Thermobifida fusca

Thermobifida fusca, belonging to the Actinomycetales, produces three closely related siderophores, namely, the fuscachelins (92). Fuscachelin B starts with the sequence DHB - Arg-Gly-Gly-Ser, which is bound to the hydroxylated N -amino group of Om. Its N -amino group (the carboxyl group is free) is bound to the C-terminus of the sequence Gly-Gly-Arg-DHB (32). Fuscachelin A is considered to be the genuine metabolite, with B and C degradation products. [Pg.19]

Dimise EJ, Widboom PF, Bruner SD (2008) Structure Elucidation and Biosynthesis of Fuscachelins, Peptide Siderophores from the Moderate Thermophile Thermobifida fusca. Proc Natl Acad Sci USA 105 15311... [Pg.58]

Integration of Computer Modeling and Initial Studies of Site-Directed Mutagenesis to Improve Cellulase Activity on Cel9A from Thermobifida fusca... [Pg.287]

Torres DE Pazmino, Baas BJ, Janssen DB, Fraaije MW. Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca. Biochemistry 2008 47 4082-4093. [Pg.510]

Cutinase Thermobifida fusca Release of oligomers, hydrophilicity, XPS, Maldi-Tof, K/S values after dying [24, 37, 54, 55, 57]... [Pg.373]

The mechanisms of a few Baeyer-Villiger monooxygenases have been studied in detail. The catalytic cycles of cyclohexanone monooxygenase from Acinetobacter NCIB 9871 and phenylacetone monooxygenase from Thermobifida fusca are similar to each other and to that of As with FMO, wasteful and toxic... [Pg.85]

Among the attempts being made are the use of hydrolases from the actinomycete Thermobifida fusca [54, 55], hydrolytic enzymes such as lipases [56], and micro-organisms of the genus Rhizobium [57]. [Pg.112]

Irwin DC, Zhang S, Wilson DB. (2000). Cloning, expression and characterization of a family 48 exocellulase, Cel48a, from Thermobifida fusca. Eur J Biochem, 267(16), 4988 997. [Pg.99]

Abstract The functionalization of synthetic polymers such as poly(ethylene terephthalate) to improve their hydrophilicity can be achieved biocatalytically using hydrolytic enzymes. A number of cutinases, lipases, and esterases active on polyethylene terephthalate have been identified and characterized. Enzymes from Fusarium solani, Thermomyces insolens, T. lanuginosus, Aspergillus oryzae, Pseudomonas mendocina, and Thermobifida fusca have been studied in detail. Thermostable biocatalysts hydrolyzing poly(ethylene terephthalate) are promising candidates for the further optimization of suitable biofunctionalization processes for textile finishing, technical, and biomedical applications. [Pg.97]

Thermobifida fusca Fabric, fibers HPLC, UV-spectroscopy, dye assay, water absorption tests, gravimetric analysis SEM, AFM, XPS Hydrolysis, increased hydrophilicity, improved dye uptake, weight loss [2, 3, 11, 26, 27, 31, 38]... [Pg.100]

Billig S, Oeser T, Birkemeyer C, Zimmermann W (2010) Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3. Appl Microbiol Biotech 87 1753-1764... [Pg.116]

Chen S, Su L, Billig S, Zimmermann W, Chen J, Wu J (2010) Biochemical characterization of the cutinases from Thermobifida fusca. J Mol Catal B Enzym 63 121-127... [Pg.116]

Feuerhack A, Alisch-Mark M, Kisner A, Pezzin SH, Zimmermann W, Andreaus J (2008) Biocatalytic surface modification of knitted fabrics made of poly (ethylene terephthalate) with hydrolytic enzymes from Thermobifida fusca KW3b. Biocatal Biotransform 26 357-364... [Pg.117]

Lykidis A, Mavromatis K, Ivanova I, Anderson I, Land M, DiBartolo G, Martinez M, Lapidus A, Lucas S, Copeland A, Richardson P, Wilson DB, Kyrpides N (2007) Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX. J Bacteriol 189 2477-2486... [Pg.118]

Deng, Y., and S. Fong. 2010. Influence of Culture Aeration on the Cellulase Activity of Thermobifida Fusca. Applied Microbiology and Biotechnology 85 (4) 965-974. [Pg.16]

Two of the most active strains were identified and belong both to the genus Thermobifida and are consistent with the Thermobifida fusca taxon. [Pg.346]

A copolyester depolymerising extracellular enzyme was isolated and characterised from the strain Thermobifida fusca DSM 43793. The enzyme exhibits a homology of 65% with a triacylglycerol-lipase from Streptomyces sp. (strain Mil) [94], has a molar mass of approximately 27,000 D and an optimal temperature for hydrolysing BTA-copolyesters of about 60 °C. The identification of the enzyme having a lipaselike structure is in accordance with the observation that many lipases are able to attack polyesters [2, 86, 95] and are probably also predominantly responsible for the microbial induced depolymerisation of synthetic polyesters in nature. [Pg.347]

PPT) were treated with polyesterases from Thermomyces lanuginosus, Penicillium citrinum, Thermobifida fusca and Fusarium solani pisi, and the cutinase from Thermobifida fusca was found to release the highest amounts of hydrolysis prodncts from PPT materials [37]. The Thermobifida fusca enzyme hydrolysed both PPT fibres and films, whereas the lipase from Thermomyces lanuginosus was only able to hydrolyse the fibres. Due to the higher surface area, fibres are more easily attacked by enzymes than films. [Pg.168]

Bloois EV, Pazmiho DET, Winter RT, Fraaije MW (2010) A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfrimily. Appl Microbiol Biotechnol... [Pg.235]

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