Hostname: page-component-cd9895bd7-jkksz Total loading time: 0 Render date: 2024-12-25T00:56:08.988Z Has data issue: false hasContentIssue false
  • English
  • Français

Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications

Published online by Cambridge University Press:  09 March 2007

Klaas D. Kussendrager  and
A. C. M. van Hooijdonk
Klaas D. Kussendrager*
Affiliation:
DMV-International, R&D Center, PO Box 13, 5460 BA Veghel, The Netherlands
A. C. M. van Hooijdonk
Affiliation:
DMV-International, R&D Center, PO Box 13, 5460 BA Veghel, The Netherlands
*
*Corresponding author: Klaas D. Kussendrager, email [email protected]
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Lactoperoxidase (LP) is one of the most prominent enzymes in bovine milk and catalyses the inactivation of a wide range of micro-organisms in the lactoperoxidase system (LP-s). LP-systems are also identified as natural antimicrobial systems in human secretions such as saliva, tear-fluid and milk and are found to be harmless to mammalian cells. The detailed molecular structure of LP is identified and the major products generated by the LP-s and their antimicrobial action have been elucidated for the greater part. In this paper several aspects of bovine LP and LP-s are discussed, including physico-chemical properties, occurrence in milk and colostrum and mechanisms of action. Since the introduction of industrial processes for the isolation of LP from milk and whey the interest in this enzyme has increased considerably and attention will be paid to potential and actual applications of LP-systems as biopreservatives in food and other products.

Keywords

LactoperoxidaseLP-systemAntimicrobial propertiesApplications
Type
Research Article
Information
British Journal of Nutrition , Volume 84 , Issue S1 , November 2000 , pp. 19 - 25
Copyright
Copyright © The Nutrition Society 2000

References

Bardsley, WC (1985) Steady-state kinetics of lactoperoxidase-catalysed reactions. In The Lactoperoxidase System, Chemistry and Biological Significance, pp. 55–83 [Pruit, KM and Tenovuo, JO, editors]. New York: Marcel Dekker .Google Scholar
Booth, KS, Kimura, S, Lee, HC, Ikeda-Saito, M and & Caughey, WS (1989) Bovine myeloperoxidase and lactoperoxidase each contain a high affinity binding site for calcium. Biochemical and Biophysical Research Communications 160, 879–902.CrossRefGoogle ScholarPubMed
Boots, MicroCheck (1992) Natural biocide comes fresh from the dairy Cosmetics & Toiletries Manufacturers & Suppliers (CTMS) 6–2, 35.Google Scholar
Cals, MM, Mailliart, P, Brignon, G, Anglade, P & Ribadeau Dumas, B (1991) Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. European Journal of Biochemistry 198, 733–738.CrossRefGoogle ScholarPubMed
Carlstrom, A (1969) Lactoperoxidase, Identification of multiple molecular forms and their relationships. Acta Chemica Scandinavica 23, 171–184.CrossRefGoogle Scholar
de Wit, JN & van Hooydonk, ACM (1996) Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Netherlands Milk & Dairy Journal 50, 227–244.Google Scholar
Dosako, S (1991) Lactic acid bacterium starter containing peroxidase, fermented milk product, and production thereof European Patent Application.Google Scholar
Ekstrand, B (1994) Lactoperoxidase and lactoferrin. In Natural Antimicrobial Systems and Food Preservation, pp.15–63 [Dillon, VM and Board, RG, editors] Wallingford: CAB International.Google Scholar
Godfrey, DC (1990) Anti-microbial compositions European Patent Specification.Google Scholar
Guthrie, WG (1992) A novel adaptation of a naturally occurring antimicrobial system for cosmetic protection. SOFW-Journal 118, 556–562.Google Scholar
Heràndez, CMM, van Markwijk, BW & Vreeman, HJ (1990) Isolation and properties of lactoperoxidase from bovine milk. Netherlands Milk and Dairy Journal 44, 213–231.Google Scholar
Hoogendoorn, H (1985) Activation of the salivary peroxidase antimicrobial system: clinical studies. In The Lactoperoxidase System, Chemistry and Biological Significance, pp.217–227 [Pruitt, KM and Tenovuo, JO, editors].New York: Marcel Dekker.Google Scholar
Hu, S, Treat, RW & Kincaid, JR (1993) Distinct heme active-site structure in lactoperoxidase revealed by resonance raman spectroscopy. Biochemistry 32, 10125–10130.CrossRefGoogle ScholarPubMed
Kiermeier, F & Kayser, C (1960) Zur Kenntnis der Lactoperoxidase. Zeitschrift für Lebensmittel-Untersuchung und-Forschung 112, 481–498.CrossRefGoogle Scholar
Korhonen, H (1977) Antimicrobial factors in bovine colostrum. Journal of the Scientific Agriculture Society of Finland 49, 434–447.Google Scholar
Korhonen, HJ & Reiter, B (1983) Production of H2O2 by bovine blood and milk polymorphonuclear leucocytes. Acta Microbiologica Polonica 32, 53–64.Google ScholarPubMed
Modi, S, Behere, DV & Mitra, S (1989) Binding of thiocyanate to lactoperoxidase: 1H and 15N nuclear resonance studies. Biochemistry 28, 4689–4694.CrossRefGoogle ScholarPubMed
Nakada, M, Dosako, S, Hirano, R, Ooka, M & Nakajima, I (1996) Lactoperoxidase suppresses acid production in yoghurt during storage under refrigeration. International Dairy Journal 6, 33–42.CrossRefGoogle Scholar
Paul, KG (1963) Peroxidases The Enzymes, pp.27–274Boyer, PD, Lardy, H and Myrback, K, editors]. New York: Academic Press.Google Scholar
Paul, KG & Ohlsson, PI (1985) The chemical structure of lactoperoxidase. In The Lactoperoxidase System, Chemistry and Biological Significance, pp.15–29 [Pruitt, KM and Tenovuo, JO, editors] New York: Marcel Dekker.Google Scholar
Pellico, MA & Montgomery, RE (1989) Di-enzymatic dentrifice European Patent Specification.Google Scholar
Pruitt, KM & Kamau, DN (1993) Quantitative analysis of bovine lactoperoxidase system components and of the effects of the activated system on bacterial growth and survival. In Proceedings of the IDF Seminar Indigenous Antimicrobial Agents of Milk, Recent Developments, pp. 73–87.Google Scholar
Reiter, B, Härnulv, G (1984) Lactoperoxidase antibacterial system: natural occurrence, biological functions and practical applications. Journal of Food Protection 47, 724–732.Google ScholarPubMed
Reiter, B & Perraudin, JP (1991) Lactoperoxidase: biological. In functions Peroxydases in Chemistry and Biology, pp.143–180. Boca Raton: CRC Press.Google Scholar
Sievers, G (1979) The prosthetic group of milk peroxidase is protehym IX. Biochimica et Biophysica Acta 579, 181–190.CrossRefGoogle ScholarPubMed
Sievers, G (1980) Structure of milk lactoperoxidase. A study using circular dichroism and difference absorption spectroscopy. Biochimica et Biophysica Acta 624, 249–259.CrossRefGoogle ScholarPubMed
Thanabal, V & La Mar, GN (1989) A nuclear Overhauser effect investigation of the molecular and electronic structure of the heme crevice in lactoperoxidase. Biochemistry 28, 7038–7044.CrossRefGoogle ScholarPubMed
Thomas, EL (1985) Products of lactoperoxidase-catalyzed oxidation of thiocyanate and halides. In The Lactoperoxidase System, Chemistry and Biological Significance, pp.31–53 [Pruitt, KM and Tenovuo, JO, editors]. New York: Marcel Dekker.Google Scholar
Wolfson, LM & Sumner, SS (1993) Antimicrobial activity of the lactoperoxidase system. A review. Journal of Food Protection 56, 887–892.CrossRefGoogle Scholar
Zeng, J & Fenna, RE (1992) X-ray crystal structure of canine myeloperoxidase at 3 Å resolution. Journal of Molecular Biology 226, 185–207.CrossRefGoogle ScholarPubMed