细长微球孢溶胶菌PORT2及其GH16琼脂酶的鉴定

Q3 Environmental Science
Santi Rukminita Anggraeni, M. Ansorge‐Schumacher
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引用次数: 0

摘要

琼脂糖具有潜在的生物活性,是第三代生物燃料的可持续来源。它们通过琼脂酶辅助生物转化提供被认为是温和和环保的过程。本工作报道了一种来自印尼西爪哇沿海海水Batu Karas的中温嗜胶菌的特性。16S rRNA分析表明该细菌与微球菌属有亲缘关系,特别是与长芽孢杆菌有亲缘关系。利用基因组挖掘方法克隆了一个编码琼脂酶AgaF16A的基因,并在大肠杆菌BL21(DE3)中表达。AgaF16A的蛋白序列与Microbulbifer thermotolerans JAMB-A94的糖苷水解酶(GH) 16b琼脂酶的催化结构域相似度为86.79%。该酶将琼脂糖和琼脂低聚物裂解成新琼脂己糖和新琼脂四糖。对印尼琼脂植物中提取的天然琼脂也有活性。AgaF16A在较宽的pH和温度范围内具有活性。在50℃条件下孵育1小时,活性保持在80%以上,具有热稳定性,有利于技术应用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characterization of Agarolytic Bacterium Microbulbifer elongatus PORT2 and Its GH16 Agarase
Sugars from agar exhibit potential biological activities and comprise a sustainable source of  third-generation biofuel. Their provision through enzyme-assisted bioconversion of agar is considered a mild and environmentally-friendly process. This work reports a mesophilic-agarolytic bacterium characterization from  Batu Karas, West Java-Indonesia coastal seawater. Analysis 16S rRNA showed a phylogeny relationship of the bacterium to the genus Microbulbifer, especially to M. elongatus. A gene coding for agarase AgaF16A was cloned and expressed in E. coli BL21(DE3) using a genome mining approach. The protein sequence of AgaF16A showed 86.79% similarity to the catalytic domain of glycoside hydrolase (GH) 16 b-agarase from Microbulbifer thermotolerans JAMB-A94. The enzyme cleaved agarose and agar oligomers larger than neoagarooctaose into neoagarohexaose and neoagarotetraose. It also showed activity on natural agar extracted from Indonesian agarophytes. The AgaF16A was active in wide pH and temperature ranges. It retained more than 80% activity after one hour incubation at 50 °C, indicating thermostability, favorable for technical application.
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来源期刊
CiteScore
1.40
自引率
0.00%
发文量
10
审稿时长
16 weeks
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