Thiocyanate mediated antifungal and antibacterial property of goat milk lactoperoxidase

Jacob, Benoy; Antony, K Essy; Sreekumar, B; Haridas, M.

doi:10.1016/s0024-3205(00)80003-x

Cited by 55 publications

(33 citation statements)

References 12 publications

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“…Thus, the lactoperoxidase-thiocyanate-hydrogen peroxide system can be not only fungistatic [44] but also fungicidal for Candida albicans; independently, it is phosphate-buffered at salivary concentrations or higher.…”

Section: Discussionmentioning

confidence: 99%

Effect of lactoperoxidase on the antimicrobial effectiveness of the thiocyanate hydrogen peroxide combination in a quantitative suspension test

Welk

Meller

Schubert³

et al. 2009

BMC Microbiology

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BackgroundThe positive antimicrobial effects of increasing concentrations of thiocyanate (SCN-) and H2O2 on the human peroxidase defence system are well known. However, little is known about the quantitative efficacy of the human peroxidase thiocyanate H2O2 system regarding Streptococcus mutans and sanguinis, as well as Candida albicans. The aim of this study was to evaluate the effect of the enzyme lactoperoxidase on the bactericidal and fungicidal effectiveness of a thiocyanate-H2O2 combination above the physiological saliva level. To evaluate the optimal effectiveness curve, the exposure times were restricted to 1, 3, 5, and 15 min.ResultsThe bactericidal and fungicidal effects of lactoperoxidase on Streptococcus mutans and sanguinis and Candida albicans were evaluated by using two test mixtures of a 2.0% (w/v; 0.34 M) thiocyanate and 0.4% (w/v; 0.12 M) hydrogen peroxide solution, one without and one with lactoperoxidase. Following the quantitative suspension tests (EN 1040 and EN 1275), the growth of surviving bacteria and fungi in a nutrient broth was measured. The reduction factor in the suspension test without lactoperoxidase enzyme was < 1 for all three tested organisms. Thus, the mixtures of 2.0% (w/v; 0.34 M) thiocyanate and 0.4% (w/v; 0.12 M) hydrogen peroxide had no in vitro antimicrobial effect on Streptococcus mutans and sanguinis or Candida albicans. However, the suspension test with lactoperoxidase showed a high bactericidal and fungicidal effectiveness in vitro.ConclusionThe tested thiocyanate and H2O2 mixtures showed no relevant antimicrobial effect. However, by adding lactoperoxidase enzyme, the mixtures became not only an effective bactericidal (Streptococcus mutans and sanguinis) but also a fungicidal (Candida albicans) agent.

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Section: Discussionmentioning

confidence: 99%

Effect of lactoperoxidase on the antimicrobial effectiveness of the thiocyanate hydrogen peroxide combination in a quantitative suspension test

Welk

Meller

Schubert³

et al. 2009

BMC Microbiology

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“…Antibacterial activity of bovine lactoperoxidase was done by disc diffusion method of Baer-Kirby using Mueller-Hinton Agar Medium with slight modification [14,22] and compared with well known antibacterial substances such as penicilline, ampicilline, ceftriaxon and amoxicillin-clavulanate. For [14].…”

Section: Materials and Metodsmentioning

confidence: 99%

“…As shown in the figure, bovine lactoperoxidase have molecular weight about 80000 Da. LPO isolated from camel milk are found to be antibacterial even in the absence of a medium containing thiocyanate-H 2 O 2 [14]. LPO can exert a bacteriostatic effect on both Gram-positive and Gram-negative bacteria [23].…”

Section: Materials and Metodsmentioning

confidence: 99%

“…It was reported that most pathogenic bacteria are inhibited by a medium containing thiocyanate-H 2 O 2 [24]. LPO-thiocyanate-H 2 O 2 system is effective as agent against many of the diseases caused by organisms in plants and animals [14,15]. The enzyme lactoperoxidase catalyzes the oxidation of thiocyanate by hydrogen peroxide, yielding short oxidation products, as hypothiocyanite ions responsible for the antimicrobial effect [25].…”

Section: Materials and Metodsmentioning

confidence: 99%

“…Lactoperoxidase isolated from goat milk is found to be antibacterial with thiocyanate-H 2 O 2 medium [14] of the A. hydrophila, Citrobacter freundi, E. coli, K. pneumoniae, P. mirabilis, Shigella dysenterioe, S. sonnei, P. aeruginosa, Salmonella enteritidis, S. schotmuelleri, S. typhi, Serratia marcescens. In another study, LPO was isolated from goat milk and its antibacterial prop-erties have been investigated for exploring the possibilities of developing it as an agent to help fight against diseases [15].…”

Section: Materials and Metodsmentioning

confidence: 99%

See 2 more Smart Citations

Purification of Bovine Milk Lactoperoxidase and Investigation of Antibacterial Properties at Different Thiocyanate Mediated

Uğuz

Özdemir

2005

Appl Biochem Microbiol

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Bovine lactoperoxidase ( LPO ) was purified with amberlite CG 50 H + resin, CM sephadex C-50 ion-exchange chromatography, and sephadex G-100 gel filtration chromatography from skim milk. The activity of lactoperoxidase was measured by using 2.2-azino-bis(3-ethylbenzthiazoline-6 sulfonic acid) diammonium salt ( ABTS ) as a choromogenic substrate at pH 6.0. Purification degree for the purified enzyme was controlled with SDS-PAGE and R z value ( A 412 / A 280 ). R z value for the purified LPO was 0.8. K m value at pH 6.0 at 20 ° C for the LPO was 0.20 mM. V max value was 7.87 µ mol/ml min at pH 6.0 at 20 ° C. Bovine LPO showed high antibacterial activity in 100 mM thiocyanate -100 mM H 2 O 2 medium for some pathogenic bacteria, such as Aeromonas hydrophila ATCC 7966, Micrococcus luteus LA 2971, Mycobacterium

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The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

Köksal

Kalın

Gerni

et al. 2017

J Biochem Mol Toxicol

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In this study, inhibition profiles of some natural products, which are digoxin, L-Dopa, dopamine, isoliquiritigenin, and 1,1,2,2-tetrakis(p-hydroxyphenyl)ethane (Tetrakis), were investigated against bovine lactoperoxidase (LPO) enzyme. Digoxin, L-Dopa, and dopamine are active ingredients of some drugs, which have important functions in our body, especially in cases of heart failure. Isoliquiritigenin and tetrakis are types of natural phenolic compounds, which play an important role in cancer prevention and treatment. LPO enzyme was purified from bovine milk using sepharose-4B-l-tyrosine sulfonamide affinity column chromatography. LPO is responsible for the nonimmune biological defense system and has antibacterial activity so selection of these active substances is important. The inhibition studies are performed with the ABTS substrate. Bovine LPO enzyme was effectively inhibited by phenolic molecules. K values of these natural products were found as 0.20 ± 0.09, 0.22 ± 0.17, 0.49 ± 0.11, 0.49 ± 0.27, and 1.20 ± 0.25 μM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition.

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Thiocyanate mediated antifungal and antibacterial property of goat milk lactoperoxidase

Cited by 55 publications

References 12 publications

Effect of lactoperoxidase on the antimicrobial effectiveness of the thiocyanate hydrogen peroxide combination in a quantitative suspension test

Effect of lactoperoxidase on the antimicrobial effectiveness of the thiocyanate hydrogen peroxide combination in a quantitative suspension test

Purification of Bovine Milk Lactoperoxidase and Investigation of Antibacterial Properties at Different Thiocyanate Mediated

The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

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