A NOVEL HEAT-STABLE LIPOLYTIC ENZYME FROM SULFOLOBUS-ACIDOCALDARIUS DSM-639 DISPLAYING SIMILARITY TO POLYHYDROXYALKANOATE DEPOLYMERASES

A fragment of genomic DNA from Sulfolobus acidocaldarius DSM 639 encod ing a lipolytic enzyme was cloned and sequenced. The 314-amino acid po lypeptide displays a maximum sequence similarity (43%) to a putative p olyhydroxyalkanoate depolymerase from Pseudomonas oleovorans and conta ins the pentapeptide G-X-1-S-X-2-G which is typical of serine hydrolas es. The protein is highly thermostable and is able to hydrolyse a vari ety of lipid substrates thus providing a promising tool for potential biotechnological applications. (C) 1998 Federation of European Microbi ological Societies. Published by Elsevier Science B.V. All rights rese rved.