A new spectrophotometric assay for native β-lactoglobulin in raw and processed bovine milk

Lieske, B.; Konrad, G.; Faber, Wolfgang

doi:10.1016/s0958-6946(97)00072-1

Cited by 12 publications

(12 citation statements)

References 21 publications

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“…The second method to determine applied β-Lg is a spectrophotometric assay developed for native β-Lg in raw and processed milk [12]. The spectrophotometric analysis of β-Lg in the serum of the quarter milk sample amounted to 2.55 g·L -1 β-Lg (SD 0.04), thus agreeing with the chromatographic findings.…”

Section: Investigations Of the Biophysical Properties Of Bsa In Raw Milksupporting

confidence: 62%

An improved analytical approach for the determination of bovine serum albumin in milk

Lieske

Jantz²,

Finke³

2005

Lait

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-The content of bovine serum albumin (BSA) in milk is considered as a marker of the mammary gland health of the cow. Based on its physico-chemical properties, BSA tends to form aggregates hindering its exact determination with the previously known colorimetric bromcresol green dye (BCG) procedure. The BCG method was improved by adjusting the milk salt buffer system for the exact determination of BSA in milk. In a parallel approach, size-exclusion chromatography was applied. It was found that the analytical availability of BSA in milk samples was best when milk samples were directly analyzed with BCG without sample treatments such as precipitation and filtration. Spiked milk samples showed a recovery of 98.8% (+/-1.5%) with the improved method. The revised BCG method was fast and reliable in comparison with size-exclusion chromatography, allowing an exact determination of BSA in milk. Based on the spectrometric and chromatographic results it was concluded that the partial oligomerization of BSA occurring in milk depends on different factors: pH, ionic strength, concentration of BSA, actual immunological status and substances affiliated to it. The improved BCG method could be effectively used for the control of the mammary gland health status of cows.bovine serum albumin / bromcresol green dye method / udder's health status Résumé -Une approche analytique améliorée pour la détermination de la sérum-albumine dans le lait de vache. La teneur du lait en sérum-albumine (BSA) est considérée comme un indice de la santé de la glande mammaire de la vache. En raison de ses propriétés physicochimiques, la BSA a tendance à s'agréger, ce qui en empêche la détermination précise avec la méthode colorimé-trique au vert de bromocrésol (BCG) actuellement connue. La méthode au BCG a été améliorée en ajustant le système tampon salin du lait en vue de la détermination exacte de la BSA dans le lait. Parallèlement, on a appliqué la chromatographie d'exclusion. La mise en évidence analytique de la BSA dans l'échantillon de lait était meilleure quand on analysait les échantillons de lait directement avec la procédure au BCG sans les avoir préalablement traités par des méthodes comme la précipi-tation et la filtration. Les échantillons de lait surchargés ont présenté un taux de récupération de 98,8 % (+/-1,5 %) avec la méthode améliorée. La méthode au BCG améliorée s'est montrée rapide et fiable par rapport à la chromatographie d'exclusion et a permis la détermination exacte de la BSA dans le lait. On a pu conclure, sur la base des résultats spectrométriques et chromatographiques obtenus, que l'oligomérisation partielle de la BSA qui se produit dans le lait dépend de plusieurs facteurs : le pH, la force ionique, la concentration de la BSA, le statut immunologique effectif et la présence des substances qui y sont liées. La méthode au BCG améliorée pourrait donner de bons résultats dans la surveillance du statut sanitaire des glandes mammaires de la vache. sérum-albumine bovine / méthode au vert de bromocrésol / statut sanitaire de...

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Section: Investigations Of the Biophysical Properties Of Bsa In Raw Milksupporting

confidence: 62%

An improved analytical approach for the determination of bovine serum albumin in milk

Lieske

Jantz²,

Finke³

2005

Lait

Self Cite

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“…Chemical composition of whey used in this study was in accordance with previous studies (Lieske et al, 1997;Tunçtürk, Andiç, & Ocak, 2010). pH of whey was 5.51 ±0.11 and β-Lg content was 0.38 ±0.04 g/L.…”

Section: Resultssupporting

confidence: 85%

“…Physicochemical properties of whey which are acidity (SH, pH), fat, protein, dry matter contents and β-Lg contents were determined (Lieske, Konrad, & Faber, 1997). Before the isolation process of β-Lg from whey, all whey samples centrifuged at 15333 x g, 4ºC for 15 min as a pretreatment procedure to remove fat and particulates (Lozano, Giraldo, & Romero, 2008).…”

Section: Physicochemical Analysismentioning

confidence: 99%

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Comparison of Different Methods for Beta Lactoglobulin Isolation

Özer¹,

Öner²

2018

Food Health

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Abstract:The aim of this study was to introduce a simple, high efficient and less expensive method for isolation of β-Lg from whey. Anion exchange chromatography, pepsin enzyme treatment and ultrafiltration tecniques were preferred for isolation process to compare differences. In addition to, centrifuge ultrafiltration techniques were using for the first time for isolation of β-Lg from whey. Physicochemical analysis of whey samples indicated that protein and β-Lg content in whey samples changed from 0.07 to 0.8% and 0.24 to 0.29 g/L, respectively. Treatment with the use of pepsin enzyme, anion exchanges chromatography and ultrafiltration techniques, resulted to β-Lg of 1.43, 6.56 and 43.59 folds respectively. Our results showed that ultrafiltration techniques are rapid and efficient that allows high protein yield and has advantages over other methods since it preserves the native structure of β-Lg. Additionally, when the enzymatic hydrolysis was used together with ultrafiltration technique, it was found efficient and pure than the enzymatic hydrolysis together with dialyse membrane. Also this study concluded that pepsin enzyme treatment and anion exchange chromatography are economic methods but they are not efficient enough and very time consuming. However isolation efficiency can be increased the use of isolation methods together.

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“…As compared to other references that mention the concentration of b-LG in raw milk [32,33], the concentrations that we have determined are lower. Now, it is well known that b-LG is highly sensitive to temperature [34]. Indeed, in the latter work, it has for example been shown that the native concentration of b-LG decreases from 3.5 to less than 0.5 mg/mL after 90 s at 957C.…”

Section: Quantification Of â-Lg In Milkmentioning

confidence: 78%

Capillary electrophoresis immunoassay using magnetic beads

Chen¹,

Busnel²,

Gassner³

et al. 2008

Electrophoresis

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Protein A-coated magnetic beads (0.3 mm) have been trapped in a small portion of a neutrally coated capillary (50 mm id). Anti-b-lactoglobulin (b-LG) antibodies have then been immobilized on the beads through strong affinity with protein A to subsequently capture b-LG from model or real samples. Once the immunocomplexes formed at physiological pH, a discontinuous buffer system has been used to release the partners and preconcentrate them by transient ITP. The antigens and antibodies have finally been separated by CZE and detected by UV absorbance. An LOQ of 55 nM has been achieved. This methodology has been applied to quantify native b-LG in pasteurized and ultra-high-temperature-treated bovine milk. All the described procedures, including immunosorbent preparation, sample extraction, cleanup, preconcentration, and separation are completely automated on a commercial CE instrument. As this CE immunoassay method is simple, rapid, selective, and sensitive, it should be a practical and attractive technology for the analysis of complicated biological samples.

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A new spectrophotometric assay for native β-lactoglobulin in raw and processed bovine milk

Cited by 12 publications

References 21 publications

An improved analytical approach for the determination of bovine serum albumin in milk

An improved analytical approach for the determination of bovine serum albumin in milk

Comparison of Different Methods for Beta Lactoglobulin Isolation

Capillary electrophoresis immunoassay using magnetic beads

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