López-López Olalla, Cerdán María-Esperanza, González-Siso María-Isabel
Grupo EXPRELA, Centro de Investigacións Científicas Avanzadas (CICA), Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias, Universidade da Coruña, Campus de A Coruña, 15071 A Coruña, Spain.
Microorganisms. 2015 Nov 4;3(4):792-808. doi: 10.3390/microorganisms3040792.
Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media. At present, they represent about 20% of commercialized enzymes for industrial use. Lipolytic enzymes from thermophilic microorganisms are preferred for industrial use to their mesophilic counterparts, mainly due to higher thermostability and resistance to several denaturing agents. However, the production at an industrial scale from the native organisms is technically complicated and expensive. The thermophilic bacterium Thermus thermophilus (T. thermophilus) has high levels of lipolytic activity, and its whole genome has been sequenced. One esterase from the T. thermophilus strain HB27 has been widely characterized, both in its native form and in recombinant forms, being expressed in mesophilic microorganisms. Other putative lipases/esterases annotated in the T. thermophilus genome have been explored and will also be reviewed in this paper.
脂解酶、酯酶（EC 3.1.1.1）和脂肪酶（EC 3.1.1.3）催化醇与羧酸之间酯键的水解及其在有机介质中的形成。目前，它们约占商业化工业用酶的20%。与嗜温微生物来源的脂解酶相比，嗜热微生物来源的脂解酶更适合工业应用，主要是因为其具有更高的热稳定性和对多种变性剂的耐受性。然而，从天然生物体进行工业规模生产在技术上复杂且成本高昂。嗜热栖热菌（嗜热栖热放线菌）具有高水平的脂解活性，其全基因组已被测序。嗜热栖热菌HB27菌株的一种酯酶，无论是天然形式还是重组形式，都已在嗜温微生物中表达并得到广泛表征。嗜热栖热菌基因组中注释的其他假定脂肪酶/酯酶也已被研究，本文也将对其进行综述。
