Separation and identification of hen egg protein isoforms using SDS–PAGE and 2D gel electrophoresis with MALDI-TOF mass spectrometry

Raikos, Vassilios; Hansen, Rasmus; Campbell, Lydia; Euston, Stephen R.

doi:10.1016/j.foodchem.2005.08.047

Cited by 67 publications

(52 citation statements)

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“…Raikos et al [1] identified a lysozyme and ovalbumin in the egg white with masses similar to those described in this work (respectively, 13-14 and 50-55 kDa). These bands, however, did not show SOD activity by use of zymography (at the level of error of the method).…”

Section: Discussionsupporting

confidence: 85%

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Changes in activity during storage and characteristics of superoxide dismutase from hen eggs (Gallus gallus domesticus)

Wawrzykowski

Kankofer

2011

Eur Food Res Technol

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Hen eggs are one of the most popular food stuffs. Moreover, they can be the source of not only nutrients but also factors of biological origin, which may be used for food preservation and food additives. The aim of the study was to determine and describe the activity of superoxide dismutase isoforms (SOD; EC 1.15.1.1) in hen eggs (Gallus gallus domesticus). Our electrophoretic studies confirmed the presence of SOD isoenzyme bands with molecular weight of 14-15 and 50-70 kDa in egg yolk. By contrast, in egg white, we confirmed the presence of a protein with molecular weight of 13-14 and 50-55 kDa. Zymografic pattern confirmed the activity of SOD isoforms of the enzyme present in the egg yolk; however, it did not confirm enzyme activity in egg white (at the level of error of the used method). Study has also shown SOD activity during storage at 4°C for 9 days in egg yolk and egg white. In start time, SOD activity in egg yolk is clearly different from a small activity in the protein (respectively, 90.5 ± 22.2 and 7.9 ± 3.9 U g -1 ). It did not change during 6 days storage but between 6th and 9th day, it decreased significantly in egg yolk while remained low but unchanged in egg white. Present study confirmed the presence of SOD and its activity in hen egg yolk.

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Section: Discussionsupporting

confidence: 85%

“…They can be consumed unprocessed, processed, or as components of other food products [1]. They provide with high-quality nutritive proteins.…”

Section: Introductionmentioning

confidence: 99%

Changes in activity during storage and characteristics of superoxide dismutase from hen eggs (Gallus gallus domesticus)

Wawrzykowski

Kankofer

2011

Eur Food Res Technol

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“…1,2) Even though the amounts of both proteins in EW were sufficient to be detected, there is no report about the presence of dBPS 1 and dBPS 2 . [8][9][10] This may be due to the extremely low molecular masses of dBPS 1 and dBPS 2 . This group of small basic proteins, consisting of dBPS 1 , dBPS 2 , cygnin, meleagrin, and ''similar to meleagrin,'' showed close phylogenetic relationships to each other.…”

Section: Discussionmentioning

confidence: 99%

“…5,6) To date, many minor proteins have not been identified. [7][8][9][10] Among the referenced proteins in avian EW, most are acidic proteins, having pI < 7, while only two are identified as basic proteins, proteins that have pI > 7, lysozyme (pI ¼ 10:7) and avidin (pI ¼ 10). 1,2) Both proteins have been sequenced and are well characterized.…”

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confidence: 99%

Structural and Physicochemical Characteristics of Novel Basic Proteins Isolated from Duck Egg White

Naknukool

Hayakawa

Sun

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Novel basic proteins, duck basic protein small 1 (dBPS 1 ) and 2 (dBPS 2 ), were isolated from duck egg white by cation-exchange and gel filtration chromatography. Protein sequence analyses indicated that they possessed 39 amino acid residues with three disulfide bonds. The amino acid sequence of dBPS 1 showed 45% identity with dBPS 2 . The amino acid sequence of dBPS 2 was the same as cygnin, a small protein from black swan, and strongly homologous with meleagrin from turkey and chicken. Phylogenic relationships implied that dBPS 1 and dBPS 2 share a common ancestry with cygnin and meleagrin. Based on MALDI-TOF mass spectra, the molecular masses of dBPS 1 and dBPS 2 were 4,373, and the 4,486 Da. pI of dBPS 1 and dBPS 2 elucidated by isoelectric focusing were 9.35 and 9.44. FT-IR spectra classified these proteins as ( ) proteins. Both dBPS 1 and dBPS 2 , possessed high heat stability, Td 101.2 and 98.3 C. Indirect ELISA results showed that the dBPS 1 /dBPS 2 -related proteins were distributed in the oviduct and gallbladder.

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“…Bands 4, 6, 9, 13, 14 and 18, of (142-146), (105-107), (79-81), (43-44), (40-41) and (16-17) kDa, respectively, stand out for their greater intensity. Band 4 (142-146 kDa) would be LDL apoproteins (low density lipoproteins in plasma) according to Raikos et al (Raikos et al, 2006, Jolivet et el., 2006; and band 6 (105-107 kDa) would be HDL apoproteins (high density lipoproteins) according to Guilmineau et al (2005) or even -livetin (104 kDa). The ovotransferrin or conalbumin (band 9) is identified by estimated molecular weight (79-81 kDa) and because it is the second most accentuated band, fitting its relative proportion in egg white (13%) (Belitz and Grosch, 1997).…”

Section: Sds-pagementioning

confidence: 99%

Impacto De Nuevas Tecnologías De Conservación Sobre La Estructura Y Los Principales Componentes Químicos De Alimentos Fluidos

Molés¹

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AGRADECIMIENTOSQuisiera agradecer este trabajo a todas aquellas personas que de alguna manera han contribuido a que mi mayor pesadilla se convierta en un sueño hecho realidad:En especial a ti Isa, porque para mí has sido mucho más que una directora de tesis. Sabes que sin ti, yo no hubiera podido. Gracias, de verdad, por confiar en mí y ayudarme a seguir adelante.A Isabel, por darme la oportunidad de realizar esta tesis. Por todo su esfuerzo y dedicación en este trabajo y por el bien del grupo en general. Porque siempre estará con nosotros. Y porque nunca olvidaré todos los momentos que compartimos y sus sabios consejos.A toda la gente del Lab 13 (Empar, Amparo, Ana, Virginia, Laura, Juanvi, José, Luis, María y Julia) por su ayuda constante y tiempo dedicado en el laboratorio, por los buenos momentos compartidos y sobre todo por su amistad.A mis padres, porque a ellos se lo debo todo. A mi padre, por su gran apoyo y ayuda y por la confianza depositada en mí. A mi madre, por su incondicional cariño y compresión.A mis hermanos, por estar siempre ahí, dispuestos a contar conmigo y a echarme una mano siempre que la necesito.A mi hermana, porque a pesar de la distancia, siempre está a mi lado para escucharme y darme buenos consejos.A mi abuela, por preocuparse por mí a lo largo de tantos años y porque sé que siempre estará ahí para cuidar de mí.A mis sobrinas, por contagiarme con su alegría e ilusión en la vida.A Bubu, por sacarme a pasear cada día y regalarme su compañía.Y a ti Jesús, por estar siempre a mi lado y compartir tantos sueños juntos.Por último, agradecer a todos los organismos que han contribuido a que la realización de esta tesis doctoral haya sido posible:A la Comisión Europea por la financiación del proyecto "Innovative NonThermal Processing Technologies to Improve the Quality and Safety of Ready-toEat (RTE) Meals (FP6-2004-FOOD-23140 HIGHQ RTE)" en el cual se enmarca el presente trabajo.Al Departamento de Tecnología de Alimentos de la Universidad Politécnica de Valencia, por formarme durante estos años y ofrecerme sus instalaciones para la realización de esta tesis.Al Swedish Institute for Food and Biotechnology y a la Università di Bologna, por proporcionar las muestras analizadas en este trabajo.Al Servicio de Microscopía Electrónica de la Universidad Politécnica de Valencia, y en especial a Manolo, José Luis y Merche, por su ayuda.Al Ministerio de Educación y Ciencia (MEC) por concederme una beca, dentro del Programa de Formación del Profesorado Universitario (FPU), para la realización de esta tesis. RESUMENLa aplicación de nuevas tecnologías en el ámbito de la conservación de alimentos pretende dar respuesta al incremento de la demanda, por parte de los consumidores, de alimentos más parecidos a los frescos o naturales, más nutritivos y de fácil y rápida preparación (ready-to-eat meals). Las tecnologías más estudiadas en la actualidad se basan en el empleo de sistemas de destrucción o inactivación bacteriana sin necesidad de emplear un tratamiento térmico intenso. Se pretende así reducir los cam...

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Separation and identification of hen egg protein isoforms using SDS–PAGE and 2D gel electrophoresis with MALDI-TOF mass spectrometry

Cited by 67 publications

References 38 publications

Changes in activity during storage and characteristics of superoxide dismutase from hen eggs (Gallus gallus domesticus)

Changes in activity during storage and characteristics of superoxide dismutase from hen eggs (Gallus gallus domesticus)

Structural and Physicochemical Characteristics of Novel Basic Proteins Isolated from Duck Egg White

Impacto De Nuevas Tecnologías De Conservación Sobre La Estructura Y Los Principales Componentes Químicos De Alimentos Fluidos

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