By G. Antranikian, G. Antranikian, M. Ciaramella, M.S. da Costa, E.A. Galinski, R. Ladenstein, S. Maloney, V.T. Marteinsson, M. Moracci, R. Müller, J. van der Oost, F.M. Pisani, D. Prieur, N.J. Russell, M. Rossi, H. Santos, R. Sharp, W.M. de Vos
During this designated factor overview articles summarize the main striking beneficial properties of microorganisms which can live to tell the tale less than severe stipulations. those microorganisms are tailored to dwelling at a hundred° C in volcanic springs, at low temperatures within the chilly polar seas, at excessive strain within the deep sea, at very high and low pH values (pH 0-1 or pH 10-11), or at very excessive salt concentrations (35%). the newest findings at the molecular biology and the protein constitution of those unique organisms are awarded. furthermore, the aptitude functions of extremophiles are reviewed, together with the construction of enzymes, appropriate solutes and using those extremophiles within the degradation of xenobiotics.
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Extra resources for Biotechnology of Extremophiles
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M o l e c u l a r Biology o f Barophiles . . . . . . . . . . . 3 T h e r m o p h i l i c Life at D e e p - S e a H y d r o t h e r m a l Vents . . . . . Taxonomy of Deep-Sea Hyperthermophiles .............. Responses to H y d r o s t a t i c Pressure ................... 30 30 31 4 Conclusions 32 5 References ......................... ................................ 33 1 Introduction P r o k a r y o t i c life is d r i v e n b y availability o f e n e r g y a n d c a r b o n sources a n d e l e c t r o n acceptors, b u t also b y n u m e r o u s p h y s i o - c h e m i c a l p a r a m e t e r s .
66 Excursion into Protein T h e r m o d y n a m i c s : Stability, Determined by Thermal Unfolding of Small Proteins from Hyperthermophiles .. 67 Extrinsic Stabilization - Archaebacterial Chaperonins Catalyze Folding and Repair of D a m a g e d Proteins, at Least in Vitro . . . . 5 Amylase and Pullulanase . . . . . . . . . . . . . . . . . . Cyclodextrin Glycosyl Transferase (CGTase) . . . . . . . . . . . Xylanases . . .