In the study, an extracellular enzyme HML CBH1 was purified from the fermentation solution of Aspergillus oryzae HML366, and characterized by biological and molecular analysis. Following the culturing of A. oryzae HML366 under the optimized conditions for enzyme production, an enzyme named HML CBH1 with a molecular weight of 48 kDa was purified using 3000 Da cellulose ultrafiltration column and anion exchange chromatography. The specific activity of the purified enzyme was 9.65 U/mg, and the optimum temperature and pH for the enzyme were 50 and 5.0 °C, respectively. The enzyme was stable at temperatures below 60 °C and pH ranging from 3.0 to 10.0. The partial amino acid sequence of HML CBH1 was analyzed by time-of-flight mass spectrometry, and Mascot and Blast analysis showed that the HML CBH1 sequence was identical to the protein gi:22138643, belonging to the glycoside hydrolase family 7, and had exoglucanase and endoglucanase activity.

本研究从米曲霉HML366的发酵液中纯化出一种胞外酶HML CBH1 ，并通过生物学和分子分析对其进行表征。米曲霉培养后HML366在优化的产酶条件下，采用3000 Da纤维素超滤柱和阴离子交换层析纯化出一种分子量为48 kDa的酶HML CBH1。纯化酶的比活为9.65 U/mg，酶的最适温度和pH分别为50和5.0°C。该酶在低于 60°C 的温度和 3.0 至 10.0 的 pH 值范围内是稳定的。通过飞行时间质谱分析HML CBH1的部分氨基酸序列，Mascot和Blast分析表明HML CBH1序列与蛋白gi:22138643相同，属于糖苷水解酶家族7，具有外切葡聚糖酶和内切葡聚糖酶活性。