Prevalence and stability of lysozyme in cheese

Schneider, Nadine; Werkmeister, K.; Becker, Cord‐Michael; Pischetsrieder, Monika

doi:10.1016/j.foodchem.2011.03.010

Cited by 38 publications

(25 citation statements)

References 17 publications

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“…In the wine industry, lysozyme partially replaces sulfites and is added at doses of 250-500 mg/L to inhibit malolactic fermentation and to stabilize the wine afterwards [20,21]. Residual levels of 0.06-327 mg/L were found in lysozyme-treated wines [22,23], while in commercial cheeses, concentrations of 30.8-386.2 mg/kg were found to be present [24]. Lysozyme has also been used as an antibacterial agent during beer production [25], to extend the shelf-life of meat [26] and shrimp [27], as an alternative to antibiotics [28,29] in veterinary medicine or as anti-inflammatory drug in the treatment of wounds and infections [4,30].…”

Section: Properties Of Lysozyme and Its Importance For Daily Lifementioning

confidence: 99%

Aptamer-Based Electrochemical Sensing of Lysozyme

Vasilescu

Wang

et al. 2016

Chemosensors

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Protein analysis and quantification are required daily by thousands of laboratories worldwide for activities ranging from protein characterization to clinical diagnostics. Multiple factors have to be considered when selecting the best detection and quantification assay, including the amount of protein available, its concentration, the presence of interfering molecules, as well as costs and rapidity. This is also the case for lysozyme, a 14.3-kDa protein ubiquitously present in many organisms, that has been identified with a variety of functions: antibacterial activity, a biomarker of several serious medical conditions, a potential allergen in foods or a model of amyloid-type protein aggregation. Since the design of the first lysozyme aptamer in 2001, lysozyme became one of the most intensively-investigated biological target analytes for the design of novel biosensing concepts, particularly with regards to electrochemical aptasensors. In this review, we discuss the state of the art of aptamer-based electrochemical sensing of lysozyme, with emphasis on sensing in serum and real samples.

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Section: Properties Of Lysozyme and Its Importance For Daily Lifementioning

confidence: 99%

Aptamer-Based Electrochemical Sensing of Lysozyme

Vasilescu

Wang

et al. 2016

Chemosensors

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“…Despite EWL represents only 3%-4% of the egg white dry weight or about 2500-3000 ppm fresh-weight bases (Liburdi et al, 2014;Stadelman & Coterril, 1984), it is being widely used mainly in food industry due to its antibacterial properties (Tirelli & De Noni, 2007;Benkerroum, 2008;Schneider et al, 2011). It is usually added directly into food products (Liburdi et al, 2005) including cheese (Davidson, 2001), vegetable, seafood, pasta, and salads (Davidson, 2001).…”

Section: Introductionmentioning

confidence: 99%

Purification of Egg White Lysozyme from Indonesian Kampung Chicken and Ducks

Wulandari

Fardiaz²,

Budiman³

et al. 2015

Med Pet

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Egg white lysozyme (EWL) has considerably a wide functional protein exhibiting antibacterial activity mainly against Gram-positive bacteria. The EWL is widely applied in food industry and is considerably safe. Despite its high potency, EWL of Indonesian poultry has never been studied and exploited. This study was aimed to purify EWL from two Indonesian poultry: kampung chicken and Cihateup duck, and compared to egg of commercial laying hens. The eggs in this study were obtained from field laboratory of Faculty of Animal Science, Bogor Agricultural University (IPB) and classified in AA quality based on the interior quality. First attempt to purify the EWL was performed by using ethanol precipitation yielding purified EWL which was still contaminated by other proteins, hence designated as partially purified EWL. Final concentrations of partially purified EWL of kampung chicken, commercial laying hens, and Cihateup duck were about 5800, 5400, and 5500 μg/mL, respectively. To confirm whether the use of ethanol in the purification affecting EWL antibacterial activities, the activities were examined against Staphylococcus aureus. It demonstrated that the partially purified EWL exhibited ability to inhibit S. aureus at 6 and 26 h suggesting that the method was feasible as it did not interfere EWL antibacterial activities. Yet, based on SDS-Page, purity was the issue in ethanol precipitation method. Further attempt using ion exchange chromatography at pH 10 successfully purified lysozyme as indicated by a single band corresponding to lysozyme size (~14 kD) free from bands of other proteins. Altogether, a single step of ion exchange chromatography is sufficient and promising to isolate EWL from Indonesian poultry for various industrial purposes.Key words: Indonesian poultry, lysozyme, egg, kampung chicken, Cihateup duck ABSTRAK Lisozim putih telur memiliki fungsi yang luas, salah satunya adalah memiliki aktivitas sebagai antibakteri terutama terhadap bakteri Gram positif. Lisozim dari putih telur �uga banyak diapli-. Lisozim dari putih telur �uga banyak diaplikasikan di industri pangan dan dinyatakan aman untuk pangan. Sampai saat ini lisozim dari putih telur yang berasal dari unggas lokal (Indonesia) belum dipela�ari dan dikembangkan. Tu�uan penelitian ini adalah melakukan purifikasi putih telur dari telur unggas lokal, yaitu ayam kampung dan itik Cihateup dibandingkan dengan telur ayam ras. Sampel telur yang didapatkan dari Laboratorium Lapang Fakultas Peternakan diklasifikasikan pada grade AA berdasarkan kualitas interior. Tahap pertama purifikasi lisozim putih telur dengan presipitasi etanol menghasilkan protein lain selain lisozim (purifikasi parsial). Konsentrasi lisozim putih telur hasil purifikasi parsial telur ayam kampung, ayam ras dan itik Cihateup masing-masing adalah 5800, 5400, dan 5500 ug/mL. Untuk melihat efek penggunaan etanol dalam proses purifikasi terhadap aktivitast antibakteri lisozim, kemampuan daya hambat lisozim terhadap Staphylococcus aureus telah dianalisis. Lisozim putih telur hasil pu...

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“…The dairy industry was one of the first to be interested in using these generally recognized as safe substances. In fact, nisin and lysozyme are currently used effectively in cheeses as an alternative to nitrates to prevent late blowing caused by Clostridium tyrobutyricum (8,38). Nisin is also used in various cheese and milk products to inhibit gram-positive pathogenic bacteria, including Clostridium botulinum, Listeria monocytogenes, and Staphylococcus aureus (13,31,35,37).…”

mentioning

confidence: 99%

Effects of Nisin and Lysozyme on Growth Inhibition and Biofilm Formation Capacity of Staphylococcus aureus Strains Isolated from Raw Milk and Cheese Samples

Sudağıdan

Yemenicioğlu

2012

Journal of Food Protection

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Effects of nisin and lysozyme on growth inhibition and biofilm formation capacity of 25 Staphylococcus aureus strains isolated from raw milk (13 strains) and cheese (12 strains) were studied. Nisin was tested at concentrations between 0.5 and 25 mg/ ml; the growth of all strains was inhibited at 25 mg/ml, but the resistances of strains showed a great variation at lower nisin concentrations. In contrast, lysozyme tested at concentrations up to 5.0 mg/ml showed no inhibition on the growth of strains. Nisin used at the growth inhibitory concentration prevented the biofilm formation of strains, but strains continued biofilm formation at subinhibitory nisin concentrations. Lysozyme did not affect the biofilm formation of 19 of the strains, but it caused a considerable activation in the biofilm formation capacity of six strains. Twelve of the strains contained both biofilm-related protease genes (sspA, sspB, and aur) and active proteases; eight of these strains were nisin resistant. These results suggest a potential risk of S. aureus growth and biofilm formation when lysozyme is used in the biopreservation of dairy products. Nisin can be used to control growth and biofilm formation of foodborne S. aureus, unless resistance against this biopreservative develops.

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Prevalence and stability of lysozyme in cheese

Cited by 38 publications

References 17 publications

Aptamer-Based Electrochemical Sensing of Lysozyme

Aptamer-Based Electrochemical Sensing of Lysozyme

Purification of Egg White Lysozyme from Indonesian Kampung Chicken and Ducks

Effects of Nisin and Lysozyme on Growth Inhibition and Biofilm Formation Capacity of Staphylococcus aureus Strains Isolated from Raw Milk and Cheese Samples

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