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A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to
J L Arpigny1, D Jendrossek, K E Jaeger
1Lehrstuhl für Biologie der Mikroorganismen, Ruhr-Universität Bochum, Germany. jeanlouis.arpigny@ruhr-uni-bochum.de
FEMS Microbiology Letters
|October 24, 1998
Abstract:
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-X1-S-X2-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.