Hostname: page-component-78c5997874-j824f Total loading time: 0 Render date: 2024-11-04T21:50:42.563Z Has data issue: false hasContentIssue false

Generation of hydrogen peroxide by a low molecular weight compound in whey of Holstein dairy cows

Published online by Cambridge University Press:  21 April 2008

Senkiti Sakai*
Affiliation:
Department of Animal Breeding, The Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan
Takahiro Satow
Affiliation:
Department of Cell Biology, The Graduate School of Bioresource Sciences, Nihon University, Kameino 1866, Fujisawa 252-8510, Japan
Kazuhiko Imakawa
Affiliation:
Department of Animal Breeding, The Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan
Kentaro Nagaoka
Affiliation:
Department of Animal Breeding, The Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan
*
*For correspondence; e-mail: [email protected]

Abstract

Using an ultrafiltration membrane (molecular cut-off, 3000), low molecular weight compounds in bovine milk were collected (YM-3 filtrate). A hydrogen peroxide (H2O2)-like substance was generated in the YM-3 filtrate. This substance was undetected at 0 h, but increased in a time-dependent manner, peaking after 2 h of incubation at 38°C. After incubating the YM-3 filtrate with catalase and lactoperoxidase, the signal showing the presence of this substance disappeared. The substance was quantified using one chemiluminescence and three colorimetric H2O2 detection systems. In all systems, their estimates were within the same range. The amount of substance, as estimated by the chemiluminescence H2O2 detection system, was correlated with that estimated by the other three colorimetric systems (r=0·98, 0·95 and 0·87). The substance was eluted at the same position as H2O2 by gel filtration on Superdex 30. Thus, the substance had the same characteristics as H2O2. An H2O2-generating substance in either the YM-3 filtrate or whey had a molecular mass of about 600. In this study, we clarify that bovine milk is capable of generating H2O2 by utilizing a low molecular weight compound. Thus, we present a new type of H2O2-supplying system in bovine milk.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Althaus, RL, Molina, MP, Rodríguez, M & Fernández, N 2001 Analysis time and lactation stage influence on lactoperoxidase system components in dairy ewe milk. Journal of Dairy Science 84 18291835CrossRefGoogle ScholarPubMed
Barett, NE, Grandison, AS & Lewis, MJ 1999 Contribution of the lactoperoxidase system to the keeping quality of pasteurized milk. Journal of Dairy Research 66 7380CrossRefGoogle Scholar
Björck, L 1978 Antibacterial effect of the lactoperoxidase system on psychrotrophic bacteria in milk. Journal of Dairy Research 45 109118CrossRefGoogle ScholarPubMed
Björck, LC & Claesson, O 1979 Xanthine oxidase and as a source of hydrogen peroxide for the lactoperoxidase system in milk. Journal of Dairy Science 62 12111215CrossRefGoogle Scholar
Björck, L, Rosen, CG, Marshall, V & Reiter, R 1975 Antibacterial activity of the lactoperoxidase system in milk against pseudomonads and other Gram-negative bacteria. Applied Microbiology 30 199204CrossRefGoogle ScholarPubMed
Brieley, MS & Eisenthal, R 1974 Association of xanthine oxidase with the bovine milk-fat-globule membrane: catalytic properites of the free and membrane-bound enzyme. Biochemical Journal 143 149157CrossRefGoogle Scholar
Ekstrand, B 1989 Antimicrobial factors in milk—a review. Food Biotechnology 3 105126.CrossRefGoogle Scholar
Escribano, J, Garcia-Canovas, F & Garcia-Carmona, R 1988 A kinetic study of hypoxanthine oxidation by milk xanthine oxidase. Biochemical Journal 254 829833CrossRefGoogle ScholarPubMed
Fonteh, FA, Grandison, AS & Lewis, MJ 2002 Variations of lactoperoxidase activity and thiocyanate content in cows' and goats' milk throughout lactation. Journal of Dairy Research 69 401409CrossRefGoogle ScholarPubMed
Furtmüller, PG, Jantschko, W, Regesberger, G, Jakopitsch, C, Arnhold, J & Obinger, C 2002 Reaction of lactoperoxidase compound I with halides and thiocyanate. Biochemistry 41 1189511900CrossRefGoogle ScholarPubMed
Imai, K, Nawa, H, Tanaka, M & Ogata, H 1986 Novel aryl oxalate esters for peroxyoxalate chemiluminescence reactions. Analyst 111 209211CrossRefGoogle Scholar
Jiang, Z-Y, Woollard, ACS & Wolff, SP 1990 Hydrogen peroxide production during experimental protein glycation. FEBS Letters 268 6971CrossRefGoogle ScholarPubMed
Korhonen, HJ & Reiter, B 1983 Production of H2O2 by bovine blood and milk polymorphonuclear leucocytes. Acta Microbiology Poland 32 5364Google ScholarPubMed
Morr, CV & Swenson, PE 1973 Milk ultracentrifugal opalescent layer. 3. Yield and casein and lipid composition as a function of centrifugation time. Journal of Dairy Science 56 13891395CrossRefGoogle Scholar
Pick, E 1986 Microassays for superoxide and hydrogen peroxide production and nitroblue tetrazolium reduction using an enzyme immunoasay microplate reader. In Methods in Enzymology Vol. 132 (Eds Sabato, GD & Everse, J) pp. 407421. New York NY, USA: Academic PressGoogle Scholar
Pruitt, KM, Tenovuo, J, Andrews, RW & McKane, T 1982 Lactoperoxidase-catalysed oxidation of thiocyanate: polarographic study of the oxidation products. Biochemistry 21 562567CrossRefGoogle Scholar
Reiter, B & Harnulv, BG 1984 Lactoperoxidase antibacterial system: natural occurrence, biological functions and practical applications. Journal of Food Protection 47 724732CrossRefGoogle ScholarPubMed
Schiffman, AP, Schültz, M & Wiesner, H 1992 False negative and postitve results in testing for inhibitory substances in milk. Factors influencing the brillant black reduction test (BRT®). Milchwiessenshaft 65 325331Google Scholar
Shindler, JS & Bardsley, WG 1975 Steady-state kinetics of lactoperoxidase with ABTS as chromogen. Biochemical and Biophysical Research Communications 67 13071312CrossRefGoogle ScholarPubMed
Sun, Y, Nonobe, E, Kobayashi, Y, Kuraishi, T, Aoki, F, Yamamoto, K & Sakai, S 2002 Characterization and expression of L-amino acid oxidase of mouse milk. Journal of Biological Chemistry 277 1908019086CrossRefGoogle ScholarPubMed
Tiemeyer, W, Stohrer, M & Giesecke, D 1984 Metabolites of nucleic acids in bovine milk. Journal of Dairy Science 67 723728CrossRefGoogle ScholarPubMed
Thomas, EL, Bonezan, PM & Learn, DB 1991 Lactoperoxidase: structure and catalytic properties. In: Peroxidases in Chemistry and Biology Vol. 1 (Eds Everse, J, Everse, KE & Grisham, MB) pp. 123142. Boston MA, USA: CRC PressGoogle Scholar
Upadhayay, KG 1992 Pre-treatment of milk for cheese manufacture and their significance. Indian Dairyman 44 2644Google Scholar
Wolfson, LM & Summer, SA 1993 Antibacterial activity of the lactoperoxidase system: a review. Journal of Food Protection 56 887892CrossRefGoogle ScholarPubMed
Zapico, P, Gaya, P, De Paz, M, Nuñez, M & Medina, M 1991 Influence of breed, analysis and days of lactation on lactoperoxidase system components in goat milk. Journal of Dairy Science 74 783787CrossRefGoogle ScholarPubMed