Novel cellulases from an extremophilic filamentous fungi Penicillium citrinum:: production and characterization
Novel cellulases from an extremophilic filamentous fungi Penicillium citrinum:: production and characterization
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DOI：
10.1007/s10295-008-0304-2
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发表时间：
2008-04-01
影响因子：
3.4
通讯作者：
Ghosh, Sanjay
中科院分区：
文献类型：
--
作者：
Dutta, Tanmay;Sahoo, Rupam;Ghosh, Sanjay
纤维素酶解具有潜在的经济和环境友好的应用前景。因此，发现新的极端嗜热纤维素酶是满足工业需求的必要条件。桔青霉（Penicillium citrinum，MTCC 6489）是本实验室从土壤中分离到的一株产耐碱、耐热纤维素酶的菌株。以麸皮为底物，研究了桔黄假单胞菌固体发酵和液体发酵产内切葡聚糖酶和滤纸酶的情况。内切葡聚糖酶的酶谱分析显示存在两种不同的异构体的分子量。其中一个是90 kDa，另一个是38 kDa。部分纯化的内切葡聚糖酶在其pH最适曲线中分别在pH 5.5和8.0处显示出两个不同的峰。而FPase的最适pH曲线只有一个峰（pH6.5）。桔青霉纤维素酶在自然界中是热稳定的。本文首次报道了从耐碱性真菌桔青霉（Penicilliumcitrinum）中分离得到的一种碱稳定纤维素酶。桔黄假单胞菌的耐热内切葡聚糖酶可能作为洗衣剂的添加剂具有潜在的有效性。
The enzymatic hydrolysis of cellulose has potential economical and environment-friendly applications. Therefore, discovery of new extremophilic cellulases is essential to meet the requirements of industry. Penicillium citrinum (MTCC 6489) that was previously isolated from soil in our laboratory, produced alkali tolerant and thermostable cellulases. Endoglucanase and filter paper activity hydrolase (FPAse) production of P. citrinum were studied using wheat bran substrate in solid state and submerged culture. Zymogram analysis of endoglucanase revealed the presence of two isoforms differing in molecular weight. One of them was 90 kDa and other one was 38 kDa. Partially purified endoglucanase showed two different peaks at pH 5.5 and 8.0, respectively, in its pH optima curve. But FPase showed only one peak (at pH 6.5) in its pH optima curve. Cellulase of P. citrinum is thermostable in nature. The present work reports for the first time, the alkali stable cellulase from alkali tolerant fungus Penicillium citrinum. Thermostable endoglucanase from P. citrinum may have potential effectiveness as additives to laundry detergents.