Skip to main content
Log in

Purification, distribution, and characterization activity of lipase from oat seeds (Avena sativa L.)

  • Review
  • Published:
Journal of the Korean Society for Applied Biological Chemistry Submit manuscript

Abstract

Plant lipases have been chiefly studied as an esterase for hydrolyzation of triacylglycerol (a true lipase), which supplies energy for seed germination. Lipases are widely distributed in plants, animals, insects, and microorganisms. However, recent studies suggest that plant lipases have physiological functions other than triacylglycerol hydrolysis. In the present study, a plant lipase that has enzyme properties distinct from those of a true lipase was purified and characterized from oat seedlings. The lipase was purified 189-fold to a 0.53% purification ratio with high specific activity (34.656 U/mg). Analysis of the protein by Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed a homogenous purified lipase. The lipase had higher enzyme specificity to monoacylglyceride and short chain fatty acids. Synthesis of the lipase was active at an early stage of germination for 6 days and decreased thereafter. Most of the lipase was found in the upper part of the oat seedling excluding the root. Within the young leaves, the lipase is located only in vessels and sieve tubes. However, infection of a pathogen, Pseudomonas syrinae pv. oryzae, elevated the lipase synthesis. In addition, the lipase had an ability to hydrolyze E.coli lipopolysaccharide. These results suggested that oat lipase may play a physiological role in defense against pathogens.

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.

Institutional subscriptions

Similar content being viewed by others

References

  • Bhardwaj K, Raju A, and Rajasekharan R (2001) Identification, Purification, and Characterization of a Thermally Stable Lipase from Rice Bran. A New Member of the (Phospho) Lipase Family. Plant Physiology 127, 1728–1738.

    CAS  Google Scholar 

  • Cai S, Wang O, Wang M, He J, Wang Y, Zhang D et al. (2012) In vitro inhibitory effect on pancreatic lipase activity of subfractions from ethanol extracts of fermented oats (Avena sativa L.) and synergistic effect of three phenolic acids. J Agric Food Chem 60, 7245–7251.

    Article  CAS  Google Scholar 

  • de Sousa JS, Cavalcanti-Oliveira EdA, Aranda DAG, and Freire DMG (2010) Application of lipase from the physic nut (Jatropha curcas L.) to a new hybrid (enzyme/chemical) hydroesterification process for biodiesel production. Journal of Molecular Catalysis B: Enzymatic 65, 133–137.

    Article  Google Scholar 

  • Frédéric B, Ali T, Claude, and Robert (2000) Methods for lipase detection and assay a critical review. Eur J Lipid Sci Technol 102, 133–153.

    Article  Google Scholar 

  • Fuchs C, Vine N, and Hills MJ (1996) Purification and characterization of the acid lipase from the endosperm of castor oil seeds. Journal of Plant Physiology 149, 23–29.

    Article  CAS  Google Scholar 

  • Gimenez-Ibanez S and Rathjen JP (2010) The case for the defense: plants versus Pseudomonas syringae. Microbes Infect 12, 428–437.

    Article  CAS  Google Scholar 

  • Hasan F, Shah AA, and Hameed A (2006) Industrial applications of microbial lipases. Enzyme and Microbial Technology 39, 235–251.

    Article  CAS  Google Scholar 

  • Hasan F, Shah AA, and Hameed A (2009) Methods for detection and characterization of lipases: A comprehensive review. Biotechnol Adv 27, 782–798.

    Article  CAS  Google Scholar 

  • Katherine MS and John BO (2002) Lipid metabolism in plants. Biochemistry of Lipid: Lipoprotein and Membrane (4th ed.), pp. 97–130, Elsevier B. V., USA.

    Google Scholar 

  • Kishore JP, Manojkumar ZC, and Raghunath TM (2011) Lipase biodiversity. Indian Journal of Science and Technology 4(8), 971–982.

    Google Scholar 

  • Klose C and Arendt EK (2012) Proteins in oats; their synthesis and changes during germination: a review. Crit Rev Food Sci Nutr 52, 629–639.

    Article  CAS  Google Scholar 

  • Koeck M, Hardham AR, and Dodds PN (2011) The role of effectors of biotrophic and hemibiotrophic fungi in infection. Cell Microbiol 13, 1849–1857.

    Article  CAS  Google Scholar 

  • Konno K (2011) Plant latex and other exudates as plant defense systems: roles of various defense chemicals and proteins contained therein. Phytochemistry 72, 1510–1530.

    Article  CAS  Google Scholar 

  • Kwon SJ, Jin HC, Lee S, Nam MH, Chung JH, Kwon SI et al. (2009) GDSL lipase-like 1 regulates systemic resistance associated with ethylene signaling in Arabidopsis. Plant J 58, 235–245.

    Article  CAS  Google Scholar 

  • Lee DS, Kim BK, Kwon SJ, Jin HC, and Park OK (2009) Arabidopsis GDSL lipase 2 plays a role in pathogen defense via negative regulation of auxin signaling. Biochem Biophys Res Commun 379, 1038–1042.

    Article  CAS  Google Scholar 

  • Mew TW (1987) Current Status and Future Prospects of Research on Bacterial Blight of Rice. Ann Rev Phytopathol 25, 359–382.

    Article  Google Scholar 

  • Oh IS, Park AR, Bae MS, Kwon SJ, Kim YS, Lee JE et al. (2005) Secretome analysis reveals an Arabidopsis lipase involved in defense against Alternaria brassicicola. Plant Cell 17, 2832–2847.

    Article  CAS  Google Scholar 

  • Park YI, Do KH, Kim IS, and Park HH (2012) Structural and functional studies of casein kinase I-like protein from rice. Plant Cell Physiol 53, 304–311.

    Article  Google Scholar 

  • Patel MT, Nagarajan R, and Kilara A (1996) Lipase-Catalyzed Biochemical Reactions in Novel Media: A Review. Chemical Engineering Communications 152-3, 365–404.

    Article  Google Scholar 

  • Pierre V (2003) Plant lipases and their applications in oils and fats modification. Eur J Lipid Sci Technol 105, 308–317.

    Article  Google Scholar 

  • Reis P, Holmberg K, Watzke H, Leser ME, and Miller R (2009) Lipases at interfaces: a review. Adv Colloid Interface Sci 147–148, 237–250.

    Article  Google Scholar 

  • Rivera I, Mateos-Diaz JC, and Sandoval G (2012) Plant lipases: partial purification of Carica papaya lipase. Methods Mol Biol 861, 115–122.

    Article  CAS  Google Scholar 

  • Sahasrabudhe MR (1982) Measurement of Lipase Activity in Single Grains of Oat (Avena sativa L.). JAOCS 59(8), 354–355.

    CAS  Google Scholar 

  • Vajanti MP and Mumtaz AS (2002) Review of Enzymatic Properties of Lipase in Plants, Animals and microoranism. Pakistan Journal of Applied science 2(4), 474–484.

    Google Scholar 

  • Vijayakumar KR and Gowda LR (2013) Rice (Oryza sativa) lipase: molecular cloning, functional expression and substrate specificity. Protein Expr Purif 88, 67–79.

    Article  CAS  Google Scholar 

  • Volokita M, Rosilio-Brami T, Rivkin N, and Zik M (2011) Combining comparative sequence and genomic data to ascertain phylogenetic relationships and explore the evolution of the large GDSL-lipase family in land plants. Mol Biol Evol 28, 551–565.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to SangJun Moon.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jung, H., Moon, S. Purification, distribution, and characterization activity of lipase from oat seeds (Avena sativa L.). J Korean Soc Appl Biol Chem 56, 639–645 (2013). https://doi.org/10.1007/s13765-013-3119-4

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s13765-013-3119-4

Keywords

Navigation