Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.10.3.2 (laccase)
 4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This report represents the conclusions of a Joint FAO/WHO Expert Committee convened to evaluate the safety of various food additives, with a view to recommending acceptable daily intakes (ADIs) and to prepare specifications for the identity and purity of food additives. The first part of the report contains a general discussion of the principles governing the toxicological evaluation of food additives (including flavouring agents) and contaminants, assessments of intake, and the establishment and revision of specifications for food additives. A summary follows of the Committee's evaluations of toxicological and intake data on various specific food additives (alpha-amylase from Bacillus lichenformis containing a genetically engineered alpha-amylase gene from B. licheniformis, annatto extracts, curcumin, diacetyl and fatty acid esters of glycerol, D-tagatose, laccase from Myceliophthora thermophila expressed in Aspergillus oryzae, mixed xylanase, beta-glucanase enzyme preparation produced by a strain of Humicola insolens, neotame, polyvinyl alcohol, quillaia extracts and xylanase from Thermomyces lanuginosus expressed in Fusarium venenatum), flavouring agents, a nutritional source of iron (ferrous glycinate, processed with citric acid), a disinfectant for drinking-water (sodium dichloroisocyanurate) and contaminants (cadmium and methylmercury). Annexed to the report are tables summarizing the Committee's recommendations for ADIs of the food additives, recommendations on the flavouring agents considered, and tolerable intakes of the contaminants considered, changes in the status of specifications and further information requested or desired.
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PMID:Evaluation of certain food additives and contaminants. 1535 33

Sugarcane bagasse was pretreated with the white-rot fungus Ceriporiopsis subvermispora for 30 d of incubation. The solid-state fermentation of 800 g of bagasse was carried out in 20-L bioreactors with an inoculum charge of 250 mg of fungal mycelium/kg of bagasse. The oxidative enzymes manganese peroxidase (MnP), lignin peroxidase (LiP), and laccase (Lac) and the hydrolytic enzyme xylanase (Xyl) were measured by standard methods and related to the fungus's potential for delignification. Among the lignocellulolytic assayed enzymes, Xyl was detected in larger quantity (4478 IU/kg), followed by MnP (236 IU/kg). LiP and Lac were not detected. The results of chemical analysis and mass component loss showed that C. subvermispora was selective to lignin degradation. Pretreated sugarcane bagasse and control pulps were obtained by soda/anthraquinone (AQ) pulping. Pulp yields, kappa number, and viscosity of all pulps were determined by chemical analysis of the samples. Yields of soda/AQ ranged from 46 to 54%, kappa numbers were 15-25, and the viscosity ranged from 3.6 to 7 cP for pulps obtained from pretreated sugarcane bagasse.
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PMID:Ceriporiopsis subvermispora used in delignification of sugarcane bagasse prior to soda/anthraquinone pulping. 1592 Feb 73

Two wood-dwelling ascomycetes, Xylaria hypoxylon and Xylaria polymorpha, were isolated from rotting beech wood. Lignin degradation was studied following the mineralization of a synthetic [formula: see text]-labelled lignin in solid and liquid media. Approximately 9% of the synthetic lignin was mineralized by X. polymorpha during the growth on beech wood meal, and the major fraction (65.5%) was polymerized into water- and dioxan-insoluble material. Both fungi produced laccase (up to 1,200 U l-1) in an agitated complex medium based on tomato juice; peroxidase activity (<80 U l-1) was only detected for X. polymorpha in soybean meal suspension. The enzymatic attack of X. polymorpha on beech wood resulted in the formation of three fractions of water-soluble lignocellulose fragments with molecular masses of 200, 30 (major fraction) and 3 kDa, as demonstrated by high-performance size exclusion chromatography. This fragment pattern differs considerably from that of the white-rot fungus Bjerkandera adusta, which preferentially released smaller lignocellulose fragments (0.8 kDa). The finding that X. polymorpha produced large lignocellulose fragments, along with the fact that high levels of hydrolytic enzymes (esterase 630 U l-1, xylanase 120 U l-1) were detected, indicates the cleavage of bonds between the lignin and hemicellulose moieties.
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PMID:Mineralization of 14C-labelled synthetic lignin and extracellular enzyme activities of the wood-colonizing ascomycetes Xylaria hypoxylon and Xylaria polymorpha. 1602 87

The effects of xylanase pretreatment of high lignin content softwood (SW) kraft pulp on subsequent pulp treatment with laccase in combination with gallic acid were investigated. Although xylanase pretreatment was ineffective in enhancing the laccase-facilitated biografting of gallic acid to kraft fibers, it was beneficial for subsequent treatment with laccase exclusively. Treating pulp fibers with xylanase followed by laccase provided a collective 25% and 46% increase in dry and wet tensile strength properties, respectively.
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PMID:Modification of high-lignin kraft pulps with laccase. Part 2. Xylanase-enhanced strength benefits. 1608 Jul 15

To evaluate the potential of using the enzymes from spent mushroom compost (SMC) as an industrial enzyme, the production of alpha-amylase, cellulase, beta-glucosidase, laccase, and xylanase was determined from the SMC of four edible mushroom species (Pleurotus ostreatus, Lentinula edodes, Flammulina velutipes and Hericium erinaceum). Among the tested SMC, the SMC of L. edodes showed the highest enzyme activity in alpha-amylase (229 nkat/g), cellulase (759 nkat/g) and beta-glucosidase (767 nkat/g) in 0.5% Triton X-100, and that of P. ostreatus showed the highest activity in laccase (1452 nkat/g) in phosphate-buffered 0.2% Triton X-100. The highest xylanase activity (119 nkat/g) was found in the SMC of F. velutipes.
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PMID:Detection and recovery of hydrolytic enzymes from spent compost of four mushroom species. 1611 Sep 12

Lentinus edodes and Pleurotus species from various origins were compared for the first time for their ability to produce lignocellulolytic enzyme in solid-state (SSF) and submerged (SF) fermentation of various plant raw material. Fungi cultivation in identical culture conditions revealed wide differences among both species and strains of the same species. The yields of CMCase (62.3Uml(-1)), xylanase (84.1 U ml(-1)), FPA (5.9 U ml(-1)), and laccase (4103 Ul(-1)) are the best so far obtained with the strains of oyster mushrooms. The study pointed out that the nature of lignocellulosic material and the method of fungi cultivation are factors determining the expression of lignocellulolytic potential of fungi as well as the ratio of individual enzymes in enzyme complex. SSF of tree leaves is favorable for laccase and MnP secretion by the majority L. edodes and Pleurotus strains, whereas SF provides better production of hydrolytic enzymes.
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PMID:Lentinus edodes and Pleurotus species lignocellulolytic enzymes activity in submerged and solid-state fermentation of lignocellulosic wastes of different composition. 1735 Aug 27

Cross-linking enzymes generate covalent bonds in and between food biopolymers. These enzymes are interesting tools for tailoring dough and bread structures, as the characteristics of the biopolymers significantly determine the viscoelastic and fracture properties of dough and bread. In this study, the influence of oxidative cross-linking enzymes, tyrosinase from the filamentous fungus Trichoderma reesei and laccase from the white rot fungus Trametes hirsuta, on dough and bread were examined. Oxidation of low molecular weight phenolic model compounds of flour, cross-linking of gluten proteins, dough rheology, and bread making were characterized during or after the enzymatic treatments. In the dough and bread experiments, laccase and tyrosinase were also studied in combination with xylanase. Of the model compounds tyrosine, p-coumaric acid, caffeic acid, ferulic acid, and Gly-Leu-Tyr tripeptide, tyrosinase oxidized all except ferulic acid. Laccase was able to oxidize each of the studied compounds. The phenolic acids were notably better substrates for laccase than l-tyrosine. When the ability of the enzymes to cross-link isolated gliadin and glutenin proteins was studied by the SDS-PAGE analysis, tyrosinase was found to cross-link the gliadin proteins effectively, whereas polymerization of the gliadins by laccase was observed only when a high enzyme dosage and prolonged incubation were used. Examination of large deformation rheology of dough showed that both laccase and tyrosinase made doughs harder and less extensible, and the effects increased as a function of the enzyme dosage. In bread making, interestingly, the pore size of the breads baked with tyrosinase turned out to be remarkably larger and more irregular when compared to that of the other breads. Nevertheless, both of the oxidative enzymes were found to soften the bread crumb and increase the volume of breads, and the best results were achieved in combination with xylanase.
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PMID:Elucidating the mechanism of laccase and tyrosinase in wheat bread making. 1760 67

Tomato pomace and pectin were used as the sole carbon sources for the production of polygalacturonase from a strain of Coriolus versicolor in submerged culture. The culture of C. versicolor grown on tomato pomace exhibited a peak of polygalacturonase activity (1,427 U/l) on the third day of culture with a specific activity of 14.5 U/mg protein. The production of polygalacturonase by C. versicolor grown on pectin as a sole carbon source increased with the time of cultivation, reaching a maximum activity of 3,207 U/l of fermentation broth with a specific activity of 248 U/mg protein. The levels of different isoenzymes of polygalacturonase produced during the culture growth were analysed by native PAGE. Differential chromatographic behaviour of lignocellulosic enzymes produced by C. versicolor (i.e. polygalacturonase, xylanase and laccase) was studied on immobilized metal chelates. The effect of ligand concentration, pH, the length of spacer arm and the nature of metal ion were studied for enzyme adsorption on immobilized metal affinity chromatography (IMAC). The adsorption of these lignocellulosic enzymes onto immobilized metal chelates was pH-dependent since an increase in protein adsorption was observed as the pH was increased from 6.0 to 8.0. The adsorption of polygalacturonase as well as other enzymes to immobilized metal chelates was due to coordination of histidine residues which are available at the protein surface since the presence of imidazole in the equilibration buffer abolished the adsorption of the enzyme to immobilized metal chelates. A one-step purification of polygalacturonase from C. versicolor was devised by using a column of Sepharose 6B-EPI 30-IDA-Cu(II) and purified enzyme exhibited a specific activity of about 150 U/mg protein, final recovery of enzyme activity of 100% and a purification factor of about 10. The use of short spacer arm and the presence of imidazole in equilibration buffer exhibited a higher selectivity for purification of polygalacturonase on this column with a high purification factor. The purified enzyme preparation was analysed by SDS-PAGE as well as by "in situ" detection of enzyme activity.
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PMID:Production of polygalacturonase from Coriolus versicolor grown on tomato pomace and its chromatographic behaviour on immobilized metal chelates. 1825 72

Commercial mushroom tyrosinase contains other proteins, enzymes, carbohydrates, and phenolic material besides tyrosinase. Carbohydrate and phenolic material comprise a large percentage of the powder resuspensions derived from Agaricus bisporus. Enzyme assays identified the presence of tyrosinase, laccase, beta-glucosidase, beta-galactosidase, beta-xylosidase, cellulase, chitinase, xylanase, and mannanase in the commercial tyrosinase. Protein sequencing indicated the presence of tyrosinase, a lectin, and a putative mannanase as well as 10 unidentified protein/peptides in the commercial tyrosinase preparations. Characteristics of tyrosinase isoforms were similar in two different commercial tyrosinase sources. Inhibition studies indicated that I 50 values for some tyrosinase inhibitors were different when the crude powder was compared to a partially purified tyrosinase. The presence of these contaminants has the potential to affect studies using commercial tyrosinase.
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PMID:Enzyme, protein, carbohydrate, and phenolic contaminants in commercial tyrosinase preparations: potential problems affecting tyrosinase activity and inhibition studies. 1850 Aug 13

The effects of Trametes hirsuta laccase and Pentopan Mono BG xylanase and their combination on oat, wheat, and mixed oat-wheat doughs and the corresponding breads were investigated. Laccase treatment decreased the content of water-extractable arabinoxylan (WEAX) in oat dough due to oxidative cross-linking of feruloylated arabinoxylans. Laccase treatment also increased the proportion of water-soluble polysaccharides (WSNSP) apparently due to the beta-glucanase side activity present in the laccase preparation. As a result of the laccase treatment, the firmness of fresh oat bread was increased. Xylanase treatment doubled the content of WEAX in oat dough and slightly increased the amount of WSNSP. Increased stiffness of the dough and firmness of the fresh bread were detected, probably because of the increased WEAX content, which decreased the amount of water available for beta-glucan. The combination of laccase and xylanase produced slight hydrolysis of beta-glucan by the beta-glucanase side activity of laccase and enhanced the availability of AX for xylanase with concomitant reduction of the amount and molar mass of WSNSP. Subsequently, the volume of oat bread was increased. Laccase treatment tightened wheat dough, probably due to cross-linking of WEAX to higher molecular weight. In oat-wheat dough, laccase slightly increased the proportion of WSNSP between medium to low molecular weight and increased the specific volume of the bread. Xylanase increased the contents of WEAX and WSNSP between medium to low molecular weight in oat-wheat dough, which increased the softness of the dough, as well as the specific volume and softness of the bread. The results thus indicate that a combination of laccase and xylanase was beneficial for the textures of both oat and oat-wheat breads.
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PMID:Effects of laccase and xylanase on the chemical and rheological properties of oat and wheat doughs. 1855 94


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