一种来自药用真菌灵芝的漆酶。
A laccase from the medicinal mushroom Ganoderma lucidum.
作者信息
Wang H X, Ng T B
机构信息
State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing 100094, China.
出版信息
Appl Microbiol Biotechnol. 2006 Sep;72(3):508-13. doi: 10.1007/s00253-006-0314-9. Epub 2006 Apr 25.
A protein demonstrating laccase activity and potent inhibitory activity towards human immunodeficiency virus (HIV)-1 reverse transcriptase (IC50 1.2 microM) was isolated from fresh fruiting bodies of the medicinal mushroom Ganoderma lucidum. The laccase had a novel N-terminal sequence and a molecular mass of 75 kDa, which is higher than the range (55-56 kDa) reported for most other mushroom laccases. It was isolated by sequential chromatography on DEAE-cellulose and Affi-gel blue gel and adsorption on Con A-Sepharose. Unlike some of the previously isolated laccases, it was adsorbed only on Con A-Sepharose. The enzyme required a pH of 3-5 and a temperature of 70 degrees C to exhibit maximal activity. Minimal activity was detected at pH 6 and 7. Activity was undetectable at pH 8 and 9 and after exposure to 100 degrees C for 10 min.
从药用蘑菇灵芝的新鲜子实体中分离出一种具有漆酶活性且对人类免疫缺陷病毒1型（HIV-1）逆转录酶具有强效抑制活性（半数抑制浓度为1.2微摩尔）的蛋白质。该漆酶具有一个新的N端序列，分子量为75 kDa，高于大多数其他蘑菇漆酶报道的范围（55 - 56 kDa）。它通过在DEAE - 纤维素和Affi - 凝胶蓝凝胶上的连续色谱法以及在Con A - 琼脂糖上的吸附作用进行分离。与一些先前分离的漆酶不同，它仅吸附在Con A - 琼脂糖上。该酶在pH值为3 - 5且温度为70℃时表现出最大活性。在pH值为6和7时检测到的活性最低。在pH值为8和9时以及在100℃下暴露10分钟后，活性无法检测到。
Zotero 插件