Phenylalanine Ammonia-lyase Enzyme as a New Marker for Selection of Cyanobacteria for Absorption of Nickel in the Aquatic Environment

Authors

Department of Microbiology, Karaj Branch, Islamic Azad University, Karaj, Alborz, Iran

Abstract

Industrial activity can cause the release ofnickel into aquatic ecosystems with a negativeimpact on living organisms. Cyanobacteriahave an important role in regulating pollution,reducting dissolved nickel in water, and increasingthe mineral’s sedimentation. Recentlythe presence of phenylalanine ammonia lyaseenzyme has been proved in cyanobacteria.This study aims to investigate the correlationbetween phenylalanine ammonia lyase activityand the rate of nickel absorption. For thispurpose, a number of cyanobacteria Anabaenaspecies, endogenous to Iran, were prepared bydry and wet treatment with nickel. The nickeluptake was evaluated by atomic absorption andcomparison with a standard curve .The phenylalanineammonia lyase was extracted fromcyanobacteria and the enzyme activity wasmeasured at different pH values. The resultsshowed that some of the samples under studyhad remarkable ability to absorb nickel and thatthere were significant differences in the activityof the enzyme phenylalanine ammonia lyase atdifferent pH values. This study established therelationship between the level of activity of thisenzyme and the rate of nickel absorption.

Keywords

References

  1. Cain A, Vannela RL, Woo LK. (2008). Cyanobacteria
  2. as a biosorbent for mercuric ion. Bioresource Technology.
  3. : 6578–6586.
  4. Carrieri D, Wawrousek K, Eckert C, Yu J, Maness PC.
  5. (2011). The role of the bidirectional hydrogenase in
  6. cyanobacteria. Bioresource Technology. 102: 8368–
  7. Collier JL, Brahamsha B, Palenik B. (1999). The marine
  8. cyanobacterium Synechococcus sp. WH 7805
  9. requires urease (urea amiohydrolase, EC 3.5.1.5) to
  10. utilize urea as a nitrogen source: Molecular Genetic
  11. and biochemical analysis of the enzyme. Microbiology.
  12. : 447–459.
  13. Dixon RA and Paiva NL. (1995). Stress induced phenyl
  14. propanoid metabolism. Plant Cell. 7: 1085– 1097.
  15. Dupont CL, Johnson DA, Phillippy K, Paulsen IT, Brahamsha
  16. B, Palenik B. (2012). Genetic Identification
  17. of a High Affinity Ni Transporter and the Transcriptional
  18. Response to Ni Deprivation in Synechococcus
  19. sp. Strain WH8102. Applied Environmental Microbiology.
  20. : 7822–7832.
  21. Eckert C, Boehm M, Carrieri D, Yu J, Dubini A, Nixon
  22. PJ, Maness P. (2012). Genetic Analysis of the Hox
  23. Hydrogenase in the Cyanobacterium Synechocystis sp.
  24. PCC 6803 Reveals Subunit Roles in Association, Assembly,
  25. Maturation, and Function. Journal of Biology
  26. and Chemistry. 287: 43502– 43515.
  27. Hahlbrock K and Scheel D. (1989). Physiology and molecular
  28. biology of phenyl-propanoid metabolism. Annual
  29. Review Plant Physiology and Plant Molecular Biology.
  30. : 347–369.
  31. Kobayashi M and Shimizu S. (1999). Cobalt proteins.
  32. European Journal of Biochemistry. 261: 1–9.
  33. Lu-Sheng H, Yi-Lin H, Chuan-Shan Y, Chieh-Yang C,
  34. Chien-Chih Y, Ping-Du L. (2011). Molecular characterization
  35. of a phenylalanine ammonia-lyase gene (BoPAL1)
  36. from Bambusa oldhamii. Molecular Biology Reports.
  37. : 283-290.
  38. McIntosh CL, Germer F, Schulz R, Appel J, Jones AK.
  39. (2011). The [NiFe]-Hydrogenase of the Cyanobacterium
  40. Synechocystis sp. PCC 6803 Works Bidirectionally
  41. with a Bias to H 2 Production. Journal of American
  42. Chemistry Society. 133: 11308 –11319.
  43. Quintero MJ, Muro- Pastor, AM, Herrero A, Flores E
  44. (2000). Arginine catabolism in the cyanobacterium
  45. Synechocystis sp. Strain PCC 6803 involves the urea
  46. cycle and arginase pathway. Jouranl of Bacteriology.
  47. : 1008–1015.
  48. Ragsdale SW. (2009). Nickel-based Enzyme Systems.
  49. Journal of Biological Chemistry. 284: 18571–18575.
  50. Sigma (1998). https://www.sigmaaldrich.com/content/
  51. dam/sigma aldrich/docs/Sigma/ General Information/
  52. phenylalanine ammonia lyase l-phenylalanine as a substrate.

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