Electrophoretic analisys to detect and quantify additional whey in milk and dairy beverages

Souza, Elizabeth Maria Talá de; Arruda, Sandra Fernandes; Brandão, Patrícia Oliveira; Siqueira, Egle Machado de Almeida

doi:10.1590/s0101-20612000000300007

Cited by 20 publications

(13 citation statements)

References 7 publications

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“…A eletroforese é útil para detectar e quantificar a presença de ingredientes estranhos à composição de diversos produtos (ABDEL-AZIZ et al, 1997;SOUZA et al, 2000). SDS-PAGE (eletroforese em gel de poliacrilamida na presença de dodecil-sulfato de sódio) também é utilizada para avaliar a degradação e a oxidação proteica e para avaliar a cura de produtos específicos, como presuntos de designação de origem controlada e, ainda, durante a aplicação de tratamento térmico (LARREA et al, 2006;XIA et al, 2009).…”

Section: Eletroforese De Proteínasunclassified

Controle da utilização de ingredientes não cárneos para injeção e marinação de carnes

2010

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Section: Eletroforese De Proteínasunclassified

Controle da utilização de ingredientes não cárneos para injeção e marinação de carnes

2010

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“…Samples were solubilized with 8M urea before loading onto the gel. Denaturation by 8M urea disrupted the casein micelles into the constituent a, h, n, and g-casein molecules in the region of 25 to 35 kDa (Souza et al, 2000).…”

Section: Sds-page Analysismentioning

confidence: 99%

“…To obtain approximately similar concentrations of whey proteins in the various samples, 100 AL of TGM and 500 AL of MF permeate were mixed with 900 AL of 8M urea (Souza et al, 2000). The casein standard was mixed with deionized water at 4 g/L concentration to form a suspension to mimic milk.…”

Section: Sds-page Analysismentioning

confidence: 99%

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Optimized recovery of monoclonal antibodies from transgenic goat milk by microfiltration

Baruah

Belfort

2004

Biotech & Bioengineering

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The Predictive Aggregate Transport Model for microfiltration is used in combination with optimum fluid mechanics and electrostatics to maximize recovery of a heterologous immunoglobulin (IgG) from transgenic goat milk. The optimization algorithm involved varying pH (6.8 -9), transmembrane pressure (2 -4.5 psi), milk feed concentration (1 -2X), membrane module type (linear vs. helical design), and axial velocity (Reynolds number: 830-1170). Operation in the pressure-dependent regime at low uniform transmembrane pressures (c2 psi) using permeate circulation in co-flow, at the pI of the protein (9 in this case) was used to increase IgG recovery from less than 1% to over 95%. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and attenuated total reflection Fourier transform infrared spectroscopy of the microfiltration permeate samples confirmed that all the fat globules and most of the casein micelles were retained in the MF membrane whereas a large amount of the target IgG was transported through the membrane. Transmembrane pressure and hence permeation flux was kept low (c15 lmh) to maximize IgG membrane transport and thus recovery, due to a sparse deposit on the membrane which facilitated high solute transport. Next, an analytical method was used to optimize the diafiltration process using the aggregate transport model, experimental target protein sieving coefficients and permeation flux . The methodology reported here should be generalizable to the recovery of target proteins found in other complex suspensions of biological origin using the microfiltration process. B 2004 Wiley Periodicals, Inc.

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“…Several methodologies have been used to detect and study the structure and properties of GMP (LIESKE; KONRAD, 1996;OZIMEK, 2000b;DE SOUSA et al, 2000;MIRALLES et al, 2001;BENITEZ;NOA 2001;ROSSANO;D'ELIA;RICCIO, 2001;WANG;LUCCY, 2003;KIM et al, 2005). However, recently used isolation techniques for GMP production are based on chromatography, electrophoresis, and ultrafltration of caseinate/casein as peptide source (SILVA-HERNÁNDEZ et al, 2005;IKAWA;OZIMEK, 2007;SODRE DA SILVA et al, 2007;KREUS;KULOZIK, 2009;SUSIL;BRAD, 2010).…”

Section: Sodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis (Smentioning

confidence: 99%

Isolation and recovery of glycomacropeptide from milk whey by means of thermal treatment

Rojas

Torres

2013

Food Sci. Technol

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During enzymatic process of cheese manufacturing, rennin cleaves κ-casein releasing two fractions: para-κ-casein and glycomacropeptide (GMP), which remains soluble in milk whey. GMP is a peptide with structural particularities such as chain carbohydrates linked to specific threonine residues, to which a great variety of biological activities is attributed. Worldwide cheese production has increased generating high volumes of milk whey that could be efficiently used as an alternative source of high quality peptide or protein in foodstuff formulations. In order to evaluate isolation and recovery on whey GMP by means of thermal treatment (90 °C), 18 samples (2 L each) of sweet whey, resuspended commercial whey (positive control) and acid whey (negative control) were processed. Indirect presence of GMP was verified using chemical tests and PAGE-SDS 15%. At 90 °C treated sweet whey, 14, 20 and 41 kDa bands were observed. These bands may correspond to olygomers of GMP. Peptide recovery showed an average of 1.5 g/L (34.08%). The results indicate that industrial scale GMP production is feasible; however, further research must be carried out for the biological and nutritional evaluation of GMP's incorporation to foodstuff as a supplement.

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Electrophoretic analisys to detect and quantify additional whey in milk and dairy beverages

Cited by 20 publications

References 7 publications

Controle da utilização de ingredientes não cárneos para injeção e marinação de carnes

Controle da utilização de ingredientes não cárneos para injeção e marinação de carnes

Optimized recovery of monoclonal antibodies from transgenic goat milk by microfiltration

Isolation and recovery of glycomacropeptide from milk whey by means of thermal treatment

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