Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion
Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion
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DOI：
10.1007/s10529-006-9166-8
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发表时间：
2006-11-01
影响因子：
2.7
通讯作者：
Yun, Han Dae
中科院分区：
文献类型：
--
作者：
Hong, Su Young;Lee, Jin Suk;Yun, Han Dae
通过基因融合从海洋热藻中获得一种人工的、双功能的、耐热的纤维素酶-木聚糖酶。当xynA在cel5C下游融合时，融合蛋白表现出纤维素酶和木聚糖酶的活性，而当xynA在cel5C上游融合时，融合蛋白没有活性。该酶在pH 5.0和80℃条件下活性最佳，时间为30 min。经羧甲基纤维素-和木聚糖- sds - page分析，大肠杆菌表达了该融合酶，表观分子量约为152 kDa。
An artificial, bifunctional, thermostable cellulase-xylanase enzyme from Thermotoga maritima by gene fusion. The fusion protein exhibited both cellulase and xylanase activity when xynA was fused downstream of cel5C but no activities were shown when xynA was fused upstream of cel5C. The enzyme was optimally active at pH 5.0 and 80 degrees C over 30 min. E. coli expressed the fusion enzyme, with an apparent molecular mass of approximately 152 kDa by carboxymethyl cellulose- and xylan-SDS-PAGE.