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Fusarium solani, cutinase

Humicola lanuginosa Pseudomonas aeruginosa Fusarium solani cutinase Rabbit gastric... [Pg.293]

Lipid-degrading esterase Fusarium solani cutinase... [Pg.4]

Martinez, C., de Geus, P., Lauwereys, M., Matthyssens, G. and Cambillau, C. (1992) Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356, 615-618... [Pg.191]

Fusarium solani cutinase CO2 hexanol + hexanoic acid 130 bar 45 °C [31]... [Pg.421]

Longhi S, Czjzek M, Lamizin V, Nicolas A, Cambillau C (1997) Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase stereochemical analysis. J Mol Biol... [Pg.118]

Sereti Stamatis, Kolisis [67] Fusarium solani cutinase stability of enzymes Stability, reactivity. CO2 ... [Pg.806]

Woloshuk CP (1986) Cutinase of Fusarium solani f. sp. pisi mechanism of induction and relatedness to other Fusarium species. PhD thesis, Washington State University, Pullman WA... [Pg.50]

Hydrolysis oftricaprylin in trimethylpentane by Fusarium solani pisi recombinant cutinase immobilized on various zeolites (NaA, NaX, NaY, LZY-82, dealuminated Y) was investigated in order to assess the effect of chemical composition (Si/Al ratio), hydrophilic character and acidity on the catalytic activity [221]. The adsorption of... [Pg.469]

DANTZIG Cutinase-Defective Mutant o/Fusarium solani... [Pg.401]

A reduction in cutinase production should result in the PNB-1 mutant being less virulent. The pathogenesis of the two strains were evaluated in a pea stem bioassay developed by Kolattukudy and coworkers in which infection by Fusarium solani results in wound formation within three days on the epicotyl of pea sedlings (15). The virulence of T-8 had previously been shown to be reduced in this assay by the addition of inhibitors of cutinase or by rabbit anticutinase antibodies (15-18), indicating that cutinase played an important role in pathogenesis. When the cutinase-defective mutant was evaluated in the bioassay, the mutant exhibited a 55% reduction (p < 0.05) in virulence compared with the T-8 parental strain and the addition of purified cutinase at 1 mg/ml to the mutant enhanced wound formation to 80% of that of the parent (p > 0.5). These data further support the notion that the mutant was defective in cutinase. [Pg.407]

Fig. 2 Electrostatic surface rendering of Aspergillus oryzae (left) and Fusarium solani (right) cutinases. The solid density illustrates the groove on the surface proximal to the active site [53]... Fig. 2 Electrostatic surface rendering of Aspergillus oryzae (left) and Fusarium solani (right) cutinases. The solid density illustrates the groove on the surface proximal to the active site [53]...
Lin TS, Kolattukudy PE (1978) Induction of a biopolyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani f sp. pisi. J Bacteriol 133 942-951... [Pg.125]

Figure 7.8 A differential scanning calorimeter investigation of the triglyceride lipase cutinase from Fusarium solani pish at pH 8.5. The buffer 20 mM glycine (flat trace) and the protein solution in the glycine buffer have been studied separately. A distinct signal at about 55 degree C defines the thermal denaturation of the enzyme. These scans were... Figure 7.8 A differential scanning calorimeter investigation of the triglyceride lipase cutinase from Fusarium solani pish at pH 8.5. The buffer 20 mM glycine (flat trace) and the protein solution in the glycine buffer have been studied separately. A distinct signal at about 55 degree C defines the thermal denaturation of the enzyme. These scans were...
The cutinase from Fusarium solani pisii maintained its transesterification activity in [BMIm][BF4], [OMIm][PF6] and [BMIm][PF6] (in order of increasing activity) at aw=0.2 [59]. Candida rugosa lipase (CrL), which is generally much less tolerant of anhydrous media than other microbial lipases, has successfully been used in anhydrous as well as water-saturated ionic liquids [60, 61, 62, 63, 64, 65]. [Pg.232]

Cutinase from Fusarium solani Transesterification reactions Whole cells Parvaresh et al., 1992 [61] Lamare and Legoy,1995,1997 [39, 62]... [Pg.257]

Creveld, L.D., Meijberg, W., Berendsen, H.J., Pepermans, H.A. (2001). DSC studies of Fusarium solani pisi cutinase consequences for stability in the presence of surfactants. Biophys. Chem., 92(1-2), 65-75. [Pg.175]

Figure 3-22 Stereoscopic view of a section of the structure of cutinase from the fungus Fusarium solani determined to a resolution of 0.10 nm. The three amino acid residues shown are serine 120 (top), histidine 188, and aspartate 175 (lower left). The structure is presented as a contour map with a "wire mesh" drawn at a "cutoff" level of density equal to 1 a above the average, where a is the root mean square density of the entire map. The side chains of these three residues constitute the "catalytic triad" in the active site of this enzyme (see Chapter 12). At this resolution more than one conformation of a group may often be seen. For example, the gamma oxygen (OG) of S120 is seen in two positions, the major one being toward His 188. When the map is drawn with a lower contour level the N-H proton on His 188 that is hydrogen bonded to Asp 175 can also be seen.410 Courtesy of Christian Cambillau. Figure 3-22 Stereoscopic view of a section of the structure of cutinase from the fungus Fusarium solani determined to a resolution of 0.10 nm. The three amino acid residues shown are serine 120 (top), histidine 188, and aspartate 175 (lower left). The structure is presented as a contour map with a "wire mesh" drawn at a "cutoff" level of density equal to 1 a above the average, where a is the root mean square density of the entire map. The side chains of these three residues constitute the "catalytic triad" in the active site of this enzyme (see Chapter 12). At this resolution more than one conformation of a group may often be seen. For example, the gamma oxygen (OG) of S120 is seen in two positions, the major one being toward His 188. When the map is drawn with a lower contour level the N-H proton on His 188 that is hydrogen bonded to Asp 175 can also be seen.410 Courtesy of Christian Cambillau.
Hydrolytic degradation of poly(e-CL)/PLLA block copolyester at pH 7.4 and 37 °C over a 5-week period is controlled by the initial crystallinity of the poly(e-CL) and its overall composition. The rate of degradation increased with increasing PLLA content [203 ]. Microorganisms, such as Fusarium solani and Fusarium moniliforme, that secrete poly(e-CL) depolymerase (cutinase), were more effective with those polymers that had longer poly(e-CL) sequence lengths [218]. The... [Pg.32]

Fusarium solani pisi cutinase (enantioselective) Gliocladium roseum (enantioselective) Humicola lanuginosa (enantioselective)... [Pg.1962]

Cutinase Fusarium solani PET Textile fibers, vascular Araujo et al. [Pg.96]

Purdy, R.E. and Kolattukudy, P.E. 1975. Hydrolysis of plant cutin by plant pathogens purification, amino acids composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry, 14 2824-31. [Pg.103]

An MD study of an enzyme, the serine protease cutinase from Fusarium solani pisi, in [C4mim][PF6] and [C4mim][N03] was presented. The authors observed an enzyme structure that is dependent on the amount of water present in the IL [124], They showed that the enzyme is preferentially stabilized in [C4mim][PF6] at 5-10 wt% (weight of water over protein) water content at 298 K. [C4mim][PF6] rendered a more native-like enzyme structure at the same water content of 5—10 wt% as... [Pg.245]

R312 M. R. Egmond and J. De Vlieg, Fusarium Solani Pisi Cutinase , Biochimie, 2000, 82, 1015... [Pg.24]

Cutinase enzyme from Fusarium solani pisi, immobilized on a 4-A molecular sieve, catalyzes the transesterification of the R isomer of 1-phenyl-ethanol in the racemic mixture [Eq. (7), R = C2H5), giving the R ester and the S alcohol, both in essentially 100% e.e ... [Pg.469]


See other pages where Fusarium solani, cutinase is mentioned: [Pg.34]    [Pg.110]    [Pg.34]    [Pg.110]    [Pg.127]    [Pg.29]    [Pg.399]    [Pg.400]    [Pg.403]    [Pg.405]    [Pg.407]    [Pg.411]    [Pg.117]    [Pg.130]    [Pg.157]    [Pg.371]    [Pg.268]    [Pg.371]    [Pg.98]    [Pg.224]    [Pg.196]    [Pg.528]    [Pg.54]    [Pg.55]   
See also in sourсe #XX -- [ Pg.117 , Pg.119 ]




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