Purification and characterization of a novel extracellular halophilic and organic solvent-tolerant amylopullulanase from the haloarchaeon, Halorubrum sp. strain Ha25

Extremophiles

Volumn 18, Issue 1, 2014, Pages 25-33

  Siroosi, Maryam ^a   Amoozegar, Mohammad Ali ^a   Khajeh, Khosro ^b   Fazeli, Mostafa ^a   Habibi Rezaei, Mehran ^a  

^a UNIVERSITY OF TEHRAN   (Iran)

^b TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

Extreme halophilic archaea; Halophilic amylopullulanase; Halorubrum; Organic solvent tolerance; Protein purification

Indexed keywords

AMYLOPULLULANASE; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; GLYCOSIDASE; SOLVENT;

ARTICLE; CHEMISTRY; ENZYMOLOGY; HALORUBRUM; HEAT; ISOLATION AND PURIFICATION; OSMOLARITY;

ARCHAEAL PROTEINS; BACTERIAL PROTEINS; GLYCOSIDE HYDROLASES; HALORUBRUM; HOT TEMPERATURE; OSMOLAR CONCENTRATION; SOLVENTS;

EID: 84890477293     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-013-0589-6     Document Type: Article

References (46)

1. Adams MWW, Kelly RM (1995) Enzymes from microorganisms in extreme environments. Chem Eng News 73: 32-42.
2. Al-ZaZaee MM, Gurumurthy DM, Rajeshwara AN (2011) Identification, characterization of novel halophilic Bacillus Cereus Ms6: a source for extra cellular A-amylase. Adv Environ Biol 5: 992-999.
3. Boone DR, Castenhoiz RW, Garrity GM (2001) Bergey's manual of systematic bacteriology: The Archaea and the deeply branching and phototrophic bacteria. Springer, New York.
4. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
5. Chung YC, Kobayashi T, Kanai H, Akiba T, Kudo T (1995) Purification and properties of extracellular amylase from the hyperthermophilic archaeon Thermococcus profundus DT5432. Appl Environ Microbiol 61: 1502-1506.
6. Coronado MJ, Vargas C, Hofemeister J, Ventosa A, Nieto J (2000) Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiol Lett 183: 67-71.
7. Danson MJ, Hough DW (1997) The structural basis of protein halophilicity. Comp Biochem Physiol 117: 307-312.
8. Diger A, Antranikian G (1995) Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli. Appl Environ Microbiol 61: 567-575.
9. Domań-Pytka M, Bardowski J (2004) Pullulan degrading enzymes of bacterial origin. Crit Rev Microbiol 30: 107-121.
10. Dong G, Vieille C, Zeikus G (1997) Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl Environ Microbiol 63: 3577-3584.
11. Doukyua N, Ogino H (2010) Organic solvent-tolerant enzymes. Biochem Eng J 48: 270-282.
12. Duffner F, Bertoldo C, Andersen JT, Wagner K, Antranikian G (2000) A new thermoactive pullulanase from Desulfurococcus mucosus: cloning, sequencing, purification, and characterization of the recombinant enzyme after expression in Bacillus subtilis. J Bacteriol 182: 6331-6338.
13. Dussault H (1955) An improved technique for staining red halophilic bacteria. J Bacteriol 70: 484.
14. Dyall-Smith M (2009) The Halohandbook: protocols for halobacterial genetics. Haloarchaeal Genetics Laboratory, Melbourne.
15. Forbes B, Sahm D, Weissfeld A (2007) Bailey and Scott's diagnostic microbiology. 12th edn. Mosby Inc., St. Louis, pp 80-89.
16. Fukushima 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.
17. Ganghofner D, Kellermann J, Staudenbauer W, Bronnenmeier K (1998) Purification and properties of amylopullulanase, a glucoamylase and an alpha glucosidase in the amylolytic enzyme system of Thermoanaerobacteriumthermosaccharolyticum. Biosci Biotechnol Biochem 62: 302-308.
18. Ghollasi M, Khajeh K, Mollania N, Zareian S, Naderi-Manesh H (2008) An investigation on acarbose inhibition and the number of active sites in an amylopullulanase (L14-APU) from an Iranian Bacillus sp. Biologia 63(6): 1051-1056.
19. Gomes I, Gomes J, Steiner W (2003) Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresour Technol 90: 207-214.
20. Grant WD, Kamekura M, McGenity TJ, Ventosa A (2001) Bergey's manual of systematic bacteriology: the archaea and deeply branching and phototrophic bacteria, vol 1, 2nd edn. Springer, New York.
21. Gutiérrez C, González C (1972) Method for simultaneous detection of proteinase and esterase activities in extremely halophilic bacteria. Appl Microbiol 24: 516-517.
22. Hatada Y, Igarashi K, Ozaki K, Ara K, Hitomi J, Kobayashi T, Kawai S, Watabe T, Ito S (1996) Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1, 4 and α-1, 6 linkages in polysaccharides at different active sites. J Biol Chem 271: 24075-24083.
23. Hutcheon GW, Bolhuis A (2005) Characterisation of a highly stable a-amylase from the halophilic archaeon Haloarcula hispanica. Extremophiles 9: 487-495.
24. Jiao Y, Ming-Sheng L, Xu J, Fang Y (2011) A GH57 family amylopullulanase from deep-sea Thermococcus siculi: expression of the gene and characterization of the recombinant enzyme. Curr Microbiol 62: 222-228.
25. Kim OS, Cho YJ, Lee K, Yoon SH, Kim M, Na H, Park SC, Jeon YS, Lee JH, Yi H, Won S, Chun J (2012) Introducing EzTaxon-e: a prokaryotic 16S rRNA Gene sequence database with phylotypes that represent uncultured species. Int J Syst Evol Microbiol 62: 716-721.
26. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
27. Makhdoumi Kakhki A, Amoozegar MA, Mahmodi Khaledi E (2011) Diversity of hydrolytic enzymes in haloarchaeal strains isolated from salt lake. Int J Environ Sci Tech 8: 705-714.
28. Mancinelli RL, Landheim R, Sanchez-Porro C, Dornmayr-Pfaffenhuemer M, Gruber C, Legat A, Ventosa A, Radax C, Ihara K, White M, Stan-Lotter H (2009) Halorubrum chaoviator sp. nov., a haloarchaeon isolated from sea salt in Baja California, Mexico, Western Australia and Naxos, Greece. Int J Syst Evol Microbiol 59: 1908-1913.
29. Margesin R, Schinner F (2001) Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 5: 73-83.
30. Mathupala S, Lowe S, Gregory Zeikus J (1993) Sequencing of the amylopullulanase (apu) gene of Therrnoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis. J Biol Chem 268: 16332-16334.
31. Melasneimi H (1987) Effect of carbon source on production of thermostable a-amylase, pullulanase and a-glucosidase by Clostridium thermohydrosulfuricum. J Gen Microbiol 133: 883-890.
32. Mevarech M, Frolow F, Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86: 155-164.
33. Miller G (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal Chem 31: 426-428.
34. Mrudula S, Reddy G, Seenayya G (2011) Purification and characterization of highly thermostable amylopullulanase from a thermophilic, anaerobic bacterium Clostridiumthermosulfurogenes SVM17. MJM 7(2): 97-106.
35. Nair SU, Singhal RS, Kamat MY (2006) Enhanced production of thermostable pullulanase type 1 using Bacillus cereus FDTA 13 and its mutant. Food Technol Biotechnol 44(2): 275-282.
36. Nair SU, Singhal RS, Kamat MY (2007) Induction of pullulanase production in Bacillus cereus FDTA-13. Bioresour Technol 98: 856-859.
37. Niehaus F, Bertoldo C, Kähler M, Antranikian G (1999) Extremophiles as a source of novel enzymes for industrial application. Appl Microbiol Biotechnol 51: 711-729.
38. Oren A, Ventosa A, Grant W (1997) Proposed minimal standards for description of new taxa in the order Halobacteriales. Int J Syst Evol Microbiol 47: 233-238.
39. Perez-Pomares F, Ferrer J, Pire C, Marhuenda-Egea FC, Bonete MJ (2003) α-Amylase activity from the halophilic archaeon Haloferax mediterranei. Extremophiles 7: 299-306.
40. Prakash B, Madhukumar MS, Muralikrishna G, Sreeramulu K (2009) Production, purification, and characterization of two extremely halotolerant, thermostable, and alkali-stable a-amylases from Chromohalobacter sp. TVSP 101. Process Biochem 44: 210-215.
41. Saha B, Lamed R, Lee C, Mathupala S (1990) Characterization of an endo-acting amylopullulanase from Thermoanaerobacter Strain B6A. Appl Environ Microbiol 56: 881-886.
42. Sata H, Umeda M, Kim C-H, Taniguchi H, Maruyama Y (1989) Amylase-pullulanase enzyme produced by B. circulans F-2. Biochimica et Biophysica Acta (BBA) General Subjects 991: 388-394.
43. Shafiei M, Ziaee A, Amoozegar MA (2011) Purification and characterization of an organic-solvent-tolerant halophilic a-amylase from the moderately halophilic Nesterenkonia sp. strain F. J Ind Microbiol Biotechnol 38: 275-281.
44. 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.
45. Xin L, Yu YY (2012) Characterization of an organic solvent-tolerant α-amylase from a halophilic isolate, Thalassobacillus sp. LY18. Folia Microbiol 57: 447-453.
46. Zareian S, Khajeh K, Ranjbar B, Dabirmanesh B, Ghollasi M, Mollania N (2010) Purification and characterization of a novel amylopullulanase that converts pullulan to glucose, maltose, and maltotriose and starch to glucose and maltose. Enzyme Microbial Technol 46: 57-63.