Characterization of an organic solvent-tolerant α-amylase from a halophilic isolate, Thalassobacillus sp. LY18

Folia Microbiologica

Volumn 57, Issue 5, 2012, Pages 447-453

  Li, Xin ^a   Yu, Hui Ying ^a  

^a YUNCHENG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; BACTERIAL PROTEIN; STARCH;

ARTICLE; BACILLACEAE; CHEMISTRY; CHINA; ENZYME STABILITY; ENZYMOLOGY; GENETICS; HEAT; ISOLATION AND PURIFICATION; LAKE; METABOLISM; MICROBIOLOGY;

ALPHA-AMYLASES; BACILLACEAE; BACTERIAL PROTEINS; CHINA; ENZYME STABILITY; HOT TEMPERATURE; LAKES; STARCH;

BACTERIA (MICROORGANISMS); THALASSOBACILLUS;

EID: 84865472168     PISSN: 00155632     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12223-012-0160-3     Document Type: Article

References (24)

1. Antranikian G, Vorgias CE, Bertoldo C (2005) Extreme environments as a resource for microorganisms and novel biocatalysts. Adv Biochem Eng Biotechnol 96: 219-262.
2. Bradford MM (1976) A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
3. Cadenas Q, Engel PC (1994) Activity staining of halophilic enzymes: substitution of salt with zwitterions in non-denaturing electrophoresis. Biochem Mol Biol Int 33: 785-792.
4. Chakraborty S, Khopade A, Biao R, Jian W, Liu XY, Mahadik K, Chopade B, Zhang LX, Kokare C (2011) Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9. J Mol Catal B Enzyme 68(1): 52-58.
5. Coronado MJ, Vargas C, Hofemeister J, Ventosa A, Nieto JJ (2000) Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiol Lett 183: 67-71.
6. Demirkan ES, Mikami B, Adachi M, Higas T, Utsumi S (2005) α-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli. Process Biochem 40: 2629-2636.
7. Doukyu N, Ogino H (2010) Organic solvent-tolerant enzymes. Biochem Eng J 48: 270-282.
8. Finore I, Kasavi C, Aa P, Romano I, Oner ET, Kirdar B, Dipasquale L, Nicolaus B, Lama L (2011) Purification, biochemical characterization and gene sequencing of a thermostable raw starch digesting α-amylase from Geobacillus thermoleovorans subsp. stromboliensis subsp. nov. World J Microbiol Biotechnol 27: 2425-2433.
9. Fukushima T, Mizuki T, Echigo A, Inoue A, Usami R (2005) Organic solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1. Extremophiles 9: 85-89.
10. García MT, Gallego V, Ventosa A, Mellado E (2005) Thalassobacillus devorans gen. nov., sp. nov., a moderately halophilic, phenol-degrading, Gram-positive bacterium. Int J Syst Evol Microbiol 55(Pt 5): 1789-1795.
11. Karbalaei-Heidari HR, Ziaee AA, Amoozegar MA (2007) Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents. Extremophiles 11: 237-243.
12. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
13. Li X, Yu HY (2011) Extracellular production of beta-amylase by a halophilic isolate, Halobacillus sp. LY9. J Ind Microbiol Biotechnol 38(11): 1837-1843.
14. Li X, Yu HY, Liu XX, Sun X (2011) Production and characterization of a novel extracellular metalloproteinase by a newly isolated moderate halophile, Halobacillus sp. LY6. Folia Microbiol (Praha) 56(4): 329-334.
15. Mamo G, Gessesse A (1999) Effect of cultivation conditions on growth and α-amylase production by a thermophilic Bacillus sp. Lett Appl Microbiol 29: 61-65.
16. Marhuenda-Egea FC, Bonete MJ (2002) Extreme halophilic enzymes in organic solvents. Curr Opin Biotechnol 13: 385-389.
17. Miller G (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal Chem 31: 426-428.
18. Prakash B, Vidyasagar M, Madhukumar MS, Muralikrishna G, Sreeramulu K (2009) Production, purification, and characterization of two extremely halotolerant, thermostable, and alkalistable α-amylases from Chromohalobacter sp. TVSP 101. Process Biochem 44: 210-215.
19. Ruiz DM, De Castro RE (2007) Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. J Ind Microbiol Biotechnol 34(2): 111-115.
20. Shafiei M, Ziaee AA, Amoozegar MA (2011) Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J Ind Microbiol Biotechnol 38(2): 275-281.
21. Shafiei M, Ziaeea A-A, Amoozegar MA (2010) Purification and biochemical characterization of a novel SDS and surfactant stable, raw starch digesting, and halophilic α-amylase from a moderately halophilic bacterium Nesterenkonia sp. strain F. Process Biochem 45(5): 694-699.
22. Sivaramakrishnan S, Gangadharan D, Nampoothiri KM, Soccol CR, Pandey A (2006) α-Amylases from microbial sources-an overview on recent developments. Food Technol Biotechnol 44: 173-184.
23. Ventosa A, Nieto JJ, Oren A (1998) Biology of moderately halophilic aerobic bacteria. Microbiol Mol Biol Rev 62: 504-544.
24. Zaks A, Klibanov AM (1988) Enzymatic catalysis in nonaqueous solvents. J Biol Chem 263(7): 3194-3201.