Identification and characterization of a thermostable pectate lyase from Aspergillus luchuensis var. saitoi
Identification and characterization of a thermostable pectate lyase from Aspergillus luchuensis var. saitoi
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DOI：
10.1016/j.foodchem.2018.10.059
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发表时间：
2019-03-15
期刊：
影响因子：
8.8
通讯作者：
Kato, Masashi
中科院分区：
文献类型：
--
作者：
Kamijo, Junya;Sakai, Kiyota;Kato, Masashi
果胶分解酶用于各种工业应用。我们试图从日本传统食品和饮料制备中使用的丝状真菌葡曲霉（Aspergillus luchuensis vars . saitoi）分离果胶裂解酶。所鉴定的酶被命名为AsPelA，与A. luchuensis mut的PelA同源。kawachii (AkPelA);两种酶的氨基酸序列具有99%的一致性，其中AsPelA的Ile140和Val197分别被AkPelA的Val和Asp取代。在60℃、70℃和80℃条件下培养60 min后，AsPelA活性分别降至最大活性的71%、61%和46%，而AkPelA活性分别降至16%、10%和8.5%，表明AsPelA比AkPelA更耐热。此外，AsPelA在中性到碱性的pH范围内以及有机溶剂、洗涤剂和金属离子存在下都是稳定的。我们的研究结果表明，AsPelA代表了一种候选果胶裂解酶，可用于食品、造纸和纺织工业。
Pectinolytic enzymes are used in diverse industrial applications. We sought to isolate a pectate lyase from Aspergillus luchuensis var. saitoi, a filamentous fungus used in traditional food and beverage preparation in Japan. The identified enzyme, named AsPelA, is orthologous to PelA from A. luchuensis mut. kawachii (AkPelA); the enzymes exhibit 99% amino acid sequence identity, with Ile140 and Val197 of AsPelA being replaced by Val and Asp in AkPelA, respectively. AsPelA activity decreased to 71%, 61%, and 46% of maximal activity after 60-min incubation at 60 degrees C, 70 degrees C, and 80 degrees C, whereas AkPelA activity dropped to 16%, 10%, and 8.5%, respectively, indicating that AsPelA is more thermostable than AkPelA. Furthermore, AsPelA was stable within a neutral-to-alkaline pH range, as well as in the presence of organic solvents, detergents, and metal ions. Our findings suggest that AsPelA represents a candidate pectate lyase for applications in food, paper, and textile industries.