Biochemical Diversity of Carboxyl Esterases and Lipases from Lake Arreo (Spain): a Metagenomic Approach

Supplemental material

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  • Supplemental file 1 -

    General features of reported esterases/lipases isolated from metagenomic resources (Table S1); list of primers used in the study (Table S2); percentage of identity between Arreo enzymes, determined by Matcher (EMBOSS package) (Table S3); half-saturation (Michaelis) coefficient (Km), catalytic rate constant (kcat), and catalytic efficiency (kcat/Km) values for the wild-type α/β hydrolases from Lake Arreo (Table S4); location map, vegetation and use of drainage basin map, and bathymetric map of Lake Arreo (Fig. S1); Lake Arreo proteins, as overexpressed in the active form in E. coli at 16ºC (Fig. S2); chemical structures of substrates applied for activity profiling of esterase/lipase preparations used in the present study (Fig. S3); structural models of esterases/lipases from the α/β hydrolase family characterized in this work (Fig. S4); nucleotide and amino acid sequences of esterases/lipases from Lake Arreo (“Annex”); supplemental text: GOHTAM and BLAST analyses.

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