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首页> 外文期刊>Anais da Academia Brasileira de Ciencias >Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09
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Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09

机译:生产,纯化和鉴定来自青霉青霉菌sw09的外切多聚半乳糖醛酸酶

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A soil isolate, Penicillium janthinellum sw09 has been found to produce significant amounts of an extracellular pectinase subsequently characterized as exo-polygalacturonase (exo-PG). By optimizing growth conditions, P. janthinellum sw09 produced high amount of exo-PG (16.54 units/mL). The crude enzyme was purified by gel filtration chromatography and two exo-PG activity peaks (designated as PGI and PGII) were revealed. On SDS-PAGE analysis, purified PGII using DEAE-Sepharose FF column, was found to be a single band with a molecular mass of 66.2 kDa. The purified PGII exhibited maximal activity at the temperature of 45 o C and pH 5.0. The stability profiles show that PGII is more stable in the pH range of 4.0-8.0 and below 60 o C. The K m and V max for the enzyme was 1.74 mg/mL and 18.08 ??mol/ (mLa?¢min), respectively. Due to this enzymatic characterization, this pectinase is an attractive candidate for applications in degradation of pectin.
机译:已发现土壤分离物janicinellum sw09会产生大量胞外果胶酶,随后将其表征为外切聚半乳糖醛酸酶(exo-PG)。通过优化生长条件,P。janthinellum sw09产生了大量的exo-PG(16.54单位/ mL)。通过凝胶过滤色谱法纯化粗酶,并显示两个exo-PG活性峰(称为PGI和PGII)。在SDS-PAGE分析中,发现使用DEAE-Sepharose FF柱纯化的PGII为单条带,分子量为66.2 kDa。纯化的PGII在45 o C和pH 5.0时表现出最大的活性。稳定性曲线表明,PGII在4.0-8.0和低于60 oC的pH范围内更稳定。酶的K m和V max为1.74 mg / mL和18.08 mol /(mLa·min),分别。由于这种酶学特征,该果胶酶是用于果胶降解的诱人候选物。

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