Skip to main content
Log in

Plant phospholipases A2: perspectives on biotechnological applications

  • Review
  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

The recent progress in knowledge on biochemical properties and functions of phospholipases A2 in plants paved the way for approving the suitability of these enzymes for commercial use now. The secreted phospholipases A2, representing one type of phospholipases A2 occurring in plants, show distinct differences in substrate specificities with respect to headgroup and acyl chains of the glycerophospholipids in comparison to their counterparts from animal sources. The other type of phospholipases A2 in plants, the patatin-related phospholipases A2, is characterized by broad substrate specificity. Accordingly, the unique properties of the plant enzymes open new horizons to engineered biocatalysts with improved performance, e.g., for vegetable oil refinement by degumming and for targeted modification of phospholipids.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  • Alferez F, Lluch Y, Burns JK (2008) Phospholipase A2 and postharvest peel pitting in citrus fruit. Postharvest Biol Technol 49:69–76

    Article  CAS  Google Scholar 

  • Balsinde J, Balboa MA (2005) Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells. Cell Signal 17:1052–1062

    Article  PubMed  CAS  Google Scholar 

  • Bezzine S, Bollinger JG, Singer AG et al (2002) On the binding preference of human groups IIA and X phospholipases A2 for membranes with anionic phospholipids. J Biol Chem 277:48523–48534

    Article  PubMed  CAS  Google Scholar 

  • Burke JE, Dennis EA (2009) Phospholipase A2 structure/function, mechanism and signaling. J Lipid Res 50:S237–S242

    Article  PubMed  CAS  Google Scholar 

  • Chojnacka A, Gladkowski W, Kielbowicz G et al (2009) Enzymatic enrichment of egg-yolk phosphatidylcholine with a-linolenic acid. Biotechnol Lett 31:705–709

    Article  PubMed  CAS  Google Scholar 

  • de Maria L, Vind J, Oxenboll KM et al (2007) Phospholipases and their industrial applications. Appl Microbiol Biotechnol 74:290–300

    Article  PubMed  CAS  Google Scholar 

  • Dessen A, Tang J, Schmidt H et al (1999) Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Cell 97:349–360

    Article  PubMed  CAS  Google Scholar 

  • Dhondt S, Geoffroy P, Stelmach BA et al (2000) Soluble phospholipase A2 activity is induced before oxylipin accumulation in tobacco mosaic virus-infected tobacco leaves and is contributed by patatin-like enzymes. Plant J 23:431–440

    Article  PubMed  CAS  Google Scholar 

  • Fujikawa R, Fujikawa Y, Iijima N et al (2005) Molecular cloning, expression, and characterization of secretory phospholipase A2 in tobacco. Lipids 40:901–908

    Article  PubMed  CAS  Google Scholar 

  • Ghomashchi F, Yu BZ, Berg O et al (1991) Interfacial catalysis by phospholipase A2: substrate specificity in vesicles. Biochemistry 30:7318–7329

    Article  PubMed  CAS  Google Scholar 

  • Ghosh M, Tucker DE, Burchett SA et al (2006) Properties of the Group IV phospholipase A2 family. Prog Lipid Res 45:487–510

    Article  PubMed  CAS  Google Scholar 

  • Guo Z, Vikbjerg AF, Xu X (2005) Enzymatic modification of phospholipids for functional applications and human nutrition. Biotechnol Adv 23:203–259

    Article  PubMed  CAS  Google Scholar 

  • Hirschberg HJ, Simons JW, Dekker N et al (2001) Cloning, expression, purification and characterization of patatin, a novel phospholipase A. Eur J Biochem 268:5037–5044

    Article  PubMed  CAS  Google Scholar 

  • Holk A, Rietz S, Zahn M et al (2002) Molecular identification of cytosolic, patatin-related phospholipases A from Arabidopsis with potential functions in plant signal transduction. Plant Physiol 130:90–101

    Article  PubMed  CAS  Google Scholar 

  • Iwasaki Y, Yamane T (2004) Enzymatic synthesis of structured lipids. Adv Biochem Eng Biotechnol 90:151–157

    PubMed  CAS  Google Scholar 

  • Katsir L, Chung HS, Koo AJ et al (2008) Jasmonate signaling: a conserved mechanism of hormone sensing. Curr Opin Plant Biol 11:428–435

    Article  PubMed  CAS  Google Scholar 

  • Kienesberger PC, Oberer M, Lass A et al (2009) Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J Lipid Res 50:S63–S68

    Article  PubMed  CAS  Google Scholar 

  • Kim JY, Chung YS, Ok SH et al (1999) Characterization of the full-length sequences of phospholipase A2 induced during flower development. Biochim Biophys Acta 1489:389–392

    PubMed  CAS  Google Scholar 

  • Lee HY, Bahn SC, Kang YM et al (2003) Secretory low molecular weight phospholipase A2 plays important roles in cell elongation and shoot gravitropism in Arabidopsis. Plant Cell 15:1990–2002

    Article  PubMed  CAS  Google Scholar 

  • Lee HY, Bahn SC, Shin JS et al (2005) Multiple forms of secretory phospholipases A2 in plants. Prog Lipid Res 44:52–67

    Article  PubMed  CAS  Google Scholar 

  • Lubertozzi D, Keasling JD (2009) Developing Aspergillus as a host for heterologous expression. Biotechnol Adv 27:53–75

    Article  PubMed  CAS  Google Scholar 

  • Mansfeld J, Ulbrich-Hofmann R (2007) Secretory phospholipase A2-a from Arabidopsis thaliana: functional parameters and substrate preference. Chem Phys Lipids 150:156–166

    Article  PubMed  CAS  Google Scholar 

  • Mansfeld J, Gebauer S, Dathe K et al (2006) Secretory phospholipase A2 from Arabidopsis thaliana: insights into the three-dimensional structure and the amino acids involved in catalysis. Biochemistry 45:5687–5694

    Article  PubMed  CAS  Google Scholar 

  • Munnik T, Testerink C (2009) Plant phospholipid signaling—‘in a nutshell’. J Lipid Res 50:S260–S265

    Article  PubMed  CAS  Google Scholar 

  • Murakami M, Kudo I (2002) Phospholipase A2. J Biochem 131:285–292

    PubMed  CAS  Google Scholar 

  • Murakami M, Kudo I (2004) Secretory phospholipase A2. Biol Pharm Bull 27:1158–1164

    Article  PubMed  CAS  Google Scholar 

  • Nevalainen KM, Te’o VS, Bergquist PL (2005) Heterologous protein expression in filamentous fungi. Trends Biotechnol 23:468–474

    Article  PubMed  CAS  Google Scholar 

  • Ollis DL, Cheah E, Cygler M et al (1992) The alpha/beta hydrolase fold. Protein Eng 5:197–211

    Article  PubMed  CAS  Google Scholar 

  • Pattus F, Slotboom AJ, de Haas GH (1979) Regulation of phospholipase A2 activity by the lipid–water interface: a monolayer approach. Biochemistry 18:2691–2697

    Article  PubMed  CAS  Google Scholar 

  • Pikaard CS, Brusca JS, Hannapel DJ et al (1987) The two classes of genes for the major potato tuber protein, patatin, are differentially expressed in tubers and roots. Nucleic Acids Res 15:1979–1994

    Article  PubMed  CAS  Google Scholar 

  • Rietz S, Holk A, Scherer GF (2004) Expression of the patatin-related phospholipase A gene AtPLA IIA in Arabidopsis thaliana is up-regulated by salicylic acid, wounding, ethylene, and iron and phosphate deficiency. Planta 219:743–753

    Article  PubMed  CAS  Google Scholar 

  • Roos W, Viehweger K, Dordschbal B et al (2006) Intracellular pH signals in the induction of secondary pathways—the case of Eschscholzia californica. J Plant Physiol 163:369–381

    Article  PubMed  CAS  Google Scholar 

  • Rydel TJ, Williams JM, Krieger E et al (2003) The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry 42:6696–6708

    Article  PubMed  CAS  Google Scholar 

  • Ryu SB, Lee HY, Hwang IW et al (2008) Transgenic plants with increased resistance to biotic and abiotic stresses and accelerated flowering time due to overexpression of a secretory phospholipase A2 (sPLA2). PCT Int Appl Patent WO 2008100112

  • Schaloske RH, Dennis EA (2006) The phospholipase A2 superfamily and its group numbering system. Biochim Biophys Acta 1761:1246–1259

    PubMed  CAS  Google Scholar 

  • Schwendener RA (2007) Liposomes in biology and medicine. Adv Exp Med Biol 620:117–128

    Article  PubMed  Google Scholar 

  • Senda K, Yoshioka H, Doke N et al (1996) A cytosolic phospholipase A2 from potato tissues appears to be patatin. Plant Cell Physiol 37:347–353

    PubMed  CAS  Google Scholar 

  • Seo J, Lee HY, Choi H et al (2008) Phospholipase A2b mediates light-induced stomatal opening in Arabidopsis. J Exp Bot 59:3587–3594

    Article  PubMed  CAS  Google Scholar 

  • Sonnewald U, Sturm A, Chrispeels NJ et al (1989) Targeting and glycosylation of patatin the major potato tuber protein in leaves of transgenic tobacco. Planta 179:171–181

    Article  CAS  Google Scholar 

  • Stahl U, Ek B, Stymne S (1998) Purification and characterization of a low-molecular-weight phospholipase A2 from developing seeds of elm. Plant Physiol 117:197–205

    Article  PubMed  CAS  Google Scholar 

  • Stahl U, Lee M, Sjodahl S et al (1999) Plant low-molecular-weight phospholipase A2S (PLA2s) are structurally related to the animal secretory PLA2s and are present as a family of isoforms in rice (Oryza sativa). Plant Mol Biol 41:481–490

    Article  PubMed  CAS  Google Scholar 

  • Wang X, Wang C, Sang Y et al (2002) Networking of phospholipases in plant signal transduction. Physiol Plant 115:331–335

    Article  PubMed  CAS  Google Scholar 

  • Watanabe J, Ishihara K (2008) Establishing ultimate biointerfaces covered with phosphorylcholine groups. Colloids Surf B Biointerfaces 65:155–165

    Article  PubMed  CAS  Google Scholar 

  • Zhang AL, Luo JX, Zhang TY et al (2008) Recent advances on the GAP promoter derived expression system of Pichia pastoris. Mol Biol Rep. doi:10.1007/s11033-008-9359-4

    Google Scholar 

Download references

Acknowledgment

I thank Prof. Renate Ulbrich-Hofmann for critical reading of the manuscript and appreciate her continuous support throughout all of time.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Johanna Mansfeld.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary material 1 (DOC 534 kb)

Rights and permissions

Reprints and permissions

About this article

Cite this article

Mansfeld, J. Plant phospholipases A2: perspectives on biotechnological applications. Biotechnol Lett 31, 1373–1380 (2009). https://doi.org/10.1007/s10529-009-0034-1

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10529-009-0034-1

Keywords

Navigation