Applied Biochemistry and Biotechnology

, Volume 176, Issue 3, pp 924–937 | Cite as

Molecular Characterization of a Recombinant Zea mays Phenylalanine Ammonia-Lyase (ZmPAL2) and Its Application in trans-Cinnamic Acid Production from l-Phenylalanine

  • Ying Zang
  • Ting Jiang
  • Ying Cong
  • Zhaojuan Zheng
  • Jia OuyangEmail author


Phenylalanine ammonia-lyase (PAL) is one of the most extensively studied enzymes with its crucial role in secondary phenylpropanoid metabolism of plants. Recently, its demand has been increased for aromatic chemical production, but its applications in trans-cinnamic acid production were not much explored. In the present study, a putative PAL gene from Zea mays designated as ZmPAL2 was expressed and characterized in Escherichia coli BL21 (DE3). The recombinant ZmPAL2 exhibited a high PAL activity (7.14 U/mg) and a weak tyrosine ammonia-lyase activity. The optimal temperature of ZmPAL2 was 55 °C, and the thermal stability results showed that about 50 % of enzyme activity remained after a treatment at 60 °C for 6 h. The recombinant ZmPAL2 is a good candidate for the production of trans-cinnamic acid. The vitro conversion indicated that the recombinant ZmPAL2 could effectively catalyze the l-phenylalanine to trans-cinnamic acid, and the trans-cinnamic acid concentration can reach up to 5 g/l.


Zea mays Phenylalanine ammonia-lyase l-phenylalanine Enzyme properties trans-Cinnamic acid 



This study was supported by the National Natural Science Foundation of China (31200443), Program for New Century Excellent Talents in University (NCET-11-0988), and Excellent Youth Foundation of Jiangsu Province of China (BK2012038). The authors are also grateful to National Science and Technology Support Program (2012BAD32B06) and PAPD for partial funding of this study.


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Copyright information

© Springer Science+Business Media New York 2015

Authors and Affiliations

  • Ying Zang
    • 1
  • Ting Jiang
    • 2
  • Ying Cong
    • 2
  • Zhaojuan Zheng
    • 2
  • Jia Ouyang
    • 2
    • 3
    Email author
  1. 1.College of ForestryNanjing Forestry UniversityNanjingPeople’s Republic of China
  2. 2.College of Chemical EngineeringNanjing Forestry UniversityNanjingPeople’s Republic of China
  3. 3.Jiangsu Key Laboratory of Biomass-based Green Fuels and ChemicalsNanjingPeople’s Republic of China

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