehbia Chena, David Navarro, Anne Lomascolo, François Piumi, Cécile Exertier, Ida Freda, Beatrice Vallone, Eric Record, Carmelinda Savino, Giuliano Sciara   +13 more
doaj   +1 more source

CAZac: an activity descriptor for carbohydrate-active enzymes [PDF]

Nucleic Acids Research
Abstract The Carbohydrate-Active enZYme database (CAZy; www.cazy.org) has been providing the reference classification of carbohydrate-active enzymes (CAZymes) for >30 years. Based on literature survey, the sequence-based families of CAZymes are enriched with functional data by using the International Union of Biochemistry and ...
Lombard, Vincent, Henrissat, Bernard, Garron, Marie-Line   +2 more
openaire   +4 more sources

Modelling Reactions Catalysed by Carbohydrate-Active Enzymes [PDF]

, 2014
Abstract Carbohydrate polymers are ubiquitous in biological systems and their roles are highly diverse, ranging from energy storage over mechanical stabilisation to mediating cell-cell or cell-protein interactions. The functional diversity is mirrored by a chemical diversity that results from the high flexibility of how different sugar ...
Kartal, Önder, Ebenhöh, Oliver
openaire   +1 more source

Cazypedia : carbohydrate-active enzymes, an introduction [PDF]

Glycobiology, 2011
CAZypedia is an online, community-driven effort to assemble a comprehensive encyclopedia of the enzymes and binding proteins involved in the synthesis and degradation of complex carbohydrates. An evolving encyclopedia of carbohydrate-active enzymes – ”CAZymes” CAZypedia is inspired by, and closely connected with, the actively curated CAZy Database (www.
Abbott Wade, Alber Orly, Bayer Ed, Berrin JeanGuy, Boraston Alisdair, Brumer Harry, Brzezinski Ryszard, Clarke Anthony, CobucciPonzano Beatrice, Cockburn Darrell, Coutinho Pedro, Czjzek Mirjam, Dassa Bareket, Davies Gideon John, Eijsink Vincent, Eklof Jens, Felice Alfons, FickoBlean Elizabeth, Pincher Geoff, Fontaine Thierry, Fujimoto Zui, Fujita Kiyotaka, Fushinobu Shinya, Gilbert Harry, Gloster Tracey, GoddardBorger Ethan, Greig Ian, Hehemann JanHendrik, Hemsworth Glyn, Henrissat Bernard, Hidaka Masafumi, HurtadoGuerrero Ramon, Igarashi Kiyohiko, Ishida Takuya, Janecek Stefan, Jongkees Seino, Juge Nathalie, Kaneko Satoshi, Katayama Takane, Kitaoka Motomitsu, Konno Naotake, Kracher Daniel, Kulminskaya Anna, van Bueren Alicia Lammerts, Larsen Sine, Lee Junho, Linder Markus, LoLeggio Leila, Ludwig Roland, Luis Ana, Maksimainen Mirko, Mark Brian, McLean Richard, Michel Gurvan, Michel Gurvan, Montanier Cedric, Moracci Marco, Mori Haruhide, Nakai Hiroyuki, Nerinckx Wim, Ohnuma Takayuki, Pickersgill Richard, Piens Kathleen, Pons Tirso, Rebuffet Etienne, Reilly Peter, RemaudSimeon Magali, Rempel Brian, Robinson Kyle, Rose David, Rouvinen Juha, Saburi Wataru, Sakamoto Yuichi, Sandgren Mats, Shaikh Fathima, Shoham Yuval, St John Franz, Stahlberg Jerry, Suits Michael, Sulzenbacher Gerlind, Sumida Tomomi, Suzuki Ryuichiro, Svensson Birte, Taira Toki, Taylor Ed, Tonozuka Takashi, Urbanowicz Breeanna, VaajeKolstad Gustav, Van den Ende Wim, Varrot Annabelle, Versluys Maxime, Vincent Florence, Vocadlo David, Wakarchuk Warren, Wennekes Tom, Williams Rohan, Williams Spencer, Wilson David, Withers Stephen, Yaoi Katsuro, Yip Vivian, Zhang Ran   +101 more
openaire   +9 more sources

High-quality draft genome sequence of Aquidulcibacter paucihalophilus TH1–2T isolated from cyanobacterial aggregates in a eutrophic lake

Standards in Genomic Sciences, 2017
Aquidulcibacter paucihalophilus TH1–2T is a member of the family Caulobacteraceae within Alphaproteobacteria isolated from cyanobacterial aggregates in a eutrophic lake. The draft genome comprises 3,711,627 bp and 3489 predicted protein-coding genes. The
Haiyuan Cai, Yonghui Zeng
doaj   +1 more source

Metagenomic analysis fecal microbiota of dysentery-like diarrhoea in a pig farm using next-generation sequencing

Frontiers in Veterinary Science, 2023
Porcine enteric diseases including swine dysentery involves a wide range of possible aetiologies and seriously damages the intestine of pigs of all ages.
Xi Chen, Qing Guo, Ying-Ying Li, Tie-Ying Song, Jun-Qing Ge   +4 more
doaj   +1 more source

Systems approaches to predict the functions of glycoside hydrolases during the life cycle of Aspergillus niger using developmental mutants ∆brlA and ∆flbA.

PLoS ONE, 2015
BackgroundThe filamentous fungus Aspergillus niger encounters carbon starvation in nature as well as during industrial fermentations. In response, regulatory networks initiate and control autolysis and sporulation.
Jolanda M van Munster, Benjamin M Nitsche, Michiel Akeroyd, Lubbert Dijkhuizen, Marc J E C van der Maarel, Arthur F J Ram   +5 more
doaj   +1 more source