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首页> 美国卫生研究院文献>Applied and Environmental Microbiology >Enzymatic Analysis of an Amylolytic Enzyme from the Hyperthermophilic Archaeon Pyrococcus furiosus Reveals Its Novel Catalytic Properties as both an α-Amylase and a Cyclodextrin-Hydrolyzing Enzyme
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Enzymatic Analysis of an Amylolytic Enzyme from the Hyperthermophilic Archaeon Pyrococcus furiosus Reveals Its Novel Catalytic Properties as both an α-Amylase and a Cyclodextrin-Hydrolyzing Enzyme

机译：高温嗜热古生热球菌淀粉酶的酶学分析揭示了其作为α-淀粉酶和环糊精水解酶的新型催化性能。

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摘要

Genomic analysis of the hyperthermophilic archaeon Pyrococcus furiosus revealed the presence of an open reading frame (ORF PF1939) similar to the enzymes in glycoside hydrolase family 13. This amylolytic enzyme, designated PFTA (Pyrococcus furiosus thermostable amylase), was cloned and expressed in Escherichia coli. The recombinant PFTA was extremely thermostable, with an optimum temperature of 90°C. The substrate specificity of PFTA suggests that it possesses characteristics of both α-amylase and cyclodextrin-hydrolyzing enzyme. Like typical α-amylases, PFTA hydrolyzed maltooligosaccharides and starch to produce mainly maltotriose and maltotetraose. However, it could also attack and degrade pullulan and β-cyclodextrin, which are resistant to α-amylase, to primarily produce panose and maltoheptaose, respectively. Furthermore, acarbose, a potent α-amylase inhibitor, was drastically degraded by PFTA, as is typical of cyclodextrin-hydrolyzing enzymes. These results confirm that PFTA possesses novel catalytic properties characteristic of both α-amylase and cyclodextrin-hydrolyzing enzyme.
机译：对嗜热古菌激烈热球菌的基因组分析表明，存在一个与糖苷水解酶家族13中的酶类似的开放阅读框（ORF PF1939）。这种淀粉分解酶被称为PFTA（激烈热球菌热稳定淀粉酶），已在大肠杆菌中克隆和表达。 。重组PFTA具有极高的热稳定性，最适温度为90°C。 PFTA的底物特异性表明它同时具有α-淀粉酶和环糊精水解酶的特性。像典型的α-淀粉酶一样，PFTA水解麦芽低聚糖和淀粉，主要产生麦芽三糖和麦芽四糖。但是，它也可能攻击并降解对α-淀粉酶有抵抗力的支链淀粉和β-环糊精，分别主要产生三聚葡萄糖和麦芽七糖。此外，一种有效的α-淀粉酶抑制剂阿卡波糖被PFTA急剧降解，这是环糊精水解酶的典型特征。这些结果证实PFTA具有α-淀粉酶和环糊精水解酶的新颖催化特性。

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