Thermal stabilization of psychrophilic enzymes: A case study of the cold-active hormone-sensitive lipase from Psychrobacter sp. TA144

Biotechnology Progress

Volumn 28, Issue 4, 2012, Pages 946-952

  De Santi, Concetta ^a   Durante, Lorenzo ^b   Vecchio, Pompea Del ^b   Tutino, Maria Luisa ^b   Parrilli, Ermenegilda ^b   De Pascale, Donatella ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Betaine; Hormone sensitive lipase; L proline; Psychrophilic enzymes; TMAO

Indexed keywords

ACTIVE SITE; BETAINE; BIOPHYSICAL TECHNIQUES; COLD-ACTIVE; EFFICIENT STRATEGY; HORMONE-SENSITIVE LIPASE; INDUSTRIAL BIOPROCESSES; L-PROLINE; MESOPHILIC; MODERATE TEMPERATURE; NATURALLY OCCURRING; OSMOLYTES; OSMOPROTECTANTS; PROTEIN THERMAL STABILITY; SPECIFIC ACTIVITY; THERMAL STABILIZATION; TMAO; TRIMETHYLAMINE N OXIDES;

AMINO ACIDS; BACTERIA; FLEXIBLE STRUCTURES; THERMODYNAMIC STABILITY;

ENZYME ACTIVITY;

BACTERIAL PROTEIN; CHOLESTEROL ESTERASE;

ARTICLE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; HEAT; ISOLATION AND PURIFICATION; KINETICS; MOLECULAR GENETICS; PSYCHROBACTER;

BACTERIAL PROTEINS; ENZYME STABILITY; HOT TEMPERATURE; KINETICS; MOLECULAR SEQUENCE DATA; PSYCHROBACTER; STEROL ESTERASE;

PSYCHROBACTER; PSYCHROBACTER SP.;

EID: 84864834815     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1574     Document Type: Article

References (20)

1. Tutino ML, di Prisco G, Marino G, de Pascale D. Cold-adapted esterases and lipases: from fundamentals to application. Protein Pept Lett. 2009; 16: 1172-1180.
2. Marx JC, Collins T, D'Amico S, Feller G, Gerday C. Cold-adapted enzymes from marine Antarctic microorganisms. Mar Biotechnol. 2007; 9: 293-304.
3. Siddiqui KS, Poljak A, Cavicchioli R. Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives. Cell Mol Biol (Noisy-le-grand). 2004; 50: 657-667.
4. Holthauzen LM, Auton M, Sinev M, Rösgen J. Protein stability in the presence of cosolutes. Methods Enzymol. 2011; 492: 61-125.
5. Jamal S, Poddar NK, Singh LR, Dar TA, Rishi V, Ahmad F. Relationship between functional activity and protein stability in the presence of all classes of stabilizing osmolytes. FEBS J. 2009; 276: 6024-6032.
6. Gong H, Croft K, Driedzic WR, Ewart KV. Chemical chaperoning action of glycerol on the antifreeze protein in rainbow smelt. J Thermal Biol. 2011; 36: 78-83.
7. Attri P, Venkatesu P, Lee MJ. Influence of osmolytes and denaturants on the structure and enzyme activity of alpha-chymotrypsin. J Phys Chem B. 2010; 114: 1471-1478.
8. De Santi C, Tutino ML, Mandrich L, Giuliani M, Parrilli E, Del Vecchio P, de Pascale D. The hormone-sensitive lipase from Psychrobacter sp. TA144: new insight in the structural/functional characterization. Biochimie. 2010; 92: 949-957.
9. Hotelier T, Renault L, Cousin X, Negre V, Marchot P, Chatonnet A. ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins. Nucleic Acids Res. 2004; 32: D145-D147.
10. Compton LA, Johnson WC. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal Biochem. 1986; 155: 155-167.
11. Whitmore L, Wallace BA. DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 2004; 32: 668-673.
12. Sreerama N, Woody RW. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem. 2000; 287: 252-260.
13. Santos H, da Costa MS. Compatible solutes of organisms that live in hot saline environments. Environ Microbiol. 2002; 4: 501-509.
14. Faria TQ, Lima JC, Bastos M, Maçanita AL, Santos H. Protein stabilization by osmolytes from hyperthermophiles: effect of mannosylglycerate on the thermal unfolding of recombinant nuclease from Staphylococcus aureus studied by picosecond time-resolved fluorescence and calorimetry. J Biol Chem. 2004; 279: 48680-48691.
15. Mello CC, Barrick D. Measuring the stability of partly folded proteins using TMAO. Protein Sci. 2003; 12: 1522-1529.
16. Timasheff SN. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu Rev Biophys Biomol Struct. 1993; 22: 67-97.
17. Timasheff SN. Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc Natl Acad Sci USA. 2002; 99: 9721-9726.
18. Mukaiyama A, Koga Y, Takano K and Kanaya S. Osmolyte effect on the stability and folding of a hyperthermophilic protein. Proteins: Struct Funct Bioinform. 2008; 71: 110-118.
19. He HL, Chen XL, Zhang XY, Sun CY, Zou BC, Zhang YZ. Novel use for the osmolyte trimethylamine N-oxide: retaining the psychrophilic characters of cold-adapted protease deseasin MCP-01 and simultaneously improving its thermostability. Mar Biotechnol. 2009; 11: 710-716.
20. Kulakova L, Galkin A, Nakayama T, Nishino T, Esaki N. Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly>Pro substitution near the active site on its catalytic activity and stability. Biochem Biophys Acta. 2004; 1696: 59-65.