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首页> 外文期刊>Applied and Environmental Microbiology >Isolation and partial characterization of an 87-kilodalton beta-1,3-glucanase from Bacillus circulans IAM1165.
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Isolation and partial characterization of an 87-kilodalton beta-1,3-glucanase from Bacillus circulans IAM1165.

机译:分离自环状芽孢杆菌IAM1165的87-千达尔顿β-1,3-葡聚糖酶及其部分特征。

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摘要

Bacillus circulans IAM1165 produces at least two extracellular beta-1,3-glucanases that lyse fungal cell walls. One of these extracellular enzymes was purified to homogeneity. The molecular mass was 87 kDa, and the pI was 4.3. The optimum temperature of the enzyme reaction was 70 degrees C when laminarin (a soluble beta-1,3-glucan) was used as the substrate. The pH range of the enzyme was broad (pH 4.5 to 9.0), and the optimum pH was 6.5. The enzyme is an endo beta-1,3-glucanase and has a random cleavage pattern.
机译:环状芽孢杆菌IAM1165产生至少两种裂解真菌细胞壁的细胞外β-1,3-葡聚糖酶。这些细胞外酶之一被纯化至均质。分子量为87 kDa,pI为4.3。当使用层粘连蛋白(可溶性β-1,3-葡聚糖)作为底物时,酶反应的最佳温度为70摄氏度。酶的pH范围宽(pH 4.5至9.0),最适pH为6.5。该酶是内切β-1,3-葡聚糖酶,具有随机切割模式。

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