Purification of endoglucanase produced by Penicillium citrinum isolated from Amazon
نویسندگان
چکیده
Background The cellulolytic enzyme complex has many important biotechnological applications such as beverage, textile, food, paper and cellulose industries, as well as in degradation of lignocellulosic for ethanol biofuel production [1]. According to the enzymatic activity, cellulolytic complex is subdivided in three classes: endoglucanases, exoglucanases and b-D-glycosidases. Endoglucanases (endo-b-1,4-glucanase, EC 3.2.1.4) are responsible to initiate cleavage, hydrolyzing randomly internal regions from the amorphous cellulose fiber structures, releasing oligosaccharides from different grades of polymerization. These will be hydrolyzed by exoglucanases releasing cellobiose followed by b-D-glycosidades being hydrolyzed to glucose [1]. Penicillium citrinum has worldwide occurrence. Commonly in the soil, this specie is described as good xylanase and cellulase producer [2,3]. This work describes liquid chromatography to separate endoglucanases of Penicillium citrinum supernatant from submerse fermentation process.
منابع مشابه
Endo and exoglucanases produced by Penicillium citrinum isolated from Amazon
Background Cellulolytic enzymes (glucohidrolases EC 3.2.1.-) are biocatalizators highly specific. They act in synergy to hydrolyze b-1,4 bonds between monosaccharide units of D-glucose in the cellulose chain releasing its constituents. Cellulases are categorized according to the place they act in the cellulosic fiber. Endoglucanases start hydrolysis, exoglucanases act in the reduced terminal pr...
متن کاملPurification and cDNA cloning of NADPH-dependent aldoketoreductase, involved in asymmetric reduction of methyl 4-bromo-3-oxobutyrate, from Penicillium citrinum IFO4631.
Penicillium citrinum was found to catalyze the reduction of methyl 4-bromo-3-oxobutyrate to methyl (S)-4-bromo-3-hydroxybutyrate [(S)-BHBM] with high optical purity. From the strain, a cDNA clone encoding a novel NADPH-dependent alkyl 4-halo-3-oxobutyrate reductase (KER) was isolated. Escherichia coli cells overexpressing KER produced (S)-BHBM in the presence of an NADPH-regeneration system.
متن کاملPurification and identification of a novel antifungal protein secreted by Penicillium citrinum from the Southwest Indian Ocean.
A novel antifungal protein produced by the fungal strain Penicillium citrinum W1, which was isolated from a Southwest Indian Ocean sediment sample, was purified and characterized. The culture supernatant of P. citrinum W1 inhibited the mycelial growth of some plant pathogenic fungi. After saturation of P. citrinum W1 culture supernatants with ammonium sulfate and ion-exchange chromatography, an...
متن کاملPurification, characterization, gene cloning and expression of GH-10 xylanase (Penicillium citrinum isolate HZN13)
An extracellular thermostable xylanase (Xyl-IIb) produced by Penicillium citrinum isolate HZN13 was purified to homogeneity using DEAE-Sepharose, Sephadex G-100 and Bio-Gel P-60 chromatography with specific activity of 6272.7 U/mg and 19.6-fold purification. The purification revealed the occurrence of multiple forms of xylanases (Xyl-I, Xyl-IIa, Xyl-IIb and Xyl-III). The molecular mass of highl...
متن کاملPurification and biochemical characterization of endoglucanase from Penicillium pinophilum MS 20.
Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate o...
متن کامل