Isolation and characterization of cold-active family VIII esterases from an arctic soil metagenome.

Abstract:

:Functional screening for lipolytic enzymes at low temperatures resulted in the isolation of the novel cold-active esterases, EstM-N1 and EstM-N2, from a metagenomic DNA library of arctic soil samples. EstM-N1 and EstM-N2 were 395 and 407 amino acids in length, respectively, and showed the highest similarity to class C β-lactamases. However, they shared a relatively low level of sequence similarity (30%) with each other. Phylogenetic analysis of bacterial lipolytic enzymes confirmed that EstM-N1 and EstM-N2 belonged to family VIII of bacterial esterases/lipases. The (His)(6)-tagged esterases were purified to about 99% homogeneity from the soluble fraction of recombinant Escherichia coli cultures. The purified EstM-N1 and EstM-N2 retained more than 50% of maximal activity in the temperature range of 0-35 °C, with optimal temperatures of 20 °C and 30 °C, respectively. Both enzymes preferred the short acyl chains of p-nitrophenyl esters and exhibited very narrow substrate specificity, indicating that they are typical esterases. The β-lactamase activity of EstM-N1 and EstM-N2 was also detected and reached about 31% and 13% of the positive control enzyme, Bacillus cereus β-lactamase, respectively. These first cold-active esterases belonging to family VIII are expected to be useful for potential biotechnological applications as interesting biocatalysts.

authors

Yu EY,Kwon MA,Lee M,Oh JY,Choi JE,Lee JY,Song BK,Hahm DH,Song JK

doi

10.1007/s00253-011-3132-7

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

573-81

issue

2

eissn

0175-7598

issn

1432-0614

journal_volume

90

pub_type

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