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来自环状芽孢杆菌IAM1165的87千道尔顿β-1,3-葡聚糖酶的分离与部分特性分析

Isolation and partial characterization of an 87-kilodalton beta-1,3-glucanase from Bacillus circulans IAM1165.

作者信息

Aono R, Sato M, Yamamoto M, Horikoshi K

机构信息

Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.

出版信息

Appl Environ Microbiol. 1992 Feb;58(2):520-4. doi: 10.1128/aem.58.2.520-524.1992.

Abstract

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.

摘要

环状芽孢杆菌IAM1165产生至少两种可裂解真菌细胞壁的细胞外β-1,3-葡聚糖酶。其中一种细胞外酶被纯化至同质。其分子量为87 kDa,等电点为4.3。当以海带多糖(一种可溶性β-1,3-葡聚糖)为底物时,该酶反应的最适温度为70℃。该酶的pH范围较宽(pH 4.5至9.0),最适pH为6.5。该酶是一种内切β-1,3-葡聚糖酶,具有随机切割模式。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1982/195278/9b8ae7e001ff/aem00043-0097-a.jpg

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