Open AccessA novel heat‐stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases
Author(s) -
Arpigny Jean Louis,
Jendrossek Dieter,
Jaeger KarlErich
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13209.x
Subject(s) - sulfolobus acidocaldarius , sulfolobus , polyhydroxyalkanoates , biochemistry , enzyme , serine hydrolase , biology , chemistry , serine , archaea , genetics , bacteria , gene
A fragment of genomic DNA from Sulfolobus acidocaldarius DSM 639 encoding a lipolytic enzyme was cloned and sequenced. The 314‐amino acid polypeptide displays a maximum sequence similarity (43%) to a putative polyhydroxyalkanoate depolymerase from Pseudomonas oleovorans and contains the pentapeptide G‐X 1 ‐S‐X 2 ‐G which is typical of serine hydrolases. The protein is highly thermostable and is able to hydrolyse a variety of lipid substrates thus providing a promising tool for potential biotechnological applications.