Optimization of fermentation conditions for cold-adapted amylase production by micrococcus antarcticus and its enzymatic properties

Huanjing Kexue/Environmental Science

Volumn 30, Issue 8, 2009, Pages 2473-2478

  Fan, Hong Xia ^a,b   Liu, Ying ^a   Liu, Zhi Pei ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Cold adapted amylase; Enzymatic properties; Fermentation conditions; Micrococcus antarcticus

Indexed keywords

AMYLASE;

ADAPTATION; ARTICLE; BIOSYNTHESIS; COLD; ENZYME STABILITY; ENZYMOLOGY; FERMENTATION; METABOLISM; MICROBIOLOGY; MICROCOCCUS; PHYSIOLOGY;

ADAPTATION, PHYSIOLOGICAL; AMYLASES; COLD TEMPERATURE; ENZYME STABILITY; FERMENTATION; INDUSTRIAL MICROBIOLOGY; MICROCOCCUS;

EID: 69449083093     PISSN: 02503301     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. 1998. 458-489.
2. Margesin R, Schinner F. Biodegradation of organic pollutants at low temperatures[A]. In: Biotechnological Applications of Cold-adapted Organisms[M]. Berlin; New York: Springer, 1999. 271-289.
3. 2007, 34(4): 63-66.
4. Gerday C, Aittaleb M, Bentahir M, et al. Cold-adapted enzymes: from fundamentals to biotechnology[J]. Trends in Biotechnology, 2000, 18(3): 103-107.
5. Adrienne L, Huston. Biotechnological Aspects of Cold-Adapted Enzymes[A]. In: Psychrophiles: From Biodiversity to Biotechnology[M]. Berlin; New York: Springer, 2008. 347-360.
6. Aghajari N, Feller G, Gerday C, et al. Structures of the psychrophilie Alteromonas haloplantics α-amylase give sight into cold adaption at a molecular level[J]. Structure, 1998, 6(12): 1503-1516.
7. Feller G, Payan F, Theys F, et al. Stability and structural analysis of α-amylase from the Antarctic psychrophile Alteromonas haloplantics A23[J]. Eur J Biochem, 1994, 222(2): 441-447.
8. 2002, 26(2): 3-5.
9. 2005, 27(4): 615-618.
10. Zhang J W, Zeng R Y. Purification and Characterization of a Cold-Adapted α-Amylase Produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic[J]. Mar biotechnol (NY), 2008, 10(1): 75-82.
11. 2006. 14-32.
12. Liu H C, Xu Y, Ma Y H, et al. Characterization of Micrococcus antarcticus sp. nov., a psychrophilic bacterium from Antarctica[J]. Int J Syst Evol Microbiol, 2000, 50: 715-719.
13. Kaminski U, Janke D, Prauser H, et al. Degradation of anilline and monochloroanilines by Rhodococcus sp. An117 and a pseudomonad: a comparative study[J]. Z Allg Mikrobiol, 1983, 23(4): 235-246.
14. Miller G L. Use of dinitrosalicylic acid reagent for determination of reducing sugars[J]. Anal Chem, 1959, 31(3): 426-428.
15. 1998. 332.
16. 2004. 356-360.
17. Lineweaver H, Burk D. The determination of enzyme dissociation constants[J]. J Amer Chem Soc, 1934, 56(3): 658-666.
18. Onishi H. Halophilic amylase from a moderately Micrococcus[J]. J Bacteriol, 1972, 109(2): 570-572.
19. Khire J M, Pant A. Thermostable, salt-tolerant amylase from Bacillus sp. 64[J]. World J Microbiol, 1992, 8(2): 167-170.
20. Feller G, Lonhienne T, Deroanne C, et al. Purification, characterization and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplantics A23[J]. J Biol Chem, 1992, 267(8): 5217-5221.
21. 2007. 23-30.
22. 2006, 12(5): 683-687.
23. 2007, 31(1): 27-32.
24. Feller G, Gerday C. Psychrophilic enzymes: hot topic in cold adaptation[J]. Nat Rev Microbiol, 2003, 1(3): 200-208.
25. Gupta R, Gigras P, Mohapatra H, et al. Microbial α-amylase: a biotechnological perspective[J]. Process Biochem, 2003, 38(11): 1599-1616.
26. 2007, 17(2): 34-37.
27. Hoyoux A, Blaise V, Collins T, et al. Extreme Catalysts from Low-Temperature Environments[J]. Journal of bioscience and Bioengineering, 2004, 98(5): 317-330.