Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Extracellular polyhydroxybutyrate depolymerase/esterase of T.thermophilus is associated with flagellin of the type III export system
Δημιουργός/Συγγραφέας:	Pantazaki, A.A. Papaneophytou, C. Hirano, H. [EL] Κυριακίδης, Δ.Α.[EN] Kyriakidis, D.A.
Εκδότης:	Springer
Ημερομηνία:	2009
Γλώσσα:	Αγγλικά
DOI:	10.1007/s00253-008-1842-2
Περίληψη:	The thermophilic bacterium Thermus thermophilus HB8 has been characterized as a polyhydroxybutyrate (PHB)-degrading microorganism since it grows efficiently and forms clear zones on agar plates containing PHB as sole carbon source. T. thermophilus extracellular PHB depolymerase was purified to homogeneity using an affinity chromatography protocol. The purified enzyme was estimated to have an apparent molecular mass of 42 kDa. The extracellular PHB depolymerase gene was identified as the TTHA0199 gene product of T. thermophilus HB8. The amino acid sequence of the TTHA0199 gene product shared significant homologies to other carboxylesterases. A catalytic triad was identified consisting of S(183), E(310), and H(405). A pentapeptide sequence (GX(1)SX(2)G) exists within the molecule, characteristic for PHB depolymerases (lipase box) and for other serine hydrolases. Purified extracellular PHB depolymerase was stable at high temperatures with an optimum activity at pH 8.0. The apparent Km value of the purified enzyme for PHB was 53 microg/ml. As the main product of the enzymic hydrolysis of PHB, the monomer 3-hydroxybutyrate was identified, suggesting that the enzyme acts principally as an exo-type hydrolase.
Τίτλος πηγής δημοσίευσης:	Appl Microbiol Biotechnol
Τόμος/Κεφάλαιο:	83
Τεύχος:	4
Σελίδες:	659-668
Θεματική Κατηγορία:	[EL] Βιολογία (Γενικά)[EN] Biology (General)
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Κάτοχος πνευματικών δικαιωμάτων:	© 2010 The authors
Όροι και προϋποθέσεις δικαιωμάτων:	This is the author's version (post refereeing). The definite version of this aricle apperas in "Appl Microbiol Biotechnol . 2009 Jun;83(4):659-68. doi: 10.1007/s00253-008-1842-2. Epub 2009 Feb 13" and can be found at http://dx.doi.org/10.1007/s00253-008-1842-2
Εμφανίζεται στις συλλογές:	Άλλα