Open AccessThe first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta Ba EstB as a novel esterase
Author(s) -
SánchezCarbente María del Rayo,
BatistaGarcía Ramón Alberto,
SánchezReyes Ayixón,
EscuderoGarcia Angela,
MoralesHerrera Catalina,
CuervoSoto Laura I.,
FrenchPacheco Leidys,
FernándezSilva Arline,
Amero Carlos,
Castillo Edmundo,
FolchMallol Jorge Luis
Publication year - 2017
Publication title -
microbiologyopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.881
H-Index - 36
ISSN - 2045-8827
DOI - 10.1002/mbo3.463
Subject(s) - esterase , biochemistry , lipase , hormone sensitive lipase , biology , enzyme , stereochemistry , chemistry
The heterologous expression and characterization of a Hormone‐Sensitive Lipases ( HSL ) esterase ( Ba EstB) from the Basidiomycete fungus Bjerkandera adusta is reported for the first time. According to structural analysis, amino acid similarities and conservation of particular motifs, it was established that this enzyme belongs to the ( HSL ) family. The cDNA sequence consisted of 969 nucleotides, while the gene comprised 1133, including three introns of 57, 50, and 57 nucleotides. Through three‐dimensional modeling and phylogenetic analysis, we conclude that Ba EstB is an ortholog of the previously described Rm EstB‐ HSL from the phylogenetically distant fungus Rhizomucor miehei . The purified Ba EstB was characterized in terms of its specificity for the hydrolysis of different acyl substrates confirming its low lipolytic activity and a noticeable esterase activity. The biochemical characterization of Ba EstB, the DLS analysis and the kinetic parameters determination revealed this enzyme as a true esterase, preferentially found in a dimeric state, displaying activity under alkaline conditions and relative low temperature ( pH = 10, 20°C). Our data suggest that Ba EstB is more active on substrates with short acyl chains and bulky aromatic moieties. Phylogenetic data allow us to suggest that a number of fungal hypothetical proteins could belong to the HSL family.