Discovery and Characterization of a Thermostable Esterase from an Oil Reservoir Metagenome  

作　　者：Anna Lewin Trine Aakvik Strand Tone Haugen Geir Klinkenberg Hans Kristian Kotlar Svein Valla Finn Drabløs Alexander Wentzel Anna Lewin;Trine Aakvik Strand;Tone Haugen;Geir Klinkenberg;Hans Kristian Kotlar;Svein Valla;Finn Drabløs;Alexander Wentzel(SINTEF Materials and Chemistry, Department of Biotechnology and Nanomedicine, Trondheim, Norway;Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway;Former at Statoil ASA, Ranheim, Norway;Department of Biotechnology, Norwegian University of Science and Technology, Trondheim, Norway)

机构地区：[1]SINTEF Materials and Chemistry, Department of Biotechnology and Nanomedicine, Trondheim, Norway [2]Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway [3]Former at Statoil ASA, Ranheim, Norway [4]Department of Biotechnology, Norwegian University of Science and Technology, Trondheim, Norway

出　　处：《Advances in Enzyme Research》2016年第2期68-86,共19页酶研究进展（英文）

摘　　要：With the aim of identifying novel thermostable esterases, comprehensive sequence databases and cloned fosmid libraries of metagenomes derived from an offshore oil reservoir on the Norwegian Continental Shelf were screened for enzyme candidates using both sequence-and function-based screening. From several candidates identified in both approaches, one enzyme discovered by the functional approach was verified as a novel esterase and subjected to a deeper characterization. The enzyme was successfully over-produced in Escherichia coli and was shown to be thermostable up to 90°C, with the highest esterase activity on short-chain ester substrates and with tolerance to solvents and metal ions. The fact that the thermostable enzyme was solely found by functional screening of the oil reservoir metagenomes illustrates the importance of this approach as a complement to purely sequence-based screening, in which the enzyme candidate was not detected. In addition, this example indicates the large potential of deep-sub-surface oil reservoir metagenomes as a source of novel, thermostable enzymes of potential relevance for industrial applications.With the aim of identifying novel thermostable esterases, comprehensive sequence databases and cloned fosmid libraries of metagenomes derived from an offshore oil reservoir on the Norwegian Continental Shelf were screened for enzyme candidates using both sequence-and function-based screening. From several candidates identified in both approaches, one enzyme discovered by the functional approach was verified as a novel esterase and subjected to a deeper characterization. The enzyme was successfully over-produced in Escherichia coli and was shown to be thermostable up to 90°C, with the highest esterase activity on short-chain ester substrates and with tolerance to solvents and metal ions. The fact that the thermostable enzyme was solely found by functional screening of the oil reservoir metagenomes illustrates the importance of this approach as a complement to purely sequence-based screening, in which the enzyme candidate was not detected. In addition, this example indicates the large potential of deep-sub-surface oil reservoir metagenomes as a source of novel, thermostable enzymes of potential relevance for industrial applications.

关 键 词：METAGENOMICS Enzyme Discovery THERMOSTABLE ESTERASE 

分 类 号：Q78[生物学—分子生物学]