摘要
从台湾海峡潮间带的红树林土壤中分离到一株产纤维素酶的短小芽孢杆菌S 2 7,该菌只产生葡聚糖内切酶。对该酶的研究显示其作用最适温度为 55℃ ,最适 pH为 5～ 7,在pH9的条件下仍具有 79 0 %的活力。用pBluescriptⅡ为载体 ,E .coliDH1 0B为受体 ,克隆到该酶的基因 ,并对其进行测序。测序结果显示其全长为 1 980bp ,推测其含 660个氨基酸。比较GenBank中的已知葡聚糖内切酶 ,发现该酶的氨基酸序列与嗜纤维杆菌 (Clostridiumcel lulovorans)的EngC及Bacillussp .KSM 52 2的EG Ⅳ同源性极高。
Bacillus pumilus S\|27 screened from marine environment produces an extracellular endo\|1,4\|β\|glucanase.The enzyme has its optimal activity at pH 5.0～7.0 and 55℃ and still retained 79.0% of it at pH9.0.The gene encoded this endo\|1,4\|β\|glucanase was cloned and sequenced.The structural gene contained an open reading frame of 1980bp,corresponding to 660 amino acids,the amino acid sequence of this enzyme is very close to that of an EG of C.cellulovorans and an EG of Bacillus sp.KSM\|522,all belong to the cellulase family E2.
出处
《微生物学报》
CAS
CSCD
北大核心
2001年第1期74-81,共8页
Acta Microbiologica Sinica
基金
国家海洋局海洋生物工程重点实验室开放基金项目!(HY980 3)&&
