Wanius José Garcia da Silva

• Abstract

  The lignocellulosic biomass is the most abundant renewable carbon source on the planet, with several biotechnological applications, including the conversion of cellulose into ethanol. The cellulosome is a modular multi-enzymatic complex with high molecular mass present in anaerobic microorganisms and which presents a high efficiency in the degradation of cellulose. As a comparison, the ce…

  Functional and structural study of a cellulosomal cellulase from anaerobic fungus and its dockerin-scaffoldin interaction, AP.R

• Abstract

  The lytic polysaccharides monooxygenases (LPMOs) constitute a new class of metalloenzymes copper-dependent involved in the biodegradation of recalcitrant polysaccharides, such as cellulose, via oxidative mechanisms. These metalloenzymes have been identified and characterized only in the last ten years and have attracted the interest of researchers due to its great potential of biotechnolo…

  Studies of the mode of action of two lytic polysaccharide monooxygenases from insect (order: isoptera): molecular structure, bioinorganic chemistry and biotechnological applications, AP.R

• Abstract

  The enzymatic hydrolysis of cellulose to glucose requires mainly three types of cellulases working synergistically: endoglucanases, cellobiohydrolases and Beta-glucosidases. The endoglucanases and cellobiohydrolases are often inhibited by cellobiose. Thus, Betaglucosidases are important in terms of avoiding decreased hydrolysis rates of cellulose over time due to cellobiose accumulation. …

  Structural and functional analysis of the fibronectin type III domain (FnIII) of one beta-glucosidase belonging to the family GH3: interaction with large polymeric substrates and thermostability, AP.BIOEN.R

(Only some records are available in English at this moment)

• Abstract

  The Lytic Polysaccharide Monooxygenases (LPMOs) are a new discovered class of enzymes that assist glycoside hydrolases in the degradation of recalcitrant polysaccharides through oxidant activity. This class of metalloenzymes presents great potential for biotechnological applications, mainly in the area of degradation of structural polysaccharides. LPMOs can be used as complements to incre…

  Periplasmic expression, purification and characterization of the inorganic biochemistry of an oxidative enzyme of the insect Bombyx mori (silkworm), BP.MS

• Abstract

  Vanillin is one of the most important flavoring agents in the world, and widely used inthe food industry as in cakes, ice cream, chocolates, sweets and beverages. The price ofnatural vanillin (isolated from the pod of tropical orchids of the genus Vanilla) varies betweenUS$ 1,200 and US$ 4,000 per kilogram, in contrast to the price of synthetic vanillin at underUS$ 15 per kilogram. Feruli…

  Biophysical and biochemical characterization of two bacterial enzymes Involved in the conversion of ferulic acid to vanillin, BP.DR

• Abstract

  Endo-beta-1,4-mannanase from Thermotoga petrophila (TpMan) is a hyperthermostable enzyme that catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides. The biodegradation of mannan represents a key step for various industrial applications including delignification of kraft pulps, food processing and production of second-generation biofuels. A re…

  Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the Central Domain an its role in the thermostabilization of whole enzyme, BP.DR

(Only some records are available in English at this moment)

• Abstract

  The complete enzymatic hydrolysis of mannan polysaccharides requires at least three types of enzymes working synergistically: ²-mannanase, ²-mannosidase, and ²-glucosidase. The hyperthermophilic bacterium Thermotoga petrophila produces the enzyme endo-²-1,4-mannanse (TpMan), which is composed of a GH5 catalytic domain and a carbohydrate-binding domain connected through a linker. The cryst…

  Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the central domain and its role in the thermostabilization of whole enzyme, BE.EP.DR