来自短柄青霉的β-1,6-葡聚糖酶的纯化及性质
Purification and properties of a beta-1,6-glucanase from Penicillium brefeldianum.
作者信息
Schep G P, Shepherd M G, Sullivan P A
出版信息
Biochem J. 1984 Nov 1;223(3):707-14. doi: 10.1042/bj2230707.
Abstract
An inducible endo-beta-1,6-glucanase was purified from Penicillium brefeldianum by DEAE-cellulose, Bio-Gel P-150 and high-pressure liquid chromatography. The final preparation was essentially free from beta-1,3-glucanase and beta-glucosidase activities. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed one protein band with an Mr of 44000. The Vmax. and Km values were calculated to be 624 units (mumol/min)/mg and 2.78 mg/ml respectively. The glucanase had lytic activity against mycelial cells of the yeast Candida albicans. The yield of purified beta-1,6-glucanase from 100 mg dry weight of freeze-dried culture filtrate varied from 60 to 180 units.
摘要
通过DEAE-纤维素、Bio-Gel P-150和高压液相色谱法从短柄青霉中纯化出一种诱导型内切-β-1,6-葡聚糖酶。最终制剂基本不含β-1,3-葡聚糖酶和β-葡萄糖苷酶活性。十二烷基硫酸钠/聚丙烯酰胺凝胶电泳显示有一条Mr为44000的蛋白带。Vmax和Km值经计算分别为624单位（微摩尔/分钟）/毫克和2.78毫克/毫升。该葡聚糖酶对白色念珠菌的菌丝体细胞具有裂解活性。从100毫克冻干培养滤液的干重中纯化得到的β-1,6-葡聚糖酶产量在60至180单位之间。
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