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1 |
Material Type: Artigo
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Gene Cloning, Functional Expression, and Characterization of a Novel GH46 Chitosanase from Streptomyces avermitilis (SaCsn46A)Guo, Jing ; Wang, Yi ; Gao, Wenjun ; Wang, Xinrou ; Gao, Xin ; Man, Zaiwei ; Cai, Zhiqiang ; Qing, QingApplied biochemistry and biotechnology, 2022-02, Vol.194 (2), p.813-826 [Periódico revisado por pares]New York: Springer USTexto completo disponível |
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Material Type: Artigo
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Biochemical Characterization of the First Fungal Glycoside Hydrolyase Family 3 β‑N‑Acetylglucosaminidase from Rhizomucor mieheiYang, Shaoqing ; Song, Shuang ; Yan, Qiaojuan ; Fu, Xing ; Jiang, Zhengqiang ; Yang, XinbinJournal of agricultural and food chemistry, 2014-06, Vol.62 (22), p.5181-5190 [Periódico revisado por pares]United States: American Chemical SocietyTexto completo disponível |
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Material Type: Artigo
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An Acid-Adapted Endo-α-1,5-l-arabinanase for Pectin ReleasingLang, Chong ; Yang, Rujian ; Yang, Ying ; Gao, Bei ; Zhao, Li ; Wei, Wei ; Wang, Hualei ; Matsukawa, Shingo ; Xie, Jingli ; Wei, DongzhiApplied biochemistry and biotechnology, 2016-11, Vol.180 (5), p.900-916 [Periódico revisado por pares]New York: Springer USTexto completo disponível |
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Material Type: Artigo
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Structure–function analysis of Gynuella sunshinyii chitosanase uncovers the mechanism of substrate binding in GH family 46 membersWang, Yani ; Qin, Zhen ; Fan, Liqiang ; Zhao, LimingInternational journal of biological macromolecules, 2020-12, Vol.165 (Pt B), p.2038-2048 [Periódico revisado por pares]Netherlands: Elsevier B.VTexto completo disponível |
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Material Type: Artigo
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Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68Pons, Tirso ; Naumoff, Daniil G. ; Martínez-Fleites, Carlos ; Hernández, LázaroProteins, structure, function, and bioinformatics, 2004-02, Vol.54 (3), p.424-432 [Periódico revisado por pares]Hoboken: Wiley Subscription Services, Inc., A Wiley CompanyTexto completo disponível |
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Material Type: Artigo
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Heterologous expression of a Penicillium purpurogenum exo-arabinanase in Pichia pastoris and its biochemical characterizationMardones, Wladimir ; Callegari, Eduardo ; Eyzaguirre, JaimeFungal biology, 2015-12, Vol.119 (12), p.1267-1278 [Periódico revisado por pares]Netherlands: Elsevier LtdTexto completo disponível |
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Material Type: Artigo
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Glycoside hydrolases as components of putative carbohydrate biosensor proteins in Clostridium thermocellumBahari, Liat ; Gilad, Yuval ; Borovok, Ilya ; Kahel-Raifer, Hamutal ; Dassa, Bareket ; Nataf, Yakir ; Shoham, Yuval ; Lamed, Raphael ; Bayer, Edward AJournal of industrial microbiology & biotechnology, 2011-07, Vol.38 (7), p.825-832 [Periódico revisado por pares]Berlin/Heidelberg: Springer-VerlagTexto completo disponível |
8 |
Material Type: Artigo
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Heterologous expression and characterization of α-l-arabinofuranosidase 4 from Penicillium purpurogenum and comparison with the other isoenzymes produced by the fungusRavanal, María Cristina ; Eyzaguirre, JaimeFungal biology, 2015-07, Vol.119 (7), p.641-647 [Periódico revisado por pares]Netherlands: Elsevier LtdTexto completo disponível |
9 |
Material Type: Artigo
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An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structureLing, Naomi X.-Y. ; Lee, Joanne ; Ellis, Miriam ; Liao, Ming-Long ; Mau, Shaio-Lim ; Guest, David ; Janssen, Peter H. ; Kováč, Pavol ; Bacic, Antony ; Pettolino, Filomena A.Carbohydrate research, 2012-05, Vol.352, p.70-81 [Periódico revisado por pares]Netherlands: Elsevier LtdTexto completo disponível |
10 |
Material Type: Artigo
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Investigating the binding of β-1,4-galactan to Bacillus licheniformis β-1,4-galactanase by crystallography and computational modelingLe Nours, Jérôme ; De Maria, Leonardo ; Welner, Ditte ; Jørgensen, Christel T. ; Christensen, Lars L. H. ; Borchert, Torben V. ; Larsen, Sine ; Lo Leggio, LeilaProteins, structure, function, and bioinformatics, 2009-06, Vol.75 (4), p.977-989 [Periódico revisado por pares]Hoboken: Wiley Subscription Services, Inc., A Wiley CompanyTexto completo disponível |