Fusarium solani pisi

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... 

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. 

Fusarium solani pisi cutinase (enantioselective) Gliocladium roseum (enantioselective) Humicola lanuginosa (enantioselective)... 

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... 

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

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 ... 

The potential of lipases and cutinases for the hydrolysis of vinyl acetate moieties (about 7%) in commercial PAN materials was assessed. Indeed it was shown that the commercial esterase Texazym PES and a cutinase from using Fusarium solani pisi were able to release acetate from PAN [97]. Furthermore it was demonstrated... 

Table 11.1-11. Lipase-catalyzed enantiotopos-differentiating hydrolysis of prochiral cyclic diol dialkanoates in aqueous solution (CCL Candida cylindracea lipase, PFL Pseudomonas jiuorescens lipase, MML Mucor miehei lipase, CVL Chromobacterium viscosum lipase, PPL pig pancreas lipase, MJL Mucor javanicus lipase, RSL Rhizopus sp. lipase, PCL Pseudomonas cepacia lipase, CCL, Ceotricum candidum lipase, ANL Aspergillus niger lipase, FSPC Fusarium solani pisi cutinase, CRL Candida rugosa lipase, CAL-B Candida antarctica B lipase, LIP Pseudomonas sp. lipase-Toyobo, RDL Rhizopus delemar lipase, MSL Mucor sp. lipase, CAL Candida antarctica lipase, not specified).

Later, this strategy was put into practice using another lipase [92], namely cutinase, a 21 kDa lipase isolated from the fungus Fusarium solani pisi lacking the usual lid found in most other lipases. The active site is accessible for hydrophilic or... 

Bandmann N, Collet E, Leijen J et al. (2000) Genetic engineering of the Fusarium solani pisi lipase cutinase for enhanced partitioning in PEG-phosphate aqueous two-phase system. J Biotechnol... 

Properties Fusarium solani pisi 1 11 Fusarium roseum culmorum Fusarium roseum sambucirnum Vlocladium consortiale Streptomyces scabies Helminthosporum sativum ... 

Another extracellular lipase, called cutinase , is produced by the plant-pathogenic microorganism Fusarium solani pisi for the hydrolysis of cutin - a wax ester which is excreted by plants in order to protect their leaves against microbial attack [488]. The enzyme has been purified to homogeneity [489] and has been made readily available by genetic engineering [490]. Up to now it has not been widely used for biotransformations of noimatural esters, but it certainly has a potential as a useful pure lipase for complementary piuposes [491]. 

Purdy RE, Kolattukudy PE (1973) Depolymerization of a hydroxy fatty-acid biopolymer, cutin, by an extracellular enzyme fl om Fusarium solani pisi—isolation and some properties of the enzyme. Arch Biochem Biophys 159 61-69... 

Purdy RE, Kolattukudy PE (1975) Hydrolysis of Plant Cuticle by Plant Pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi. Biochemistry 14 2823-2840... 

Typical biodegradants cutinase from Fusarium solani pisi Araujo, R Silva, C O Neill, A MIcaelo, N Guebitz, G Soares, C M Casal, M Cavaco-Paulo, A, J. Biotechnol., 128, 849-57, 2007. 

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. 

Cutinase was purified and characterized from the extracellular fluid of cutin-grown Fusarium solani pisi (3, )- Since then, cutinase has been purified from a variety of pathogenic fungi (5>6). 

Figure k The nucleotide sequence of cutinase gene from Fusarium solani pisi. Southern blots show that this isolate contains another copy of the gene. However, the copy shown above is completely homologous with the cloned cDNA which would code for a protein with the primary structure that matches the major cutinase isozyme secreted by the fungus. 

Figure S - Induction of cutinase in the spores of Fusarium solani pisi by cutin hydrolysate and monomer fractions isolated from it by thin-layer chromatorgraphy. Paranitropheny1 butyrate (PNB) hydrolyzing activity of the medium was measured after 1, 3 or 6 hours of incubation.

Figure 6 Induction of cutinase in Fusarium solani pisi by cutin hydrolysate or 10,16-dihydroxy-Cjg acid isolated from it. On the left, the levels of immunological1y measured cutinase protein and the spectro-photometrically measured catalytic activity are shown. On the right, the levels of cutinase transcripts as measured by dot blot assays with P-labeled cutinase cDNA are shown. B indicates buffer containing no cutin.

A soluble epoxide hydrolase from soybeans (sbEH) hydrolyzed 3.26 to the (9R,10R)-diol in 80% e.e. at 50% conversion [153]. However, in a subsequent paper [40], the same authors report that the diol was formed in more than 99% e.e. Compound 3.26 was converted to the same (9R,10R)-diol by mEH but with significantly reduced e.e. Epoxy fatty acid 3.27 was claimed to undergo cis-hydrolysis by the fungus Fusarium solani pisi with concomitant retention of configuration but attempts to explain this extremely unusual phenomenon remain rather speculative [97] (Fig. 7, Table 7). 

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